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Q3TIA9 Entry name Protein names Length Mass Features Intramembrane Transmembrane Topological domain Pathway Function [CC] Post-translational modification Subcellular location [CC] Subunit structure [CC] Domain [CC] Tissue specificity Involvement in disease A0A087WNV1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A087WNV1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A087WRY3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0N4SVP8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0N4SVU8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0R4J0G0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0R4J0T5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0R4J0W6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0R4J0W6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0R4J1E8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A0R4J2B2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0A1B0GT81 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A0PJK7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A2AFI4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A2AFI9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A2AQU8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A2ASX2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A2AUK7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A2RST1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA A6H6H4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA B0G0Y1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA B1AVZ0 UPP_MOUSE Uracil phosphoribosyltransferase homolog 310 34,278 Binding site (5); Chain (1); Modified residue (1); Nucleotide binding (1); Region (2) NA NA NA NA NA NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. NA NA NA NA B1AZI6 THOC2_MOUSE THO complex subunit 2 (Tho2) 1594 182,773 Chain (1); Coiled coil (2); Modified residue (8); Motif (1) NA NA NA NA FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Plays a role for proper neuronal development. {ECO:0000250|UniProtKB:Q8NI27}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000250}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Interacts with THOC1, POLDIP3 and ZC3H11A (By similarity). {ECO:0000250}. NA TISSUE SPECIFICITY: Expressed in the hippocampus and the cortical neurons. {ECO:0000269|PubMed:26166480}. NA B1B1A8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA B2RXT3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA B7FAV1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA D3YVS7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA D3YZ06 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA D3Z132 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA D3Z1Z8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA D3Z637 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9PY03 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9Q1Y3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9Q5D6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9Q616 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9Q616 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9QN37 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA E9QNN1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA F6VQH5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA F6XJA1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA F6ZV59 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA F8WJG3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA G3X920 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA G5E866 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA G5E8V9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA G5E924 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA G8JL74 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA H7BX95 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA K3W4R2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA L7N451 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA O08532 CA2D1_MOUSE Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1] 1103 124,630 Alternative sequence (3); Chain (3); Disulfide bond (1); Domain (2); Glycosylation (8); Metal binding (3); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 1074 1094 Helical. {ECO:0000255}. TOPO_DOM 25 1073 Extracellular. {ECO:0000255}.; TOPO_DOM 1095 1103 Cytoplasmic. {ECO:0000255}. NA FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250}. PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that are disulfide-linked. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Dimer formed of alpha-2-1 and delta-1 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (By similarity). {ECO:0000250}. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2A is expressed in skeletal muscle and aorta. Isoform 2B is expressed in brain. Isoform 2C is expressed in heart. Isoform 2D is expressed in heart and smooth muscle. Isoform 2E is expressed in smooth muscle. All five isoforms are expressed in the cardiovascular system. NA O08583 THOC4_MOUSE THO complex subunit 4 (Tho4) (Ally of AML-1 and LEF-1) (Aly/REF export factor) (REF1-I) (RNA and export factor-binding protein 1) (Transcriptional coactivator Aly/REF) 255 26,940 Alternative sequence (1); Beta strand (4); Chain (1); Compositional bias (1); Domain (1); Helix (2); Initiator methionine (1); Modified residue (20); Region (1) NA NA NA NA FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability.; FUNCTION: Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. PTM: Arg-50 and Arg-203 are dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding (By similarity). {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9119228}. Nucleus speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000269|PubMed:9119228}. Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q86V81}. SUBUNIT: Homomultimer (By similarity). Is part of several complexes involved in mRNA processing and export (By similarity). Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have a dynamic structure involving ATP-dependent remodeling; in the complex interacts (via C-terminus) directly with DDX39B and interacts directly with THOC1 and THOC2 (By similarity). Found in mRNA splicing-dependent exon junction complexes (EJC) (By similarity). Identified in the spliceosome C complex (By similarity). Found in a mRNP complex with UPF3A and UPF3B (By similarity). Interacts with RBM8A, NCBP1, THOC5, LEF1, RUNX1, EIF4A3, RNPS1, SRRM1, IWS1 and EXOSC1 (By similarity). Interacts with RBM15B. Interacts with NXF1; the interaction is direct (PubMed:10786854). {ECO:0000250|UniProtKB:Q86V81, ECO:0000269|PubMed:10786854}. NA TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:9119228}. NA O08692 NGP_MOUSE Neutrophilic granule protein (NGP) (Cystatin-like protein) (Myeloid bactenecin protein) (Myeloid secondary granule protein) 167 19,332 Chain (1); Sequence conflict (1); Signal peptide (1) NA NA NA NA FUNCTION: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a role as a negative regulator of tumor vascular development, cell invasion and metastasis. {ECO:0000269|PubMed:21518852}. NA SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21518852}. Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in cytoplasmic granules of neutrophilic precursors (PubMed:8749713). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}. SUBUNIT: Monomer. Homodimer; disulfide-linked. {ECO:0000269|PubMed:21518852}. NA TISSUE SPECIFICITY: Expressed in myeloid bone marrow cells. Expressed in neutrophilic precursors (at protein level) (PubMed:8749713). Expressed in myeloid bone marrow cells (PubMed:21518852). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}. NA O88512 AP1G2_MOUSE AP-1 complex subunit gamma-like 2 (Gamma2-adaptin) (G2ad) 791 87,863 Chain (1); Domain (1); Sequence conflict (1) NA NA NA NA FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000250|UniProtKB:O75843}. NA SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}; Cytoplasmic side {ECO:0000250|UniProtKB:O75843}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}. Endosome membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}. Note=Mainly localized to perinuclear vesicular structures. Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments. Colocalizes with HBV major surface antigen L to cis-Golgi-like structures. {ECO:0000250|UniProtKB:O75843}. SUBUNIT: Probably interacts with AP1S1/Sigma1A-adaptin AP1S2/Sigma1B-adaptin. Probably does not interact with APB1. Interacts with HBV major surface antigen L. Interacts with HBV core protein C in a ubiquitin-dependent manner. Binds ubiquitin. {ECO:0000250|UniProtKB:O75843}. NA TISSUE SPECIFICITY: Widely expressed. NA O88569 ROA2_MOUSE Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) 353 37,403 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (36); Motif (1); Region (2); Sequence conflict (3) NA NA NA NA FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}. PTM: Sumoylated in exosomes, promoting miRNAs-binding. {ECO:0000250|UniProtKB:P22626}.; PTM: Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methylation affects subcellular location and promotes nuclear localization (By similarity). