MAP1B_MOUSE
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 03-AUG-2022, entry version 190.
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, Spleen,
RC 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).
CC -!- FUNCTION: Phosphorylated MAP1B may play a role in the cytoskeletal
CC changes that accompany neurite extension. Possibly MAP1B binds to at
CC least two tubulin subunits in the polymer, and this bridging of
CC subunits might be involved in nucleating microtubule polymerization and
CC in stabilizing microtubules. Acts as a positive cofactor in DAPK1-
CC mediated autophagic vesicle formation and membrane blebbing (By
CC similarity). Facilitates tyrosination of alpha-tubulin in neuronal
CC microtubules. Required for synaptic maturation. {ECO:0000250,
CC ECO:0000269|PubMed:18075266, ECO:0000269|PubMed:21984824}.
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 -!- 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}.
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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; 44.
DR IntAct; P14873; 15.
DR MINT; P14873; -.
DR STRING; 10090.ENSMUSP00000068374; -.
DR iPTMnet; P14873; -.
DR PhosphoSitePlus; P14873; -.
DR SwissPalm; P14873; -.
DR jPOST; P14873; -.
DR MaxQB; P14873; -.
DR PaxDb; P14873; -.
DR PeptideAtlas; P14873; -.
DR PRIDE; P14873; -.
DR ProteomicsDB; 295778; -.
DR Antibodypedia; 4064; 306 antibodies from 34 providers.
DR DNASU; 17755; -.
DR Ensembl; ENSMUST00000064762; ENSMUSP00000068374; ENSMUSG00000052727.
DR GeneID; 17755; -.
DR KEGG; mmu:17755; -.
DR UCSC; uc007rpr.2; mouse.
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; VTKANHV; -.
DR OrthoDB; 86642at2759; -.
DR PhylomeDB; P14873; -.
DR TreeFam; TF350229; -.
DR BioGRID-ORCS; 17755; 0 hits in 71 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 238 other tissues.
DR ExpressionAtlas; P14873; baseline and differential.
DR Genevisible; P14873; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005856; C:cytoskeleton; 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: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; IPR027321; MAP1B.
DR InterPro; IPR000102; MAP1B_neuraxin.
DR PANTHER; PTHR13843; PTHR13843; 1.
DR PANTHER; PTHR13843:SF5; PTHR13843:SF5; 1.
DR Pfam; PF00414; MAP1B_neuraxin; 6.
DR PROSITE; PS00230; MAP1B_NEURAXIN; 8.
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
