ID MAP1B_MOUSE Reviewed; 2464 AA. AC P14873; E9QM11; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 198. DE RecName: Full=Microtubule-associated protein 1B; DE Short=MAP-1B; DE AltName: Full=MAP1(X); DE AltName: Full=MAP1.2; DE Contains: DE RecName: Full=MAP1B heavy chain; DE Contains: DE RecName: Full=MAP1 light chain LC1; GN Name=Map1b; Synonyms=Mtap1b, Mtap5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DOMAIN. RC STRAIN=Swiss Webster; TISSUE=Brain; RX PubMed=2480963; DOI=10.1083/jcb.109.6.3367; RA Noble M., Lewis S.A., Cowan N.J.; RT "The microtubule binding domain of microtubule-associated protein MAP1B RT contains a repeated sequence motif unrelated to that of MAP2 and tau."; RL J. Cell Biol. 109:3367-3376(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP INTERACTION WITH GAN. RX PubMed=12147674; DOI=10.1083/jcb.200202055; RA Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., RA Yang Y.; RT "Microtubule-associated protein 1B: a neuronal binding partner for RT gigaxonin."; RL J. Cell Biol. 158:427-433(2002). RN [4] RP INTERACTION WITH ANP32A. RX PubMed=12807913; DOI=10.1074/jbc.m302785200; RA Opal P., Garcia J.J., Propst F., Matilla A., Orr H.T., Zoghbi H.Y.; RT "Mapmodulin/leucine-rich acidic nuclear protein binds the light chain of RT microtubule-associated protein 1B and modulates neuritogenesis."; RL J. Biol. Chem. 278:34691-34699(2003). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1260; SER-1391 AND SER-1395, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-544; SER-561; RP SER-989; SER-1013; SER-1307; SER-1438; SER-1775 AND SER-1911, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [7] RP INTERACTION WITH TIAM2. RX PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028; RA Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M., RA Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M.; RT "Rho-kinase modulates the function of STEF, a Rac GEF, through its RT phosphorylation."; RL Biochem. Biophys. Res. Commun. 355:788-794(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [9] RP S-NITROSYLATION AT CYS-2460. RX PubMed=17704770; DOI=10.1038/ncb1625; RA Stroissnigg H., Trancikova A., Descovich L., Fuhrmann J., Kutschera W., RA Kostan J., Meixner A., Nothias F., Propst F.; RT "S-nitrosylation of microtubule-associated protein 1B mediates nitric- RT oxide-induced axon retraction."; RL Nat. Cell Biol. 9:1035-1045(2007). RN [10] RP FUNCTION IN REGULATION OF ALPHA-TUBULIN TYROSINATION, AND INTERACTION WITH RP TTL. RX PubMed=18075266; DOI=10.1159/000109863; RA Utreras E., Jimenez-Mateos E.M., Contreras-Vallejos E., Tortosa E., RA Perez M., Rojas S., Saragoni L., Maccioni R.B., Avila J., RA Gonzalez-Billault C.; RT "Microtubule-associated protein 1B interaction with tubulin tyrosine ligase RT contributes to the control of microtubule tyrosination."; RL Dev. Neurosci. 30:200-210(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; SER-1438; SER-1497 AND RP SER-1775, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-339; SER-343; RP SER-561; SER-825; SER-828; SER-829; SER-885; SER-888; THR-896; THR-905; RP THR-945; SER-967; SER-974; SER-992; SER-1013; SER-1141; SER-1151; SER-1153; RP SER-1204; SER-1207; SER-1208; SER-1225; SER-1242; SER-1247; SER-1251; RP SER-1253; SER-1255; SER-1257; SER-1260; SER-1307; SER-1317; SER-1319; RP SER-1321; THR-1323; SER-1325; SER-1334; SER-1371; SER-1373; SER-1382; RP SER-1384; SER-1391; SER-1395; SER-1403; TYR-1405; SER-1438; SER-1497; RP SER-1508; SER-1523; SER-1616; SER-1621; SER-1662; SER-1686; SER-1768; RP SER-1775; SER-1778; SER-1781; THR-1784; SER-1788; SER-1789; TYR-1792; RP SER-1793; SER-1797; SER-1877; SER-1911; THR-1928; THR-1945; SER-2030 AND RP SER-2410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [13] RP INTERACTION WITH ELAVL4, AND SUBCELLULAR LOCATION. RX PubMed=21288476; DOI=10.1016/j.biochi.2011.01.008; RA Fujiwara Y., Kasashima K., Saito K., Fukuda M., Fukao A., Sasano Y., RA Inoue K., Fujiwara T., Sakamoto H.; RT "Microtubule association of a neuronal RNA-binding protein HuD through its RT binding to the light chain of MAP1B."; RL Biochimie 93:817-822(2011). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21984824; DOI=10.1074/jbc.m111.271320; RA Tortosa E., Montenegro-Venegas C., Benoist M., Hartel S., RA Gonzalez-Billault C., Esteban J.A., Avila J.; RT "Microtubule-associated protein 1B (MAP1B) is required for dendritic spine RT development and synaptic maturation."; RL J. Biol. Chem. 286:40638-40648(2011). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2060, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=33268592; DOI=10.1172/jci.insight.136046; RA Cui L., Zheng J., Zhao Q., Chen J.R., Liu H., Peng G., Wu Y., Chen C., RA He Q., Shi H., Yin S., Friedman R.A., Chen Y., Guan M.X.; RT "Mutations of MAP1B encoding a microtubule-associated phosphoprotein cause RT sensorineural hearing loss."; RL JCI Insight 5:0-0(2020). CC -!- FUNCTION: Required for proper microtubule dynamics. Plays a role in the CC cytoskeletal changes that accompany neuronal differentiation and CC neurite extension (PubMed:33268592). Possibly MAP1B binds to at least CC two tubulin subunits in the polymer, and this bridging of subunits CC might be involved in nucleating microtubule polymerization and in CC stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated CC autophagic vesicle formation and membrane blebbing (By similarity). CC Facilitates tyrosination of alpha-tubulin in neuronal microtubules. CC Required for synaptic maturation. {ECO:0000250, CC ECO:0000269|PubMed:18075266, ECO:0000269|PubMed:21984824, CC ECO:0000269|PubMed:33268592}. CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with CC MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region CC of MAP1B. Interacts with ANP32A and TIAM2 (PubMed:12807913, CC PubMed:17320046). Interacts with the tubulin tyrosine TTL CC (PubMed:18075266). Interacts (via C-terminus) with GAN (via Kelch CC domains) (PubMed:12147674). Interacts (via N-terminus) with DAPK1 (By CC similarity). Interacts with TMEM185A (By similarity). Interacts with CC MAP1LC3B (By similarity). Interacts with KIRREL3 (By similarity). MAP1 CC light chain LC1 (via C-terminus): Interacts with ELAVL4; the CC interaction contributes to the association of ELAVL4 with microtubules CC (PubMed:21288476). MAP1 light chain LC1: Interacts with ELAVL2 and CC ELAVL3 (PubMed:21288476). {ECO:0000250|UniProtKB:P46821, CC ECO:0000269|PubMed:12147674, ECO:0000269|PubMed:12807913, CC ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:18075266, CC ECO:0000269|PubMed:21288476}. CC -!- INTERACTION: CC P14873; Q61166: Mapre1; NbExp=5; IntAct=EBI-764653, EBI-2027055; CC P14873; Q9WTU3: Scn8a; NbExp=7; IntAct=EBI-764653, EBI-6396042; CC P14873; Q9UPY8: MAPRE3; Xeno; NbExp=4; IntAct=EBI-764653, EBI-726739; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000305|PubMed:21984824}. Cytoplasm {ECO:0000250}. Synapse CC {ECO:0000269|PubMed:21984824}. Cell projection, dendritic spine CC {ECO:0000269|PubMed:21984824}. Note=Colocalizes with DAPK1 in the CC microtubules and cortical actin fibers. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [MAP1 light chain LC1]: Cytoplasm CC {ECO:0000269|PubMed:21288476}. CC -!- TISSUE SPECIFICITY: Highly expressed in brain and cochlea, mildly CC expressed in heart, and very weakly expressed in liver and muscle. In CC the cochlea, it is abundantly expressed in spiral ganglions. CC {ECO:0000269|PubMed:33268592}. CC -!- DOMAIN: Has a highly basic region with many copies of the sequence KKEE CC and KKEI/V, repeated but not at fixed intervals, which is responsible CC for the binding of MAP1B to microtubules. {ECO:0000269|PubMed:2480963}. CC -!- PTM: LC1 is coexpressed with MAP1B. It is a polypeptide generated from CC MAP1B by proteolytic processing. It is free to associate with both CC MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B. CC -!- PTM: S-nitrosylation at Cys-2460 enhances interaction with CC microtubules, and may act as an effector modification for neuronal CC nitric oxide synthase control of growth-cone size, growth-cone collapse CC and axon retraction. {ECO:0000269|PubMed:17704770}. CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X51396; CAA35761.1; -; mRNA. DR EMBL; AC170188; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS26723.1; -. DR PIR; S07549; QRMSP1. DR RefSeq; NP_032660.2; NM_008634.2. DR AlphaFoldDB; P14873; -. DR BioGRID; 201584; 49. DR IntAct; P14873; 15. DR MINT; P14873; -. DR STRING; 10090.ENSMUSP00000068374; -. DR GlyGen; P14873; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; P14873; -. DR MetOSite; P14873; -. DR PhosphoSitePlus; P14873; -. DR SwissPalm; P14873; -. DR jPOST; P14873; -. DR MaxQB; P14873; -. DR PaxDb; 10090-ENSMUSP00000068374; -. DR PeptideAtlas; P14873; -. DR ProteomicsDB; 295778; -. DR Pumba; P14873; -. DR Antibodypedia; 4064; 335 antibodies from 34 providers. DR DNASU; 17755; -. DR Ensembl; ENSMUST00000064762.6; ENSMUSP00000068374.5; ENSMUSG00000052727.7. DR GeneID; 17755; -. DR KEGG; mmu:17755; -. DR UCSC; uc007rpr.2; mouse. DR AGR; MGI:1306778; -. DR CTD; 4131; -. DR MGI; MGI:1306778; Map1b. DR VEuPathDB; HostDB:ENSMUSG00000052727; -. DR eggNOG; KOG3592; Eukaryota. DR GeneTree; ENSGT00940000155897; -. DR HOGENOM; CLU_000285_0_1_1; -. DR InParanoid; P14873; -. DR OMA; HDHRSPE; -. DR OrthoDB; 5305272at2759; -. DR PhylomeDB; P14873; -. DR TreeFam; TF350229; -. DR BioGRID-ORCS; 17755; 0 hits in 76 CRISPR screens. DR ChiTaRS; Map1b; mouse. DR PRO; PR:P14873; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; P14873; Protein. DR Bgee; ENSMUSG00000052727; Expressed in facial nucleus and 241 other cell types or tissues. DR ExpressionAtlas; P14873; baseline and differential. DR GO; GO:0097440; C:apical dendrite; ISO:MGI. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0097441; C:basal dendrite; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0030426; C:growth cone; ISO:MGI. DR GO; GO:0097457; C:hippocampal mossy fiber; ISO:MGI. DR GO; GO:0005874; C:microtubule; ISO:MGI. DR GO; GO:0005875; C:microtubule associated complex; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0036477; C:somatodendritic compartment; ISO:MGI. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0043196; C:varicosity; ISO:MGI. DR GO; GO:0003779; F:actin binding; ISO:MGI. DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:MGI. DR GO; GO:0008017; F:microtubule binding; ISO:MGI. DR GO; GO:0005543; F:phospholipid binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0048675; P:axon extension; IMP:MGI. DR GO; GO:0007409; P:axonogenesis; IGI:MGI. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl. DR GO; GO:0016358; P:dendrite development; IMP:MGI. DR GO; GO:0021700; P:developmental maturation; IEA:Ensembl. DR GO; GO:0061162; P:establishment of monopolar cell polarity; IMP:MGI. DR GO; GO:0051915; P:induction of synaptic plasticity by chemical substance; IEA:Ensembl. DR GO; GO:0046907; P:intracellular transport; IMP:MGI. DR GO; GO:0001578; P:microtubule bundle formation; IMP:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007017; P:microtubule-based process; TAS:MGI. DR GO; GO:0047497; P:mitochondrion transport along microtubule; IMP:MGI. DR GO; GO:0032387; P:negative regulation of intracellular transport; IMP:MGI. DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0071895; P:odontoblast differentiation; ISO:MGI. DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl. DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI. DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central. DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0017085; P:response to insecticide; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl. DR InterPro; IPR026074; MAP1. DR InterPro; IPR000102; MAP1B_neuraxin. DR PANTHER; PTHR13843; MICROTUBULE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR13843:SF5; MICROTUBULE-ASSOCIATED PROTEIN 1B; 1. DR Pfam; PF00414; MAP1B_neuraxin; 5. DR PROSITE; PS00230; MAP1B_NEURAXIN; 8. DR Genevisible; P14873; MM. PE 1: Evidence at protein level; KW Acetylation; Cell projection; Cytoplasm; Cytoskeleton; Methylation; KW Microtubule; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation; KW Synapse. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P46821" FT CHAIN 2..2464 FT /note="Microtubule-associated protein 1B" FT /id="PRO_0000018606" FT CHAIN 2..2202 FT /note="MAP1B heavy chain" FT /id="PRO_0000418380" FT CHAIN 2203..2464 FT /note="MAP1 light chain LC1" FT /id="PRO_0000018607" FT REPEAT 1874..1890 FT /note="MAP1B 1" FT REPEAT 1891..1907 FT /note="MAP1B 2" FT REPEAT 1908..1924 FT /note="MAP1B 3" FT REPEAT 1925..1941 FT /note="MAP1B 4" FT REPEAT 1942..1958 FT /note="MAP1B 5" FT REPEAT 1959..1975 FT /note="MAP1B 6" FT REPEAT 1993..2009 FT /note="MAP1B 7" FT REPEAT 2010..2026 FT /note="MAP1B 8" FT REPEAT 2027..2043 FT /note="MAP1B 9" FT REPEAT 2044..2060 FT /note="MAP1B 10" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 520..777 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 860..1044 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1060..1157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1179..1482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1513..1752 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1764..1823 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1848..1888 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2049..2074 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2090..2346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2290..2464 FT /note="Mediates interaction with TMEM185A" FT /evidence="ECO:0000250" FT COMPBIAS 553..743 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 751..777 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 907..929 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 930..957 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 966..994 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 995..1027 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1028..1044 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1061..1080 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1109..1131 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1179..1211 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1213..1246 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1313..1341 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1438..1453 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1457..1473 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1543..1564 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1580..1603 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1681..1743 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1781..1818 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2134..2160 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2280..2296 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2304..2319 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2320..2345 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 341 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 527 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 544 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 561 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 614 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 828 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 829 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 885 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 888 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 896 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 905 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 933 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 934 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 945 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 960 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 967 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 974 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 989 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 992 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1013 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1183 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1186 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1204 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1208 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1225 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1242 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1251 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1253 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1255 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1271 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1275 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1277 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1293 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1307 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1319 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1321 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1323 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1334 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1371 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1382 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1384 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1391 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1403 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1405 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1422 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1438 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079" FT MOD_RES 1497 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1508 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1516 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1518 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1521 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1523 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1614 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1616 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1621 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1649 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1659 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1662 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1686 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1768 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1775 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079" FT MOD_RES 1778 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1781 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1784 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1788 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1789 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1792 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1793 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1797 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1815 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15205" FT MOD_RES 1877 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1911 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1915 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 1928 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1945 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2030 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2060 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2205 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 2267 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 2285 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 2301 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46821" FT MOD_RES 2410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2460 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000269|PubMed:17704770" FT CONFLICT 743 FT /note="L -> Q (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 1348..1351 FT /note="TEKP -> SENA (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 1654 FT /note="L -> F (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 1688 FT /note="S -> C (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 1898..1899 FT /note="GG -> VR (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 1926 FT /note="I -> T (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 2231 FT /note="L -> V (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" FT CONFLICT 2333 FT /note="A -> T (in Ref. 1; CAA35761)" FT /evidence="ECO:0000305" SQ SEQUENCE 2464 AA; 270255 MW; 2835101531B0694A CRC64; MATVVVEATE PEPSGSIGNP AASTSPSLSH RFLDSKFYLL VVVGETVTEE HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEERSQGST SNSDWMKNLI SPDLGVVFLN VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIEPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE LILPNGQEVD IPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD SRESLKPATK PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK EEKPKKEVVK KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK ETPLKDAKKE VKKEEKKEVK KEEKEPKKEI KKISKDIKKS TPLSDTKKPS ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK VIKKEGKTTE AAATAVGTAA TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL KAEEIDVAKD IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE PEEDGEDNAS GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED MDDVLEKGEA EQSEEEGEEE DKAEDAREEG YEPDKTEAED YVMAVADKAA EAGVTEEQYG YLGTSAKQPG IQSPSREPAS SIHDETLPGG SESEATASDE ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM SDETNNEETE SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK SPSLSPSPPS PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV VEEHCASPEE KTLEVVSPSQ SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK PQAVPVSFEF SEAKDENERA SLSPMDEPVP DSESPVEKVL SPLRSPPLLG SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV SDLTSTGLYQ DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST ASVATSSFPE PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET EMSPSKEECP RPMSISPPDF SPKTAKSRTP VQDHRSEQSS MSIEFGQESP EHSLAMDFSR QSPDHPTLGA SVLHITENGP TEVDYSPSDI QDSSLSHKIP PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP LQEDTLSDVV PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS SVEKDSGGKT PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY YYEKTERTIK SPCDSGYSYE TIEKTIKTPE DGGYTCEITE KTTRTPEEGG YSYEISEKTT RTPEVSGYTY EKTERSRRLL DDISNGYDDT EDGGHTLGDC SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET MEKITKTPQA STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA PSQTDSDVPP ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP MQDRSPSPRH PDVSMVDPDA LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS SSPVKKGDGK SKPLAASPKP GALKESSDKV SRVASPKKKE SVEKATKTTT TPEVKATRGE EKDKETKNAA NASASKSAKT ATAGPGTTKT AKSSTVPPGL PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV VMQDESFPAC KIEL //