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P22626}. Cytoplasmic granule {ECO:0000250|UniProtKB:P22626}. Secreted, exosome {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes follwong sumoylation. {ECO:0000250|UniProtKB:P22626}. SUBUNIT: Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with CKAP5. {ECO:0000250|UniProtKB:P22626}. DOMAIN: The low complexity (LC) region is intrinsically disordered. When incubated at high concentration, it is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidences suggest that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels. {ECO:0000250|UniProtKB:P22626}. NA NA P01592 IGJ_MOUSE Immunoglobulin J chain 159 18,014 Chain (1); Disulfide bond (5); Glycosylation (1); Sequence conflict (4); Signal peptide (1) NA NA NA NA FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component. {ECO:0000269|PubMed:1517233}. NA SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1517233}. NA NA NA NA P02798 MT2_MOUSE Metallothionein-2 (MT-2) (Metallothionein-II) (MT-II) 61 6,115 Chain (1); Metal binding (20); Modified residue (2); Region (2); Sequence conflict (1) NA NA NA NA FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. NA NA NA DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. NA NA P02802 MT1_MOUSE Metallothionein-1 (MT-1) (Metallothionein-I) (MT-I) 61 6,018 Beta strand (5); Chain (1); Metal binding (20); Modified residue (1); Region (2); Sequence conflict (2) NA NA NA NA FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. NA NA NA DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. NA NA P11928 OAS1A_MOUSE 2'-5'-oligoadenylate synthase 1A ((2-5')oligo(A) synthase 1A) (2-5A synthase 1A) (EC 2.7.7.84) (p42 OAS) 367 42,429 Binding site (4); Chain (1); Metal binding (3); Region (2); Sequence conflict (8) NA NA NA NA FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}. Mitochondrion {ECO:0000250|UniProtKB:P00973}. Nucleus {ECO:0000250|UniProtKB:P00973}. Microsome {ECO:0000250|UniProtKB:P00973}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P00973}. Note=Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. {ECO:0000250|UniProtKB:P00973}. SUBUNIT: Monomer (By similarity). Homotetramer (By similarity). Interacts with OAS1D; the interaction inhibits OAS1A catalytic activity (PubMed:15899864). {ECO:0000250|UniProtKB:P00973, ECO:0000269|PubMed:15899864}. NA TISSUE SPECIFICITY: Expressed in oocytes and granulosa cells of ovary, in intestine, stomach, spleen and uterus (at protein level) (PubMed:15899864). Expressed at high levels in the digestive tract and lymphoid organs (PubMed:12396720). Expressed in ovary and spleen (PubMed:27663720). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:27663720}. NA P15392 CP2A4_MOUSE Cytochrome P450 2A4 (EC 1.14.14.1) (CYPIIA4) (Cytochrome P450-15-alpha) (Cytochrome P450-IIA3.1) (Testosterone 15-alpha-hydroxylase) 494 56,782 Chain (1); Metal binding (1); Modified residue (2); Sequence conflict (16) NA NA NA NA FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone. Also active in the 15-alpha-hydroxylation of progesterone and androstenedione. Little or no activity on corticosterone, pregnenolone, dehydroepiandrosterone, estradiol or estriol. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. NA NA TISSUE SPECIFICITY: Kidney and lung. Expressed in liver, with a strong circadian rhythmicity. Circadian expression is regulated by DBP. {ECO:0000269|PubMed:10490589}. NA P16045 LEG1_MOUSE Galectin-1 (Gal-1) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (S-Lac lectin 1) 135 14,866 Beta strand (11); Binding site (2); Chain (1); Domain (1); Frameshift (2); Initiator methionine (1); Modified residue (8); Region (2); Sequence conflict (3) NA NA NA NA FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:1986871}. NA SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Interacts with SUSD2. {ECO:0000250|UniProtKB:P09382}. NA NA NA P19639 GSTM3_MOUSE Glutathione S-transferase Mu 3 (EC 2.5.1.18) (GST class-mu 3) (Glutathione S-transferase GT9.3) 218 25,702 Chain (1); Cross-link (2); Domain (2); Erroneous initiation (1); Initiator methionine (1); Region (4) NA NA NA NA FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. NA SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. NA NA NA P35459 LY6D_MOUSE Lymphocyte antigen 6D (Ly-6D) (Thymocyte B-cell antigen) (ThB) 127 13,396 Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (1); Lipidation (1); Propeptide (1); Signal peptide (1) NA NA NA NA FUNCTION: May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification. {ECO:0000269|PubMed:19833765}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. NA NA TISSUE SPECIFICITY: Lymphoid cells lacking Ly6d, called ALP (all-lymphoid progenitor), retain full lymphoid potential and early thymic seeding activity, whereas cells containing Ly6d, called BLP (B-cell-biased lymphoid progenitor), up-regulate the B-cell specifying factors Ebf1 and Pax5 and behave essentially as B-cell progenitors (at protein level). Thymocytes and B-cells. {ECO:0000269|PubMed:19833765}. NA P57784 RU2A_MOUSE U2 small nuclear ribonucleoprotein A' (U2 snRNP A') 255 28,357 Chain (1); Cross-link (2); Domain (1); Modified residue (5); Repeat (4); Sequence conflict (2) NA NA NA NA FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA. {ECO:0000250|UniProtKB:P09661}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09661}. SUBUNIT: Identified in the spliceosome B complex. Identified in the spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B. Contributes to the binding of stem loop IV of U2 snRNA with SNRPB2. {ECO:0000250|UniProtKB:P09661}. NA NA NA P61327 MGN_MOUSE Protein mago nashi homolog 146 17,164 Chain (1); Modified residue (1) NA NA NA NA FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected in granule-like structures in the dendroplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with PYM1; the interaction is direct and dissociates the EJC from spliced mRNAs. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. NA NA NA P62627 DLRB1_MOUSE Dynein light chain roadblock-type 1 (Dynein light chain 2A, cytoplasmic) 96 10,990 Beta strand (5); Chain (1); Helix (2); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Turn (1) NA NA NA NA FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. NA SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1I1 and DYNC1I2. Self-associates. Interacts with DYNLRB2. Interacts with RAB6A; the interaction is direct. Interacts with RAB6B (GDP-bound) (By similarity). {ECO:0000250}. NA NA NA P63166 SUMO1_MOUSE Small ubiquitin-related modifier 1 (SUMO-1) (SMT3 homolog 3) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) 101 11,557 Chain (1); Cross-link (11); Domain (1); Initiator methionine (1); Modified residue (4); Propeptide (1); Site (1) NA NA NA NA FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:16990542}. PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250}.; PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:18681895}. SUBUNIT: Interacts with USP25 (via ts SIM domain) the interaction weakly sumoylates USP25. Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity). Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PRKN. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63165}. NA TISSUE SPECIFICITY: Ubiquitous. NA P70460 VASP_MOUSE Vasodilator-stimulated phosphoprotein (VASP) 375 39,667 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (12); Motif (1); Mutagenesis (4); Natural variant (1); Region (5); Repeat (2); Sequence conflict (3) NA NA NA NA FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10660044}. PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-153, the preferred site for PKG, Ser-235. In ADP-activated platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235. Phosphorylation at Ser-153 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-318 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235. {ECO:0000269|PubMed:10085070, ECO:0000269|PubMed:10882740, ECO:0000269|PubMed:12372613, ECO:0000269|PubMed:21945940}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10660044}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10660044}. Cell junction, focal adhesion {ECO:0000269|PubMed:10660044}. Cell junction, tight junction {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:10660044}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10660044}. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions (By similarity). In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer (By similarity). Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP. Interacts weakly with MEFV (By similarity). {ECO:0000250}. DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.; DOMAIN: The WH1 domain mediates interaction with XIRP1. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Lower levels in lung, ovary, placenta and fat. {ECO:0000269|PubMed:10069337}. NA Q00PI9 HNRL2_MOUSE Heterogeneous nuclear ribonucleoprotein U-like protein 2 (MLF1-associated nuclear protein) 745 84,940 Chain (1); Compositional bias (2); Domain (2); Modified residue (11); Sequence conflict (1) NA NA NA NA NA NA SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17008314}. SUBUNIT: Binds to MLF1 and retains it in the nucleus. {ECO:0000269|PubMed:17008314}. NA NA NA Q07797 LG3BP_MOUSE Galectin-3-binding protein (Cyp-C-associated protein) (CyCAP) (Lectin galactoside-binding soluble 3-binding protein) (Protein MAMA) 577 64,491 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (6); Sequence conflict (7); Signal peptide (1) NA NA NA NA FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells (By similarity). {ECO:0000250|UniProtKB:Q08380}. PTM: N-glycosylated. {ECO:0000269|PubMed:8341703}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08380}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8119883}. SUBUNIT: Homodimers and homomultimers. The multimers form ring-like structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID (By similarity). Interacts with PPIC (in vitro). The unglycosylated form interacts with PDE4DIP isoform 2/MMG8/SMYLE; this interaction may connect a pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly and acetylation (By similarity). {ECO:0000250|UniProtKB:Q08380, ECO:0000269|PubMed:8341703}. NA TISSUE SPECIFICITY: Detected in embryo, liver, spleen, kidney, lung, heart, intestine, thymus and lymph node. {ECO:0000269|PubMed:8119883, ECO:0000269|PubMed:8341703}. NA Q0VG47 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q148B1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q14AF6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q31094 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TAY9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TCL2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TD86 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TDI7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TDU5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TEP0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TFC0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TFP0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3THA6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3THE2 ML12B_MOUSE Myosin regulatory light chain 12B (Myosin regulatory light chain 2-B, smooth muscle isoform) (Myosin regulatory light chain 20 kDa) (MLC20) (Myosin regulatory light chain MRLC2) 172 19,779 Calcium binding (1); Chain (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (3) NA NA NA NA FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000250|UniProtKB:O14950}. PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000250|UniProtKB:O14950}. NA SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}. NA NA NA Q3THE2 ML12B_MOUSE Myosin regulatory light chain 12B (Myosin regulatory light chain 2-B, smooth muscle isoform) (Myosin regulatory light chain 20 kDa) (MLC20) (Myosin regulatory light chain MRLC2) 172 19,779 Calcium binding (1); Chain (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (3) NA NA NA NA FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000250|UniProtKB:O14950}. PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000250|UniProtKB:O14950}. NA SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}. NA NA NA Q3TKP3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TKP3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TRG2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TT92 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TU94 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TW96 UAP1L_MOUSE UDP-N-acetylhexosamine pyrophosphorylase-like protein 1 (EC 2.7.7.-) 507 56,614 Alternative sequence (1); Binding site (7); Chain (1); Erroneous initiation (1); Motif (2); Region (1); Sequence caution (1) NA NA NA NA NA NA NA NA NA NA NA Q3TWK8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3TWW8 SRSF6_MOUSE Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6) 339 39,025 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Modified residue (9); Sequence conflict (4) NA NA NA NA FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914}. Nucleus speckle {ECO:0000250|UniProtKB:Q13247}. SUBUNIT: Binds SREK1/SFRS12. Interacts with DYRK1A (By similarity). {ECO:0000250}. NA NA NA Q3TXV7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U054 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U263 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U3E7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U3F6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U3W2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U6P5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U6P5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3U741 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3UDY1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3UHJ0 AAK1_MOUSE AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) 959 103,346 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Modified residue (20); Nucleotide binding (1); Sequence conflict (3) NA NA NA NA FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity). {ECO:0000250}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with alpha-adaptin, AP-2, clathrin, NUMB and EPS15 isoform 2 (By similarity). Interacts with membrane-bound activated NOTCH1 but not with the inactive full-length form of NOTCH1. Preferentially interacts with monoubiquitinated activated NOTCH1 compared to the non-ubiquitinated form. {ECO:0000250, ECO:0000269|PubMed:21464124}. NA NA NA Q3UKD6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3UKJ6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3UKR1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3UNZ1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3UQA7 SELH_MOUSE Selenoprotein H (SelH) 116 12,974 Chain (1); Cross-link (1); Modified residue (1); Non-standard residue (1) NA NA NA NA FUNCTION: May be involved in a redox-related process. {ECO:0000305}. NA NA NA NA NA NA Q3UR53 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3V0K9 PLSI_MOUSE Plastin-1 630 70,408 Calcium binding (2); Chain (1); Domain (6); Modified residue (1); Region (2) NA NA NA NA FUNCTION: Actin-bundling protein in the absence of calcium. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. NA NA NA Q3V1S6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3V1Z5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q3V3U0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q499F3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4FJM5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4FJQ6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4FJR9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4FK54 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4KML7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4KML7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q4KMM5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q52KR6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q53YX2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q542D6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q542I8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q542Y0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q543B6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q543F3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q54AC6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q569X3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q569Z6 TR150_MOUSE Thyroid hormone receptor-associated protein 3 (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150) 951 108,178 Chain (1); Compositional bias (2); Cross-link (36); Initiator methionine (1); Modified residue (49); Nucleotide binding (1); Region (2) NA NA NA NA FUNCTION: Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y2W1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9Y2W1}. SUBUNIT: Associated with the large multiprotein complex TRAP (Mediator complex-like). Interacts with SFPQ; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an ESS1 exonic splicing silencer element-containing RNA. Interacts with NXF1. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes. Interacts with HELZ2 and PPARG. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q9Y2W1}. NA NA NA Q58DZ5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q58E59 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q58EU7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q58EU7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q5BL18 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q5HZH8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q5U5I3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q60749 KHDR1_MOUSE KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68) 443 48,371 Chain (1); Compositional bias (7); Cross-link (5); Domain (1); Modified residue (44); Mutagenesis (4); Region (3); Sequence conflict (6) NA NA NA NA FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species. RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (By similarity). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (PubMed:12478298, PubMed:22196734, PubMed:24469635). {ECO:0000250|UniProtKB:O75525, ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:22196734, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:9315629}. PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-receptor tyrosine kinase SRMS in an EGF-dependent manner (By similarity). Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion. {ECO:0000250|UniProtKB:Q07666, ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:7512695}.; PTM: Acetylated. Positively correlates with ability to bind RNA (By similarity). {ECO:0000250|UniProtKB:Q07666}.; PTM: Arginine methylation is required for nuclear localization. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 (By similarity). {ECO:0000250|UniProtKB:Q07666}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12496368}. Cytoplasm {ECO:0000250|UniProtKB:Q07666}. Membrane {ECO:0000269|PubMed:12496368}. Note=Predominantly located in the nucleus but also located partially in the cytoplasm. {ECO:0000250|UniProtKB:Q07666}. SUBUNIT: Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins (PubMed:9315629). Interacts with KHDRBS3/SLIM-2 and KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (PubMed:10077576, PubMed:24469635). Interacts with RASA1, FYN, GRB2, PLCG1, SRC, RBMY1A1, CBP, PRMT1 (PubMed:7799925, PubMed:7512695, PubMed:10077576, PubMed:10823932, PubMed:12496368, PubMed:12529443). Interacts with PTK6 (via SH3 and SH2 domains). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains). Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3 domain). Interacts with APC, HNRNPA1 (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of KHDRBS1 (By similarity). Interacts with ZBTB7A; negatively regulates KHDRBS1 splicing activity toward BCL2L1 (By similarity). {ECO:0000250|UniProtKB:Q07666, ECO:0000250|UniProtKB:Q91V33, ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:12529443, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:7799925, ECO:0000269|PubMed:9315629}. DOMAIN: The KH domain is required for binding to RNA. {ECO:0000269|PubMed:9315629}.; DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In adult cerebellum expressed in most neuronal cell populations, specifically in cerebellar granule cells of the internal granular layer, ROR(alpha)-positive Purkinje cells, internal granular layer and molecuar layer interneurons (at protein level). {ECO:0000269|PubMed:22196734}. NA Q61024 ASNS_MOUSE Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase) 561 64,283 Active site (1); Binding site (3); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (2); Sequence conflict (1); Site (1) NA NA NA Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1. NA NA NA NA NA NA NA Q61753 SERA_MOUSE D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (A10) 533 56,586 Active site (3); Binding site (4); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (5); Nucleotide binding (3); Sequence conflict (6) NA NA NA Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. {ECO:0000250|UniProtKB:O08651}. NA NA SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O08651}. NA NA NA Q62159 RHOC_MOUSE Rho-related GTP-binding protein RhoC (Silica-induced gene 61 protein) (SIG-61) 193 22,006 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) NA NA NA NA FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. {ECO:0000269|PubMed:20974804}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000250}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with RTKN (PubMed:8662891). Interacts with AKAP13. Interacts with DIAPH1 (By similarity). Interacts with PKN2 (PubMed:20974804). Interacts with ROCK1 and ROCK2. Interacts with ARHGDIA. Interacts with RIPOR1 (By similarity). {ECO:0000250|UniProtKB:P08134, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8662891}. NA NA NA Q62192 CD180_MOUSE CD180 antigen (Lymphocyte antigen 78) (Ly-78) (Radioprotective 105 kDa protein) (CD antigen CD180) 661 74,302 Beta strand (29); Chain (1); Domain (2); Glycosylation (10); Helix (17); Repeat (19); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) NA TRANSMEM 627 650 Helical. {ECO:0000255}. TOPO_DOM 21 626 Extracellular.; TOPO_DOM 651 661 Cytoplasmic. NA FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells. {ECO:0000269|PubMed:10880523}. NA SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers. {ECO:0000269|PubMed:21959264}. NA TISSUE SPECIFICITY: B-lymphocytes and spleen. Not detected in thymus, kidney, muscle, heart, brain or liver. NA Q62266 SPR1A_MOUSE Cornifin-A (Small proline-rich protein 1A) (SPR1 A) (SPR1A) 144 15,765 Chain (1); Region (1); Repeat (13) NA NA NA NA FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. May participate widely in the construction of cell envelopes in cornifying epithelia characterized by either increased thickness or a requirement for extreme flexibility. NA SUBCELLULAR LOCATION: Cytoplasm. NA NA TISSUE SPECIFICITY: Expressed in fetal periderm, hair follicles and in the thickened epidermis of the lip and footpad. Also present in the epithelia of various tissues such as the penis, vagina, forestomach, tongue and esophagus. {ECO:0000269|PubMed:8601731}. NA Q684Q6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q69ZD1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q69ZN7 MYOF_MOUSE Myoferlin (Fer-1-like protein 3) 2048 233,324 Alternative sequence (6); Chain (1); Compositional bias (5); Domain (5); Erroneous initiation (1); Frameshift (1); Modified residue (5); Mutagenesis (1); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) NA TRANSMEM 2013 2033 Helical. {ECO:0000255}. TOPO_DOM 1 2012 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2034 2048 Extracellular. {ECO:0000255}. NA FUNCTION: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:18502764}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures (By similarity). Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels. {ECO:0000250, ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}. SUBUNIT: Interacts with EHD1 (PubMed:21177873). Interacts with EHD2; the interaction is direct (PubMed:21177873). Interacts with DNM2 and KDR (PubMed:21177873). Interacts with RIPOR2 (By similarity). {ECO:0000250|UniProtKB:Q9NZM1, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:21177873}. DOMAIN: The C2 1 domain associates with lipid membranes in a calcium-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in myoblasts (at protein level). Expressed in endothelial cells. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}. NA Q6P1F5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q6P8Q0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q6PDL0 DC1L2_MOUSE Cytoplasmic dynein 1 light intermediate chain 2 (Dynein light intermediate chain 2, cytosolic) 492 54,218 Chain (1); Modified residue (7); Nucleotide binding (1); Sequence conflict (1) NA NA NA NA FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1 (By similarity). {ECO:0000250}. NA NA NA Q6PE01 SNR40_MOUSE U5 small nuclear ribonucleoprotein 40 kDa protein (U5 snRNP 40 kDa protein) (WD repeat-containing protein 57) 358 39,276 Chain (1); Cross-link (2); Frameshift (1); Modified residue (1); Repeat (7); Sequence conflict (2) NA NA NA NA FUNCTION: Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Associated with the spliceosome complex. Part of the U5 snRNP complex. Interacts with PRPF8. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By similarity). {ECO:0000250}. NA NA NA Q7TMX4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q7TPX2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q80UW7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q80V26 IMPA3_MOUSE Inositol monophosphatase 3 (IMP 3) (IMPase 3) (EC 3.1.3.25) (EC 3.1.3.7) (Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase) (Golgi-resident PAP phosphatase) (gPAPP) (Inositol monophosphatase domain-containing protein 1) (Inositol-1(or 4)-monophosphatase 3) (Myo-inositol monophosphatase A3) 356 38,616 Binding site (2); Chain (1); Glycosylation (1); Metal binding (6); Modified residue (1); Region (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 13 33 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 356 Lumenal. {ECO:0000255}. Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. FUNCTION: May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. {ECO:0000269|PubMed:18695242}. PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:18695242}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. NA NA NA NA Q80X54 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q80X95 RRAGA_MOUSE Ras-related GTP-binding protein A (Rag A) (RagA) 313 36,566 Chain (1); Cross-link (4); Erroneous initiation (1); Frameshift (1); Modified residue (1); Nucleotide binding (3) NA NA NA NA FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. {ECO:0000250|UniProtKB:Q7L523}. PTM: Ubiquitinated. 'Lys-68'-linked polyubiquitination of the GDP-bound inactive form of RRAGA at Lys-142, Lys-220, Lys-230 and Lys-244 by RNF152 is increased in response to amino acid starvation. Polyubiquitination promotes interaction with the GATOR1 complex. This does not affect RRAGA degradation. {ECO:0000250|UniProtKB:Q7L523}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Lysosome {ECO:0000250}. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state (By similarity). {ECO:0000250}. SUBUNIT: Can occur as a homodimer or as a heterodimer with RRAGC or RRAGD in a sequence-independent manner; heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGC, but not with RRAGB, interacts with RPTOR. The GTP-bound form of RRAGA interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGA and is negatively regulated by amino acids. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor. Interacts (inactive GDP-bound form) with RNF152; stimulated by amino acid starvation. Interacts (polyubiquitinated) with the GATOR1 complex; inactivates RRAGA. Interacts (polyubiquitinated) with TSC2 (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925). {ECO:0000250|UniProtKB:Q7L523, ECO:0000269|PubMed:25259925}. NA NA NA Q8BG07 PLD4_MOUSE Phospholipase D4 (PLD 4) (EC 3.1.4.4) (Choline phosphatase 4) (Phosphatidylcholine-hydrolyzing phospholipase D4) 503 56,154 Active site (6); Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Sequence conflict (7); Transmembrane (1) NA TRANSMEM 37 57 Helical. {ECO:0000255}. NA NA NA NA SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. NA NA NA NA Q8BHC4 DCAKD_MOUSE Dephospho-CoA kinase domain-containing protein 231 26,476 Chain (1); Domain (1); Nucleotide binding (1) NA NA NA NA NA NA NA NA NA NA NA Q8BTU4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8BUM1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8BVK3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8BXC0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8C0M2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8CD23 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8CGA1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8CHW4 EI2BE_MOUSE Translation initiation factor eIF-2B subunit epsilon (eIF-2B GDP-GTP exchange factor subunit epsilon) 717 80,086 Chain (1); Cross-link (5); Domain (1); Modified residue (11); Sequence conflict (1) NA NA NA NA FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. {ECO:0000250}. PTM: Phosphorylated at Ser-540 by DYRK2; this is required for subsequent phosphorylation by GSK3B. Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated, probably by NEDD4. {ECO:0000250}. NA SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2 (By similarity). {ECO:0000250}. NA NA NA Q8K403 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8K4Z5 SF3A1_MOUSE Splicing factor 3A subunit 1 (SF3a120) 791 88,545 Beta strand (6); Chain (1); Compositional bias (6); Cross-link (6); Domain (1); Helix (4); Modified residue (9); Repeat (2); Sequence conflict (3); Site (1); Turn (1) NA NA NA NA FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex (By similarity). Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A3 (By similarity). {ECO:0000250}. DOMAIN: SURP motif 2 mediates direct binding to SF3A3. {ECO:0000250}. NA NA Q8R3G9 TSN8_MOUSE Tetraspanin-8 (Tspan-8) 235 25,582 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) NA TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 235 Cytoplasmic. {ECO:0000255}. NA NA NA SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. NA NA NA NA Q8R480 NUP85_MOUSE Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (FROUNT) (Nucleoporin Nup85) (Pericentrin-1) 656 74,776 Chain (1); Erroneous gene model prediction (2); Modified residue (2); Sequence conflict (1) NA NA NA NA FUNCTION: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. {ECO:0000250|UniProtKB:Q9BW27}. NA SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}. SUBUNIT: Component of the nuclear pore complex (NPC). Component of the NPC Nup107-160 subcomplex, consisting of at least NUP107, NUP98/Nup96, NUP160, NUP133, NUP85, NUP37, NUP43 and SEC13. Interacts with NUP160, NUP133 and SEC13 (PubMed:12718872). Interacts with NUP37, NUP107 and NUP43. Interacts with CCR2. {ECO:0000250|UniProtKB:Q9BW27, ECO:0000269|PubMed:12718872}. NA NA NA Q8VC49 IF27B_MOUSE Interferon alpha-inducible protein 27-like protein 2B (Interferon-stimulated gene 12 protein B2) (ISG12(b2)) 283 27,772 Chain (1); Transit peptide (1); Transmembrane (3) NA TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. NA NA FUNCTION: Functions in the intrinsic apoptotic signaling pathway and may have an interferon-induced antiviral activity. {ECO:0000269|PubMed:21151029}. NA SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21151029}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:21151029). Interacts with BAK1 (PubMed:21151029). Interacts with BAX (PubMed:21151029). Interacts with adenine nucleotide translocase (PubMed:21151029). {ECO:0000269|PubMed:21151029}. NA NA NA Q8VC49 IF27B_MOUSE Interferon alpha-inducible protein 27-like protein 2B (Interferon-stimulated gene 12 protein B2) (ISG12(b2)) 283 27,772 Chain (1); Transit peptide (1); Transmembrane (3) NA TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. NA NA FUNCTION: Functions in the intrinsic apoptotic signaling pathway and may have an interferon-induced antiviral activity. {ECO:0000269|PubMed:21151029}. NA SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21151029}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:21151029). Interacts with BAK1 (PubMed:21151029). Interacts with BAX (PubMed:21151029). Interacts with adenine nucleotide translocase (PubMed:21151029). {ECO:0000269|PubMed:21151029}. NA NA NA Q8VC73 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8VC73 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8VCB1 NDC1_MOUSE Nucleoporin NDC1 (Transmembrane protein 48) 673 75,409 Chain (1); Modified residue (8); Topological domain (7); Transmembrane (6) NA TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 71 Perinuclear space. {ECO:0000255}.; TOPO_DOM 93 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 166 Perinuclear space. {ECO:0000255}.; TOPO_DOM 188 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 261 Perinuclear space. {ECO:0000255}.; TOPO_DOM 283 673 Cytoplasmic. {ECO:0000255}. NA FUNCTION: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}. SUBUNIT: Interacts with the NUP35/NUP53. {ECO:0000250|UniProtKB:Q6AXN4}. NA NA NA Q8VCN3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8VDP4 CCAR2_MOUSE Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) 922 103,002 Chain (1); Coiled coil (2); Cross-link (2); Erroneous initiation (2); Modified residue (17); Region (2); Sequence conflict (3) NA NA NA NA FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Inhibits SUV39H1 methyltransferase activity. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity) Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the ligand-dependent transcriptional activation function of ESR2. Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway. Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3. Represses the transcriptional activator activity of BRCA1. Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (By similarity). {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:23398316}. PTM: Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity. {ECO:0000250|UniProtKB:Q8N163}.; PTM: Genotoxic stress induces its sumoylation and sumoylation promotes the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated deacetylation of p53/TP53. Sumoylation leads to transcriptional activation of p53/TP53 by sequestering SIRT1 from p53/TP53. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8N163}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N163}. Cytoplasm {ECO:0000250|UniProtKB:Q8N163}. Note=Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis. {ECO:0000250|UniProtKB:Q8N163}. SUBUNIT: Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1, which inhibits the deacetylation of substrates. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with NR1D1. Interacts (via N-terminus) with ESR1 and ESR2. Interacts (via N-terminus) with HDAC3 (via C-terminus). Interacts with HDAC1 and MED2F. Interacts with MCC. Interacts (via N-terminus) with NR1H2 and NR1H3 in a ligand-independent manner. Interacts with CSNK2A1. Interacts (via N-terminus) with p53/TP53. Interacts (via N-terminus) with BRCA1 (via the BRCT domains). Interacts (via N-terminus) with CHEK2 (via protein kinase domain). Interacts with PSEM3. Interacts (via N-terminus) with PSIA3 and SENP1. The sumoylated form shows a preferential interaction with SIRT1 as compared to its unmodified form (By similarity). {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:25732823}. NA NA NA Q8VDU3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8VHM5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q8VI94 OASL1_MOUSE 2'-5'-oligoadenylate synthase-like protein 1 (2',5'-oligoadenylate synthetase-like 9) 511 59,088 Chain (1); Domain (2); Frameshift (1); Sequence conflict (19) NA NA NA NA FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity via an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:12799444}. NA SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1 (By similarity). {ECO:0000250}. NA NA NA Q8VIJ6 SFPQ_MOUSE Splicing factor, proline- and glutamine-rich (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor) 699 75,442 Chain (1); Coiled coil (1); Compositional bias (11); Cross-link (3); Domain (2); Modified residue (32); Region (1); Repeat (3); Sequence conflict (2) NA NA NA NA FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (By similarity). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}. PTM: Phosphorylated on multiple serine and threonine residues during apoptosis (By similarity). Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest (By similarity). In resting T-cells is phosphorylated at Thr-679 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-679. {ECO:0000250|UniProtKB:P23246}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P23246}. Nucleus matrix {ECO:0000269|PubMed:21680841}. Cytoplasm {ECO:0000250|UniProtKB:P23246}. Note=Predominantly in nuclear matrix. {ECO:0000250|UniProtKB:P23246}. SUBUNIT: Heterodimer with NONO. Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells. Interacts with PSPC1 (PubMed:15140795). Interacts with RNF43 (By similarity). Interacts with PITX3 and NR4A2/NURR1 (PubMed:19144721). Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA (By similarity). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (PubMed:21680841). Interacts with PER1 and PER2 (PubMed:22966205). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By similarity). Interacts with PQBP1. Component of a multiprotein complex with NONO and WASL (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}. DOMAIN: The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). The coiled coil domain is required for optimal DNA binding, and optimal transcription activation. {ECO:0000250|UniProtKB:P23246}. NA NA Q91VM5 RMXL1_MOUSE RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1) (RNA binding motif protein, X chromosome retrogene) 388 42,162 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Sequence conflict (5) NA NA NA NA FUNCTION: RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. NA NA NA NA Q91YL3 UCKL1_MOUSE Uridine-cytidine kinase-like 1 (EC 2.7.1.48) 548 60,842 Chain (1); Modified residue (3); Nucleotide binding (1) NA NA NA Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1. FUNCTION: May contribute to UTP accumulation needed for blast transformation and proliferation. {ECO:0000250}. PTM: Ubiquitinated by RNF19B; which induces proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with RNF19B. {ECO:0000250}. NA NA NA Q91YR9 PTGR1_MOUSE Prostaglandin reductase 1 (PRG-1) (EC 1.3.1.-) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (NADP-dependent leukotriene B4 12-hydroxydehydrogenase) (EC 1.3.1.74) 329 35,560 Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (2) NA NA NA NA FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer or homodimer. {ECO:0000250}. NA NA NA Q91YR9 PTGR1_MOUSE Prostaglandin reductase 1 (PRG-1) (EC 1.3.1.-) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (NADP-dependent leukotriene B4 12-hydroxydehydrogenase) (EC 1.3.1.74) 329 35,560 Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (2) NA NA NA NA FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer or homodimer. {ECO:0000250}. NA NA NA Q920X5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q925B0 PAWR_MOUSE PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) 333 35,908 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2); Motif (2); Region (2) NA NA NA NA FUNCTION: Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15606896}. PTM: Preferentially phosphorylated at the Thr-156 by PKC in cancer cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis. Nuclear localization includes nucleoplasm and PML nuclear bodies (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts (via the C-terminal region) with WT1. Interacts with THAP1. Interacts with AATF. Interacts with BACE1. Interacts with SPSB1 (via B30.2/SPRY domain); this interaction is direct and occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with SPSB2 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with SPSB4 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Component of a ternary complex composed of SQSTM1 and PRKCZ (By similarity). Interacts with actin (By similarity). {ECO:0000250|UniProtKB:Q62627, ECO:0000250|UniProtKB:Q96IZ0}. DOMAIN: The leucine-zipper domain is not essential for apoptosis, but is required for sensitization of cells to exogenous apoptotic insults and for interaction with its partners. {ECO:0000250}.; DOMAIN: The SAC domain is a death-inducing domain selective for apoptosis induction in cancer cells. This domain is essential for nuclear entry, Fas activation, inhibition of NF-kappa-B activity and induction of apoptosis in cancer cells (By similarity). {ECO:0000250}.; DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain. {ECO:0000250|UniProtKB:Q96IZ0}. NA NA Q99JG3 ANX13_MOUSE Annexin A13 (Annexin XIII) (Annexin-13) 317 35,922 Chain (1); Initiator methionine (1); Lipidation (1); Repeat (4) NA NA NA NA NA NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes. {ECO:0000250}. NA DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. NA NA Q99JW5 EPCAM_MOUSE Epithelial cell adhesion molecule (Ep-CAM) (Epithelial glycoprotein 314) (EGP314) (mEGP314) (Protein 289A) (Tumor-associated calcium signal transducer 1) (CD antigen CD326) 315 35,019 Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 267 289 Helical. {ECO:0000255}. TOPO_DOM 24 266 Extracellular. {ECO:0000255}.; TOPO_DOM 290 315 Cytoplasmic. {ECO:0000255}. NA FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity). {ECO:0000250}. PTM: Glycosylation at Asn-198 is crucial for protein stability. {ECO:0000250}. SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250|UniProtKB:P16422}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16422}. Cell junction, tight junction {ECO:0000250|UniProtKB:P16422}. Note=Colocalizes with CLDN7 at the lateral cell membrane and tight junction. {ECO:0000250|UniProtKB:P16422}. SUBUNIT: Monomer. Interacts with phosphorylated CLDN7 (By similarity). {ECO:0000250}. NA NA NA Q99K86 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q99KP6 PRP19_MOUSE Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Nuclear matrix protein 200) (PRP19/PSO4 homolog) (RING-type E3 ubiquitin transferase PRP19) (Senescence evasion factor) 504 55,239 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Region (1); Repeat (7) NA NA NA Protein modification; protein ubiquitination. FUNCTION: Isoform 1: Ubiquitin-protein ligase which is a core component of several complexes mainly involved in pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex. Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries. The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair. Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response. May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA. As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process. In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:17349974). May play a role in the biogenesis of lipid droplets (PubMed:17118936). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity). {ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:17118936, ECO:0000269|PubMed:17349974}.; FUNCTION: Isoform 2: Forced expression leads to suppression of neuronal differentiation, and on the contrary to stimulation of astroglial cell differentiation in retinoic acid-primed P19 cells (PubMed:16352598). {ECO:0000269|PubMed:16352598}. NA SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:16352598}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Lipid droplet {ECO:0000269|PubMed:17118936}. Note=Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Recruited on damaged DNA at sites of double-strand break (By similarity). {ECO:0000250|UniProtKB:Q9UMS4}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:16352598}. Nucleus {ECO:0000269|PubMed:16352598}. SUBUNIT: Homotetramer. Component of the Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes described as PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The Prp19 complex associates with the spliceosome during its assembly and remodeling recruiting additional proteins. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it interacts with the replication protein A complex (RPA). Interacts with SETMAR; required for SETMAR recruitment to site of DNA damage. Interacts with U2AF2; the interaction is direct and recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with KNSTRN (By similarity). Interacts with PSMC5 (PubMed:17349974). Isoform 2 (via N-terminus) interacts with PPIA. Isoform 2 does not interact with CDC5L (PubMed:16352598). Interacts with KHDC4 (By similarity). {ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:16352598, ECO:0000269|PubMed:17349974}. DOMAIN: The 7 WD repeats are necessary and sufficient to support interaction with the RPA complex. {ECO:0000250|UniProtKB:Q9UMS4}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissues, brain and to a lower extent in liver, kidney, muscle, lung and spleen (at protein level). {ECO:0000269|PubMed:17118936}. NA Q99LB4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q99LS5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q99M71 EPDR1_MOUSE Mammalian ependymin-related protein 1 (MERP-1) 224 25,485 Alternative sequence (1); Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) NA NA NA NA NA NA SUBCELLULAR LOCATION: Secreted. NA NA NA NA Q99M71 EPDR1_MOUSE Mammalian ependymin-related protein 1 (MERP-1) 224 25,485 Alternative sequence (1); Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) NA NA NA NA NA NA SUBCELLULAR LOCATION: Secreted. NA NA NA NA Q99MR6 SRRT_MOUSE Serrate RNA effector molecule homolog (Arsenite-resistance protein 2) 875 100,452 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (15); Sequence conflict (1) NA NA NA NA FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription. {ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22198669}. NA SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. Note=Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way. SUBUNIT: Interacts with CASP8AP2 and ERBB4 (By similarity). Interacts with NCBP1/CBP80 and DROSHA (PubMed:19632182). Interacts with LUZP4 (By similarity). Interacts with NCBP2/CBP20 and NCBP3 (By similarity). {ECO:0000250|UniProtKB:Q9BXP5, ECO:0000269|PubMed:19632182}. NA TISSUE SPECIFICITY: Widely expressed, with a preference for proliferating cells. Highly expressed in hematopoietic tissues and reduced or absent expression in parenchymal organs like liver and kidney. In the brain, expressed in the subventricular zone by niche astrocytes, ependymal cells and neural stem cells. In this cerebral context, expressed in slowly dividing cells. {ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22198669}. NA Q99PV0 PRP8_MOUSE Pre-mRNA-processing-splicing factor 8 (Splicing factor Prp8) 2335 273,616 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Region (7); Sequence conflict (2) NA NA NA NA FUNCTION: Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. {ECO:0000250|UniProtKB:Q6P2Q9}. NA SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15169873}. SUBUNIT: Part of the U5 snRNP complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri-snRNP complex. Interacts (via RNase H homology domain) with AAR2. {ECO:0000250|UniProtKB:Q6P2Q9}. DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize the protein structure. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to RNase H, but lacks RNase H activity. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in testis (preferentially in the outer cell layer), and moderately in ovary (preferentially in granulosa cells). {ECO:0000269|PubMed:11275560}. NA Q9BCZ4 SELS_MOUSE Selenoprotein S (SelS) (Minor histocompatibility antigen H47) 190 21,509 Chain (1); Erroneous termination (3); Natural variant (1); Non-standard residue (1); Region (1); Sequence conflict (1); Transmembrane (1) NA TRANSMEM 28 48 Helical. {ECO:0000255}. NA NA FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with DERL1 and (via VIM motif) with VCP, suggesting that it forms a membrane complex with DERL1 that serves as a receptor for VCP. Also interacts with DERL2, DERL3 and SELENOK. The SELENOK-SELENOS complex interacts with VCP (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BQE4}. NA NA NA Q9CQF3 CPSF5_MOUSE Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) 227 26,240 Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Motif (1); Region (3); Sequence conflict (1); Site (2) NA NA NA NA FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (By similarity). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function(PubMed:29249356). Binds to chromatin (PubMed:18032416). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (By similarity). {ECO:0000250|UniProtKB:O43809, ECO:0000269|PubMed:18032416, ECO:0000269|PubMed:29249356}. PTM: Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2. {ECO:0000250|UniProtKB:O43809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18032416}. Cytoplasm {ECO:0000250|UniProtKB:O43809}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. {ECO:0000250|UniProtKB:O43809}. SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer. Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7. The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery. Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA. Interacts with CPSF7. Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner. Interacts with PABPN1 (By similarity). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:11716503). Interacts with SNRNP70 (By similarity). Interacts with VIRMA (By similarity). {ECO:0000250|UniProtKB:O43809, ECO:0000269|PubMed:11716503}. NA TISSUE SPECIFICITY: Expressed in testis (PubMed:18032416). Expressed in male germ cells (at protein level) (PubMed:18032416). {ECO:0000269|PubMed:18032416}. NA Q9CR32 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9CX86 ROA0_MOUSE Heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) 305 30,530 Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (9) NA NA NA NA FUNCTION: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs. {ECO:0000269|PubMed:12456657}. PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA. {ECO:0000269|PubMed:12456657}.; PTM: Arg-293 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}. NA NA NA NA Q9CXX7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9CYL5 GAPR1_MOUSE Golgi-associated plant pathogenesis-related protein 1 (GAPR-1) (Golgi-associated PR-1 protein) (Glioma pathogenesis-related protein 2) (GliPR 2) 154 17,090 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Lipidation (1); Region (1); Sequence conflict (2) NA NA NA NA NA NA SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor. Note=Binds lipid-enriched microdomains of Golgi membranes not only by ionic interactions but also through the myristate. {ECO:0000250|UniProtKB:Q9H4G4}. SUBUNIT: Homodimer. Interacts with CAV1 (By similarity). {ECO:0000250}. NA NA NA Q9D020 5NT3A_MOUSE Cytosolic 5'-nucleotidase 3A (EC 3.1.3.5) (7-methylguanosine phosphate-specific 5'-nucleotidase) (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3) (Cytosolic 5'-nucleotidase III) (cN-III) (Lupin) (Pyrimidine 5'-nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) 331 37,252 Active site (2); Alternative sequence (1); Beta strand (11); Binding site (4); Chain (1); Helix (15); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (2); Turn (3) NA NA NA NA FUNCTION: Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP). CMP seems to be the preferred substrate. {ECO:0000250|UniProtKB:Q9H0P0}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. NA TISSUE SPECIFICITY: Isoform 2 is highly expressed in the brain, heart, spleen, kidney and blood. Isoform 2 is expressed (at protein level) in the spleen, skeletal muscle and gastrointestinal epithelia. NA Q9D1K2 VATF_MOUSE V-type proton ATPase subunit F (V-ATPase subunit F) (V-ATPase 14 kDa subunit) (Vacuolar proton pump subunit F) 119 13,370 Chain (1); Sequence conflict (1) NA NA NA NA FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. NA NA SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). NA NA NA Q9D1M7 FKB11_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP11 (PPIase FKBP11) (EC 5.2.1.8) (19 kDa FK506-binding protein) (19 kDa FKBP) (FKBP-19) (FK506-binding protein 11) (FKBP-11) (Rotamase) 201 22,137 Chain (1); Domain (1); Sequence conflict (2); Signal peptide (1); Transmembrane (1) NA TRANSMEM 156 176 Helical. {ECO:0000255}. NA NA FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. NA SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with IFITM5. {ECO:0000269|PubMed:20838829}. NA NA NA Q9D2Y4 MLKL_MOUSE Mixed lineage kinase domain-like protein 472 54,317 Alternative sequence (1); Beta strand (11); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Helix (19); Modified residue (5); Mutagenesis (8); Nucleotide binding (1); Region (1); Turn (2) NA NA NA NA FUNCTION: Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. Does not have protein kinase activity (PubMed:23835476, PubMed:24012422, PubMed:24019532). Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function (By similarity). {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:23835476, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24019532}. PTM: Phosphorylation by RIPK3 induces a conformational switch that is required for necroptosis. It also induces homotrimerization and localization to the plasma membrane. {ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NB16}. Cell membrane {ECO:0000250|UniProtKB:Q8NB16}. Note=Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction. {ECO:0000250|UniProtKB:Q8NB16}. SUBUNIT: Homooligomer (By similarity). Homotrimer; forms homotrimers on necroptosis induction. Upon TNF-induced necrosis, forms in complex with PGAM5, RIPK1 and RIPK3. Within this complex, may play a role in the proper targeting of RIPK1/RIPK3 to its downstream effector PGAM5 (By similarity). Interacts with RIPK3; the interaction is direct. {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. DOMAIN: The coiled coil region 2 is responsible for homotrimerization. {ECO:0000250}.; DOMAIN: The protein kinase domain is catalytically inactive but contains an unusual pseudoactive site with an interaction between Lys-219 and Gln-343 residues. Upon phosphorylation by RIPK3, undergoes an active conformation (PubMed:24012422, PubMed:24095729). {ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. TISSUE SPECIFICITY: Highly expressed in thymus, colon, intestine, liver, spleen and lung. Expressed at much lower level in skeletal muscle, heart and kidney. Not detected in brain. {ECO:0000269|PubMed:23835476}. NA Q9D4V7 RABL3_MOUSE Rab-like protein 3 236 26,298 Alternative sequence (1); Chain (1); Nucleotide binding (3); Region (1); Sequence conflict (1) NA NA NA NA NA NA NA NA NA NA NA Q9D566 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9D566 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9D6G1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9D816 CP255_MOUSE Cytochrome P450 2C55 (EC 1.14.14.1) (CYPIIC55) 490 56,096 Chain (1); Metal binding (1) NA NA NA NA FUNCTION: Metabolizes arachidonic acid mainly to 19-hydroxyeicosatetraenoic acid (HETE). {ECO:0000269|PubMed:15102943}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. NA NA TISSUE SPECIFICITY: Highest level in colon. Low levels in liver and small intestine. {ECO:0000269|PubMed:15102943}. NA Q9D8S5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9D964 GATM_MOUSE Glycine amidinotransferase, mitochondrial (EC 2.1.4.1) (L-arginine:glycine amidinotransferase) (Transamidinase) 423 48,297 Active site (3); Chain (1); Modified residue (3); Sequence conflict (2); Transit peptide (1) NA NA NA Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 1/2. FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. {ECO:0000269|PubMed:12671064}. NA SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. NA TISSUE SPECIFICITY: Expressed in kidney, brain, gonads, uterus, and embryonic head, chest and abdomen. Maternally expressed in the placenta and yolk sac of embryos. {ECO:0000269|PubMed:12671064}. NA Q9DB34 CHM2A_MOUSE Charged multivesicular body protein 2a (Chromatin-modifying protein 2a) (CHMP2a) (Vacuolar protein sorting-associated protein 2) (mVps2) 222 25,134 Chain (1); Coiled coil (2); Modified residue (6); Motif (1); Region (2) NA NA NA NA FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000250|UniProtKB:O43633}. PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15173323}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. In vitro, heteromerizes with CHMP3 (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A (By similarity). {ECO:0000250}. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart, liver and kidney. {ECO:0000269|PubMed:15173323}. NA Q9DBG9 TX1B3_MOUSE Tax1-binding protein 3 (Tax interaction protein 1) (TIP-1) 124 13,723 Beta strand (8); Chain (1); Domain (1); Helix (5); Initiator methionine (1); Modified residue (2) NA NA NA NA FUNCTION: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:12874278}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12874278}. Nucleus {ECO:0000269|PubMed:12874278}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to the cell membrane by interaction with membrane proteins. {ECO:0000250}. SUBUNIT: Interacts (via its PDZ domain) with GLS2. Interacts (via its PDZ domain) with RTKN (via the C-terminal region); this interaction facilitates Rho-mediated activation of the FOS serum response element (SRE). Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 binding (By similarity). Interacts (via its PDZ domain) with CTNNB1; this interaction inhibits the transcriptional activity of CTNNB1. Interacts with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:O14907, ECO:0000269|PubMed:12874278, ECO:0000269|PubMed:18835279}. NA NA NA Q9DBR7 MYPT1_MOUSE Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) 1029 114,996 Alternative sequence (1); Chain (1); Compositional bias (2); Modified residue (27); Motif (1); Region (1); Repeat (6) NA NA NA NA FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity (By similarity). {ECO:0000250|UniProtKB:O14974, ECO:0000250|UniProtKB:Q10728}. PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 (By similarity). Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-694, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-694 by DMPK; may inhibit the myosin phosphatase activity (By similarity). Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A (By similarity). {ECO:0000250|UniProtKB:O14974}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}. Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT (By similarity). Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN (By similarity). Interacts with NCKAP1L (By similarity). {ECO:0000250|UniProtKB:O14974}. DOMAIN: Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.; DOMAIN: The KVKF motif mediates interaction with PPP1CB. {ECO:0000250|UniProtKB:O14974}. TISSUE SPECIFICITY: Expressed in striated and vascular smooth muscle, specificcally in type 2a fibers (at protein level). Expression levels are 20-30% higher in developed males than females (at protein level). {ECO:0000269|PubMed:20634291}. NA Q9DBS1 TMM43_MOUSE Transmembrane protein 43 (Protein LUMA) 400 44,783 Chain (1); Initiator methionine (1); Modified residue (1); Topological domain (5); Transmembrane (4) NA TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 346 366 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}. TOPO_DOM 2 31 Nuclear. {ECO:0000255}.; TOPO_DOM 53 313 Perinuclear space. {ECO:0000255}.; TOPO_DOM 335 345 Nuclear. {ECO:0000255}.; TOPO_DOM 367 368 Perinuclear space. {ECO:0000255}.; TOPO_DOM 390 400 Nuclear. {ECO:0000255}. NA FUNCTION: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane. {ECO:0000269|PubMed:18230648}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum. Nucleus inner membrane; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen. SUBUNIT: Can form oligomers through the transmembrane domains. Interacts with EMD; the interaction retains EMD at the inner nuclear membrane. Interacts with LMNA and LMNB2. Interacts with SUN2 (By similarity). {ECO:0000250}. NA NA NA Q9DBX3 SUSD2_MOUSE Sushi domain-containing protein 2 820 90,641 Alternative sequence (2); Chain (1); Disulfide bond (9); Domain (4); Frameshift (1); Glycosylation (3); Helix (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 783 803 Helical. {ECO:0000255}. TOPO_DOM 23 782 Extracellular. {ECO:0000255}.; TOPO_DOM 804 820 Cytoplasmic. {ECO:0000255}. NA FUNCTION: May be a cytokine receptor for C10ORF99. May be a tumor suppressor; together with C10ORF99 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May play a role in breast tumorigenesis (PubMed:23131994). {ECO:0000250|UniProtKB:Q9UGT4, ECO:0000269|PubMed:23131994}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UGT4}; Single-pass type I membrane protein {ECO:0000305}. NA NA NA NA Q9DD06 RARR2_MOUSE Retinoic acid receptor responder protein 2 (Chemerin) 162 18,350 Chain (1); Disulfide bond (3); Natural variant (1); Propeptide (1); Signal peptide (1) NA NA NA NA FUNCTION: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an increase in secretion of proinflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Exhibits an antimicrobial function in the skin. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:18242188}. PTM: Secreted in an inactive precursor form, prochemerin, which is proteolytically processed by a variety of extracellular proteases to generate forms with differing levels of bioactivity. For example, the removal of six amino acids results in chemerin-156, which exhibits the highest activity, while removal of seven amino acids results in chemerin-155 which has slightly less activity. Some proteases are able to cleave at more than one site and chemerin forms may be sequentially processed by different enzymes to modulate activity levels. The coordinated expression and activity of chemerin-modifying enzymes is essential for regulating its bioactivation, inactivation and, consequently, biological function. Cathepsin G cleaves seven C-terminal amino acids from prochemerin (chemerin-155), elastase is able to cleave six (chemerin-156), eight (chemerin-154) or eleven (chemerin-151), plasmin cleaves five amino acids (chemerin-157), and tryptase cleaves five (chemerin-157) or eight (chemerin-154). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-157), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-156) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:18242188}. NA NA TISSUE SPECIFICITY: Expressed in the differentiated adipocytes (at protein level). Abundantly expressed in the liver, adipose tissue including visceral, epididymal, and brown adipose tissue. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188}. NA Q9EQ79 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Q9ER41 TOR1B_MOUSE Torsin-1B (Torsin ATPase-1B) (EC 3.6.4.-) (Torsin family 1 member B) 336 37,818 Chain (1); Glycosylation (2); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1) NA NA NA NA FUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:20457914}. PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus membrane. SUBUNIT: Homohexamer. Interacts with TOR1A; the interaction may be specific of neural tissues. Interacts with TOR1AIP1; TOR1AIP1 is required for TOR1B location on the nuclear membrane. Interacts (ATP-bound) with TOR1AIP2; important for endoplasmic reticulum integrity. {ECO:0000269|PubMed:20457914}. NA TISSUE SPECIFICITY: Highly expressed in liver and muscle; lower expression levels are observed in brain (at protein level). {ECO:0000269|PubMed:20015956}. NA Q9R0Y5 KAD1_MOUSE Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) 194 21,540 Alternative sequence (1); Binding site (7); Chain (1); Erroneous gene model prediction (1); Modified residue (2); Nucleotide binding (3); Region (2) NA NA NA NA FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also possesses broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). May provide a mechanism to buffer the adenylate energy charge for sperm motility. {ECO:0000250, ECO:0000269|PubMed:16790685}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171}. NA NA Q9WU81 G6PT3_MOUSE Glucose-6-phosphate exchanger SLC37A2 (Solute carrier family 37 member 2) (cAMP-inducible protein 2) 501 55,073 Alternative sequence (1); Chain (1); Frameshift (1); Glycosylation (3); Sequence conflict (2); Transmembrane (12) NA TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 118 140 Helical. {ECO:0000255}.; TRANSMEM 142 164 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}. NA NA FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. {ECO:0000250|UniProtKB:Q8TED4}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TED4}; Multi-pass membrane protein {ECO:0000255}. NA NA TISSUE SPECIFICITY: Highly expressed in bone marrow derived macrophages, and weakly in spleen. {ECO:0000269|PubMed:11004510}. NA Q9Z2G9 HTAI2_MOUSE Oxidoreductase HTATIP2 (EC 1.1.1.-) 242 26,870 Active site (2); Alternative sequence (2); Beta strand (9); Binding site (1); Chain (1); Helix (9); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (7) NA NA NA NA FUNCTION: Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. {ECO:0000269|PubMed:14695192}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. SUBUNIT: Monomer. Binds nuclear transport receptors XPO4, IPO5/RANBP5, IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and LRPPRC probably through their HEAT repeats. Binds NCOA5/CIA (By similarity). {ECO:0000250}. NA NA NA V9GX26 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Z4YK56 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA Z4YLT8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA