MAP1B_HUMAN
ID MAP1B_HUMAN Reviewed; 2468 AA.
AC P46821; A2BDK5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Microtubule-associated protein 1B;
DE Short=MAP-1B;
DE Contains:
DE RecName: Full=MAP1B heavy chain;
DE Contains:
DE RecName: Full=MAP1 light chain LC1;
GN Name=MAP1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-594.
RC TISSUE=Fetal brain;
RX PubMed=7806212; DOI=10.1006/geno.1994.1384;
RA Lien L.L., Feener C., Fischbach N., Kunkel L.M.;
RT "Cloning of human microtubule-associated protein 1B and the identification
RT of a related gene on chromosome 15.";
RL Genomics 22:273-280(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-594.
RX PubMed=12684070; DOI=10.1016/s1389-0344(03)00003-0;
RA Dergunova L.V., Raevskaya N.M., Vladychenskaya I.P., Limborska S.A.;
RT "Hmob3 brain-specific sequence is a part of phylogenetically conserved
RT human MAP1B gene 3'-untranslated region.";
RL Biomol. Eng. 20:91-96(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-594.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 2-31; 55-64; 90-98; 391-429; 520-531; 1052-1070;
RP 1233-1250; 1276-1287; 1462-1476; 1834-1958 AND 1898-1908, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Lung fibroblast;
RA Bienvenut W.V., Pchelintsev N., Adams P.D.;
RL Submitted (OCT-2009) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 2347-2370 AND 2382-2409, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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 [8]
RP INTERACTION WITH TMEM185A.
RX PubMed=15525354; DOI=10.1111/j.1471-4159.2004.02799.x;
RA Maurer M.H., Gruenewald S., Gassler N., Rossner M., Propst F., Wuerz R.,
RA Weber D., Kuner T., Kuschinsky W., Schneider A.;
RT "Cloning of a novel neuronally expressed orphan G-protein-coupled receptor
RT which is up-regulated by erythropoietin, interacts with microtubule-
RT associated protein 1b and colocalizes with the 5-hydroxytryptamine 2a
RT receptor.";
RL J. Neurochem. 91:1007-1017(2004).
RN [9]
RP INTERACTION WITH GAN.
RX PubMed=16227972; DOI=10.1038/nature04256;
RA Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.;
RT "Gigaxonin-controlled degradation of MAP1B light chain is critical to
RT neuronal survival.";
RL Nature 438:224-228(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-995; SER-1016;
RP SER-1265; SER-1276; SER-1280; THR-1282; SER-1396; SER-1400; SER-1427;
RP SER-1438; SER-1443; SER-1618; SER-1620; SER-1625; SER-1779; SER-1782 AND
RP THR-1788, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP CLEAVAGE SITE.
RX PubMed=18419581; DOI=10.1042/bj20071449;
RA Zou B., Yan H., Kawasaki F., Ordway R.W.;
RT "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH
RT reveals heavy- and light-chain subunits generated by proteolytic processing
RT at a conserved cleavage site.";
RL Biochem. J. 414:63-71(2008).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DAPK1.
RX PubMed=18195017; DOI=10.1074/jbc.m706040200;
RA Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P.,
RA Hupp T.R.;
RT "DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and
RT membrane blebbing.";
RL J. Biol. Chem. 283:9999-10014(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1396;
RP SER-1400 AND SER-1501, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-828; SER-831; SER-832; SER-937; SER-992; SER-995;
RP SER-1016; SER-1144; SER-1154; SER-1156; SER-1208; SER-1252; SER-1256;
RP SER-1260; SER-1265; THR-1282; SER-1378; SER-1387; SER-1389; SER-1400;
RP SER-1427; SER-1443; SER-1501; SER-1653; SER-1779; SER-1782; SER-1785;
RP THR-1788; SER-1797; SER-1915; SER-1917; SER-1965; SER-2271 AND SER-2289,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-541; SER-614;
RP SER-831; SER-832; SER-937; THR-948; SER-995; SER-1016; SER-1144; SER-1154;
RP SER-1208; SER-1252; SER-1256; SER-1260; SER-1262; SER-1265; SER-1276;
RP THR-1282; SER-1298; SER-1322; SER-1389; SER-1396; SER-1400; SER-1427;
RP SER-1438; SER-1443; SER-1501; SER-1779; SER-1782; SER-1785; THR-1788;
RP SER-1793; SER-1899; SER-1915; SER-1917; SER-1919; THR-1932; SER-1939;
RP THR-1949; SER-1965; THR-2034; SER-2209; SER-2271 AND THR-2305, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP INTERACTION WITH MAP1LC3B.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
RT satellites.";
RL Nature 502:254-257(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1265;
RP SER-1400; SER-1653; SER-1666; SER-1785 AND THR-1932, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP INTERACTION WITH KIRREL3.
RX PubMed=25902260; DOI=10.1371/journal.pone.0123106;
RA Liu Y.F., Sowell S.M., Luo Y., Chaubey A., Cameron R.S., Kim H.G.,
RA Srivastava A.K.;
RT "Autism and intellectual disability-associated KIRREL3 interacts with
RT neuronal proteins MAP1B and MYO16 with potential roles in
RT neurodevelopment.";
RL PLoS ONE 10:E0123106-E0123106(2015).
RN [27]
RP INVOLVEMENT IN PVNH9, AND VARIANTS PVNH9 303-ARG--LEU-2468 DEL;
RP 532-GLN--LEU-2468 DEL AND 1106-ARG--LEU-2468 DEL.
RX PubMed=29738522; DOI=10.1371/journal.pgen.1007281;
RG Epi4K Consortium, Epilepsy Phenome/Genome Project;
RA Heinzen E.L., O'Neill A.C., Zhu X., Allen A.S., Bahlo M., Chelly J.,
RA Chen M.H., Dobyns W.B., Freytag S., Guerrini R., Leventer R.J., Poduri A.,
RA Robertson S.P., Walsh C.A., Zhang M.;
RL PLoS Genet. 14:e1007281-e1007281(2018).
RN [28]
RP VARIANTS PVNH9 1032-GLU--LEU-2468 DEL AND 1664-ARG--LEU-2468 DEL, AND
RP CHARACTERIZATION OF VARIANTS PVNH9 1032-GLU--LEU-2468 DEL AND
RP 1664-ARG--LEU-2468 DEL.
RX PubMed=30150678; DOI=10.1038/s41467-018-05595-6;
RA Walters G.B., Gustafsson O., Sveinbjornsson G., Eiriksdottir V.K.,
RA Agustsdottir A.B., Jonsdottir G.A., Steinberg S., Gunnarsson A.F.,
RA Magnusson M.I., Unnsteinsdottir U., Lee A.L., Jonasdottir A.,
RA Sigurdsson A., Jonasdottir A., Skuladottir A., Jonsson L., Nawaz M.S.,
RA Sulem P., Frigge M., Ingason A., Love A., Norddhal G.L., Zervas M.,
RA Gudbjartsson D.F., Ulfarsson M.O., Saemundsen E., Stefansson H.,
RA Stefansson K.;
RT "MAP1B mutations cause intellectual disability and extensive white matter
RT deficit.";
RL Nat. Commun. 9:3456-3456(2018).
RN [29]
RP VARIANT PVNH9 679-GLU--LEU-2468 DEL.
RX PubMed=31317654; DOI=10.1002/ajmg.a.61280;
RA Julca D.M., Diaz J., Berger S., Leon E.;
RT "MAP1B related syndrome: Case presentation and review of literature.";
RL Am. J. Med. Genet. A 179:1703-1708(2019).
RN [30]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-326 AND MET-574.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Facilitates tyrosination of alpha-tubulin in neuronal
CC microtubules (By similarity). Phosphorylated MAP1B may play a role in
CC the cytoskeletal changes that accompany neurite extension. Possibly
CC MAP1B binds to at least two tubulin subunits in the polymer, and this
CC bridging of subunits might be involved in nucleating microtubule
CC polymerization and in stabilizing microtubules. Acts as a positive
CC cofactor in DAPK1-mediated autophagic vesicle formation and membrane
CC blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017}.
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. Interacts with the tubulin
CC tyrosine TTL (By similarity). Interacts (via C-terminus) with GAN (via
CC Kelch domains) (PubMed:12147674, PubMed:16227972). Interacts (via N-
CC terminus) with DAPK1 (PubMed:18195017). Interacts with TMEM185A
CC (PubMed:15525354). Interacts with MAP1LC3B (PubMed:24089205). Interacts
CC with KIRREL3 (PubMed:25902260). MAP1 light chain LC1 (via C-terminus):
CC Interacts with ELAVL4; the interaction contributes to the association
CC of ELAVL4 with microtubules (By similarity). MAP1 light chain LC1:
CC Interacts with ELAVL2 and ELAVL3 (By similarity).
CC {ECO:0000250|UniProtKB:P14873, ECO:0000269|PubMed:12147674,
CC ECO:0000269|PubMed:15525354, ECO:0000269|PubMed:16227972,
CC ECO:0000269|PubMed:18195017, ECO:0000269|PubMed:24089205,
CC ECO:0000269|PubMed:25902260}.
CC -!- INTERACTION:
CC P46821; Q9H2C0: GAN; NbExp=3; IntAct=EBI-764611, EBI-764342;
CC P46821; P50406: HTR6; NbExp=4; IntAct=EBI-764611, EBI-1182222;
CC P46821; P04637: TP53; NbExp=6; IntAct=EBI-764611, EBI-366083;
CC PRO_0000018605; Q8IZU9: KIRREL3; NbExp=4; IntAct=EBI-9517186, EBI-16427312;
CC PRO_0000018605; Q5S007: LRRK2; NbExp=5; IntAct=EBI-9517186, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18195017}. Cytoplasm {ECO:0000269|PubMed:18195017}.
CC Synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}.
CC Note=Colocalizes with DAPK1 in the microtubules and cortical actin
CC fibers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [MAP1 light chain LC1]: Cytoplasm
CC {ECO:0000250|UniProtKB:P14873}.
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.
CC -!- PTM: LC1 is generated from MAP1B by proteolytic processing.
CC {ECO:0000269|PubMed:18419581}.
CC -!- PTM: S-nitrosylation at Cys-2464 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:0000250}.
CC -!- DISEASE: Periventricular nodular heterotopia 9 (PVNH9) [MIM:618918]: A
CC form of periventricular nodular heterotopia, a disorder resulting from
CC a defect in the pattern of neuronal migration in which ectopic
CC collections of neurons lie along the lateral ventricles of the brain or
CC just beneath, contiguously or in isolated patches. PVNH9 is an
CC autosomal dominant disorder with incomplete penetrance, characterized
CC by impaired intellectual development, cognitive defects, learning
CC disabilities, and behavior abnormalities. Some patients develop
CC seizures. {ECO:0000269|PubMed:29738522, ECO:0000269|PubMed:30150678,
CC ECO:0000269|PubMed:31317654}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
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DR EMBL; L06237; AAA18904.1; -; mRNA.
DR EMBL; BN001084; CAM06633.1; -; mRNA.
DR EMBL; AC012609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95697.1; -; Genomic_DNA.
DR CCDS; CCDS4012.1; -.
DR RefSeq; NP_005900.2; NM_005909.4.
DR AlphaFoldDB; P46821; -.
DR BioGRID; 110304; 126.
DR DIP; DIP-33474N; -.
DR IntAct; P46821; 77.
DR MINT; P46821; -.
DR STRING; 9606.ENSP00000296755; -.
DR ChEMBL; CHEMBL3217382; -.
DR CarbonylDB; P46821; -.
DR GlyGen; P46821; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P46821; -.
DR MetOSite; P46821; -.
DR PhosphoSitePlus; P46821; -.
DR SwissPalm; P46821; -.
DR BioMuta; MAP1B; -.
DR DMDM; 317373388; -.
DR EPD; P46821; -.
DR jPOST; P46821; -.
DR MassIVE; P46821; -.
DR MaxQB; P46821; -.
DR PaxDb; P46821; -.
DR PeptideAtlas; P46821; -.
DR PRIDE; P46821; -.
DR ProteomicsDB; 55766; -.
DR Antibodypedia; 4064; 306 antibodies from 34 providers.
DR DNASU; 4131; -.
DR Ensembl; ENST00000296755.12; ENSP00000296755.7; ENSG00000131711.15.
DR GeneID; 4131; -.
DR KEGG; hsa:4131; -.
DR MANE-Select; ENST00000296755.12; ENSP00000296755.7; NM_005909.5; NP_005900.2.
DR UCSC; uc003kbw.5; human.
DR CTD; 4131; -.
DR DisGeNET; 4131; -.
DR GeneCards; MAP1B; -.
DR HGNC; HGNC:6836; MAP1B.
DR HPA; ENSG00000131711; Group enriched (brain, retina).
DR MalaCards; MAP1B; -.
DR MIM; 157129; gene.
DR MIM; 618918; phenotype.
DR neXtProt; NX_P46821; -.
DR OpenTargets; ENSG00000131711; -.
DR Orphanet; 98892; Periventricular nodular heterotopia.
DR PharmGKB; PA30581; -.
DR VEuPathDB; HostDB:ENSG00000131711; -.
DR eggNOG; KOG3592; Eukaryota.
DR GeneTree; ENSGT00940000155897; -.
DR HOGENOM; CLU_000285_0_1_1; -.
DR InParanoid; P46821; -.
DR OMA; VTKANHV; -.
DR OrthoDB; 86642at2759; -.
DR PhylomeDB; P46821; -.
DR TreeFam; TF350229; -.
DR PathwayCommons; P46821; -.
DR SignaLink; P46821; -.
DR SIGNOR; P46821; -.
DR BioGRID-ORCS; 4131; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; MAP1B; human.
DR GeneWiki; MAP1B; -.
DR GenomeRNAi; 4131; -.
DR Pharos; P46821; Tchem.
DR PRO; PR:P46821; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P46821; protein.
DR Bgee; ENSG00000131711; Expressed in lateral nuclear group of thalamus and 213 other tissues.
DR ExpressionAtlas; P46821; baseline and differential.
DR Genevisible; P46821; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISS:ARUK-UCL.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0097441; C:basal dendrite; ISS:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0097457; C:hippocampal mossy fiber; ISS:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; ISS:ARUK-UCL.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:DFLAT.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043196; C:varicosity; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:ARUK-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0048675; P:axon extension; TAS:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0021700; P:developmental maturation; IEA:Ensembl.
DR GO; GO:0061162; P:establishment of monopolar cell polarity; IEA:Ensembl.
DR GO; GO:0051915; P:induction of synaptic plasticity by chemical substance; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IEA:Ensembl.
DR GO; GO:0032387; P:negative regulation of intracellular transport; IEA:Ensembl.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; TAS:ARUK-UCL.
DR GO; GO:0071895; P:odontoblast differentiation; IDA:GO_Central.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
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; 6.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; S-nitrosylation; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:21406692"
FT CHAIN 2..2468
FT /note="Microtubule-associated protein 1B"
FT /id="PRO_0000018604"
FT CHAIN 2..2206
FT /note="MAP1B heavy chain"
FT /id="PRO_0000418379"
FT CHAIN 2207..2468
FT /note="MAP1 light chain LC1"
FT /id="PRO_0000018605"
FT REPEAT 1878..1894
FT /note="MAP1B 1"
FT REPEAT 1895..1911
FT /note="MAP1B 2"
FT REPEAT 1912..1928
FT /note="MAP1B 3"
FT REPEAT 1929..1945
FT /note="MAP1B 4"
FT REPEAT 1946..1962
FT /note="MAP1B 5"
FT REPEAT 1963..1979
FT /note="MAP1B 6"
FT REPEAT 1997..2013
FT /note="MAP1B 7"
FT REPEAT 2014..2030
FT /note="MAP1B 8"
FT REPEAT 2031..2047
FT /note="MAP1B 9"
FT REPEAT 2048..2064
FT /note="MAP1B 10"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1849..1896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1911..2037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2093..2349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2294..2468
FT /note="Mediates interaction with TMEM185A"
FT /evidence="ECO:0000269|PubMed:15525354"
FT COMPBIAS 553..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..959
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1039
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2324..2349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:21406692"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:23186163"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 899
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 908
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1282
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1410
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1525
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1788
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1796
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15205"
FT MOD_RES 1881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1932
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1949
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2034
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2305
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 2464
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT VARIANT 303..2468
FT /note="Missing (in PVNH9)"
FT /evidence="ECO:0000269|PubMed:29738522"
FT /id="VAR_084525"
FT VARIANT 326
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs766004582)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036016"
FT VARIANT 532..2468
FT /note="Missing (in PVNH9)"
FT /evidence="ECO:0000269|PubMed:29738522"
FT /id="VAR_084526"
FT VARIANT 574
FT /note="V -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs369022142)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036017"
FT VARIANT 594
FT /note="I -> V (in dbSNP:rs1866374)"
FT /evidence="ECO:0000269|PubMed:12684070,
FT ECO:0000269|PubMed:7806212, ECO:0000269|Ref.4"
FT /id="VAR_024530"
FT VARIANT 679..2468
FT /note="Missing (in PVNH9)"
FT /evidence="ECO:0000269|PubMed:31317654"
FT /id="VAR_084527"
FT VARIANT 869
FT /note="E -> G (in dbSNP:rs16876070)"
FT /id="VAR_030347"
FT VARIANT 1032..2468
FT /note="Missing (in PVNH9; no effect on protein expression)"
FT /evidence="ECO:0000269|PubMed:30150678"
FT /id="VAR_084528"
FT VARIANT 1106..2468
FT /note="Missing (in PVNH9)"
FT /evidence="ECO:0000269|PubMed:29738522"
FT /id="VAR_084529"
FT VARIANT 1296
FT /note="P -> L (in dbSNP:rs34093016)"
FT /id="VAR_034105"
FT VARIANT 1664..2468
FT /note="Missing (in PVNH9; no effect on protein expression)"
FT /evidence="ECO:0000269|PubMed:30150678"
FT /id="VAR_084530"
FT VARIANT 1917
FT /note="S -> R (in dbSNP:rs13153166)"
FT /id="VAR_056123"
SQ SEQUENCE 2468 AA; 270634 MW; 3FFDCB2E20049A8A CRC64;
MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE 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 LEEEQSQGST TNSDWMKNLI SPDLGVVFLN
VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIDPVI LFQKMGVGKL
EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE FILPNGQEVD LPISYLTSVS SLIVWHPANP
AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD
SRESLKPAAK PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK EEKEKPKKEV
AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV KKETPPKEVK KEVKKEEKKE
VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK KPAALKPKVP KKEESVKKDS VAAGKPKEKG
KIKVIKKEGK AAEAVAAAVG TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF
EELKAEEVDV TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE AEEPEEDGEE
HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA EEDMDEAIEK GEAEQSEEEA
DEEDKAEDAR EEEYEPEKME AEDYVMAVVD KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE
PASSIHDETL PGGSESEATA SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR
DVMSDETNNE ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK VSPSKSPSLS
PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE VTQEVVEEHC ASPEDKTLEV
VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT EVIEKPPAVP VSFEFSDAKD ENERASVSPM
DEPVPDSESP IEKVLSPLRS PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD
QVSPVSEMTS TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA SVSTASVATS
SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT FQETEMSPSK EECPRPMSIS
PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG QESPEQSLAM DFSRQSPDHP TVGAGVLHIT
ENGPTEVDYS PSDMQDSSLS HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ
IASPLQEDTL SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD LSTPGLEKDS
GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD VGGYYYEKIE RTTKSPSDSG
YSYETIGKTT KTPEDGDYSY EIIEKTTRTP EEGGYSYDIS EKTTSPPEVS GYSYEKTERS
RRLLDDISNG YDDSEDGGHT LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY
CYETAEKITR TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV SESAPSQTDS
DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP PPAPVQDRSP SPRHPDVSMV
DPEALAIEQN LGKALKKDLK EKTKTKKPGT KTKSSSPVKK SDGKSKPLAA SPKPAGLKES
SDKVSRVASP KKKESVEKAA KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG
TTKTTKSSAV PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS SSTVVMQDES
FPACKIEL
