MAP4_HUMAN
ID MAP4_HUMAN Reviewed; 1152 AA.
AC P27816; Q13082; Q59FT2; Q68D74; Q6ZUW9; Q86V26; Q96A76; Q96NS9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Microtubule-associated protein 4;
DE Short=MAP-4;
GN Name=MAP4;
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] (ISOFORM 1), AND VARIANTS TYR-427 AND ILE-628.
RX PubMed=1718985; DOI=10.1016/s0021-9258(18)54720-7;
RA West R.R., Tenbarge K.M., Olmsted J.B.;
RT "A model for microtubule-associated protein 4 structure. Domains defined by
RT comparisons of human, mouse, and bovine sequences.";
RL J. Biol. Chem. 266:21886-21896(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7857940; DOI=10.1021/bi00007a025;
RA Chapin S.J., Lue C.M., Yu M.T., Bulinski J.C.;
RT "Differential expression of alternatively spliced forms of MAP4: a
RT repertoire of structurally different microtubule-binding domains.";
RL Biochemistry 34:2289-2301(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-996 (ISOFORM 4).
RC TISSUE=Cerebellum, and Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
RC TISSUE=Eye, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-23; 322-356; 436-448; 561-574; 727-738; 810-832;
RP 853-862; 872-888 AND 923-933, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Prostatic adenocarcinoma;
RA Bienvenut W.V., Ramsay A., Leung H.Y., Zebisch A., Kolch W.;
RL Submitted (OCT-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 102-1152 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1905296; DOI=10.1242/jcs.98.1.27;
RA Chapin S.J., Bulinski J.C.;
RT "Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4) contains
RT a domain homologous to the microtubule-binding domains of neuronal MAP2 and
RT tau.";
RL J. Cell Sci. 98:27-36(1991).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1151 (ISOFORM 5).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP PHOSPHORYLATION AT SER-696 AND SER-787, FUNCTION, AND MUTAGENESIS OF
RP SER-696 AND SER-787.
RX PubMed=10791892; DOI=10.1247/csf.25.33;
RA Kitazawa H., Iida J., Uchida A., Haino-Fukushima K., Itoh T.J., Hotani H.,
RA Ookata K., Murofushi H., Bulinski J.C., Kishimoto T., Hisanaga S.;
RT "Ser787 in the proline-rich region of human MAP4 is a critical
RT phosphorylation site that reduces its activity to promote tubulin
RT polymerization.";
RL Cell Struct. Funct. 25:33-39(2000).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [14]
RP INTERACTION WITH SEPTIN2.
RX PubMed=16093351; DOI=10.1091/mbc.e05-03-0267;
RA Kremer B.E., Haystead T., Macara I.G.;
RT "Mammalian septins regulate microtubule stability through interaction with
RT the microtubule-binding protein MAP4.";
RL Mol. Biol. Cell 16:4648-4659(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; THR-521; THR-571 AND
RP SER-1073, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 (ISOFORM 4),
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571 AND SER-827, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-337 AND SER-338 (ISOFORM 3), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-99; SER-280; SER-358;
RP SER-384; SER-507; THR-521; THR-571; SER-580; THR-585; SER-636; SER-825;
RP SER-941 AND SER-1151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28 AND
RP SER-269 (ISOFORM 4), VARIANT [LARGE SCALE ANALYSIS] ILE-628, AND
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 [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1073, 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; THR-521; THR-571;
RP THR-585 AND SER-1151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-14; SER-280; THR-282; THR-354; SER-358; THR-380; SER-384;
RP SER-507; SER-510; THR-521; THR-526; THR-571; THR-585; SER-624; SER-636;
RP SER-787; SER-797; SER-825; SER-928; SER-941; SER-1073 AND SER-1151,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 (ISOFORM 4), VARIANT
RP [LARGE SCALE ANALYSIS] ILE-628, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], 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 [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; THR-282; SER-358;
RP SER-384; SER-507; THR-521; THR-526; THR-571; SER-636; SER-787; SER-941;
RP THR-942; SER-1000; SER-1073; SER-1145 AND SER-1151, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-803 (ISOFORM 5), AND IDENTIFICATION BY MASS
RP 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 [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-60; SER-280; SER-358;
RP SER-384; SER-440; THR-442; SER-507; SER-510; THR-521; THR-571; SER-580;
RP THR-585; SER-636; SER-696; SER-713; SER-723; SER-787; SER-825; SER-853;
RP SER-928 AND SER-1073, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-358; SER-384;
RP SER-636 AND SER-1000, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-269, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-838, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KNSTRN.
RX PubMed=29180244; DOI=10.1016/j.jaci.2017.10.033;
RA Sharfe N., Karanxha A., Dadi H., Merico D., Chitayat D., Herbrick J.A.,
RA Freeman S., Grinstein S., Roifman C.M.;
RT "Dual loss of p110delta PI3-kinase and SKAP (KNSTRN) expression leads to
RT combined immunodeficiency and multisystem syndromic features.";
RL J. Allergy Clin. Immunol. 142:618-629(2018).
RN [35]
RP MICROTUBULE-BINDING, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=34782749; DOI=10.1038/s41422-021-00584-9;
RA Wang L., Paudyal S.C., Kang Y., Owa M., Liang F.X., Spektor A., Knaut H.,
RA Sanchez I., Dynlacht B.D.;
RT "Regulators of tubulin polyglutamylation control nuclear shape and cilium
RT disassembly by balancing microtubule and actin assembly.";
RL Cell Res. 32:190-209(2022).
CC -!- FUNCTION: Non-neuronal microtubule-associated protein. Promotes
CC microtubule assembly. {ECO:0000269|PubMed:10791892,
CC ECO:0000269|PubMed:34782749}.
CC -!- SUBUNIT: Interacts with SEPTIN2; this interaction impedes tubulin-
CC binding. Interacts with TRAF3IP1 (By similarity). Interacts with KNSTRN
CC (PubMed:29180244). {ECO:0000250|UniProtKB:P27546,
CC ECO:0000269|PubMed:16093351, ECO:0000269|PubMed:29180244}.
CC -!- INTERACTION:
CC P27816; P16333: NCK1; NbExp=2; IntAct=EBI-715255, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:34782749}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000269|PubMed:29180244}. Note=Recruitment to
CC microtubule is inhibited by microtubules polyglutamylation.
CC {ECO:0000269|PubMed:34782749}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P27816-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27816-2; Sequence=VSP_003200;
CC Name=3;
CC IsoId=P27816-3; Sequence=VSP_032065, VSP_032068, VSP_032072,
CC VSP_032073, VSP_032074, VSP_032075;
CC Name=4;
CC IsoId=P27816-4; Sequence=VSP_032066, VSP_032067, VSP_032069,
CC VSP_032070, VSP_032076;
CC Name=5;
CC IsoId=P27816-5; Sequence=VSP_032071, VSP_032077, VSP_032079;
CC Name=6;
CC IsoId=P27816-6; Sequence=VSP_032078;
CC Name=7;
CC IsoId=P27816-7; Sequence=VSP_043240, VSP_043241;
CC -!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by
CC MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing
CC detachment from microtubules, and their disassembly (By similarity).
CC Phosphorylation on Ser-787 negatively regulates MAP4 activity to
CC promote microtubule assembly. Isoform 3 is phosphorylated on Ser-337
CC and Ser-338. {ECO:0000250, ECO:0000269|PubMed:10791892}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92614.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MAP4ID44410ch3p21.html";
CC ---------------------------------------------------------------------------
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DR EMBL; M64571; AAA59553.1; -; mRNA.
DR EMBL; U19727; AAA67361.1; -; mRNA.
DR EMBL; AK054696; BAB70795.1; -; mRNA.
DR EMBL; AK125245; BAC86099.1; -; mRNA.
DR EMBL; AB209377; BAD92614.1; ALT_INIT; mRNA.
DR EMBL; AC124916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64839.1; -; Genomic_DNA.
DR EMBL; BC008715; AAH08715.1; -; mRNA.
DR EMBL; BC012794; AAH12794.1; -; mRNA.
DR EMBL; BC015149; AAH15149.1; -; mRNA.
DR EMBL; BC051843; AAH51843.1; -; mRNA.
DR EMBL; CR749544; CAH18346.1; -; mRNA.
DR CCDS; CCDS33750.1; -. [P27816-1]
DR CCDS; CCDS46818.1; -. [P27816-6]
DR CCDS; CCDS46821.1; -. [P27816-7]
DR PIR; A41206; A33183.
DR RefSeq; NP_001127836.1; NM_001134364.1. [P27816-6]
DR RefSeq; NP_002366.2; NM_002375.4. [P27816-1]
DR RefSeq; NP_112147.2; NM_030885.3. [P27816-7]
DR AlphaFoldDB; P27816; -.
DR BMRB; P27816; -.
DR BioGRID; 110306; 135.
DR IntAct; P27816; 49.
DR MINT; P27816; -.
DR STRING; 9606.ENSP00000353375; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB01248; Docetaxel.
DR DrugBank; DB01229; Paclitaxel.
DR GlyGen; P27816; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; P27816; -.
DR MetOSite; P27816; -.
DR PhosphoSitePlus; P27816; -.
DR SwissPalm; P27816; -.
DR BioMuta; MAP4; -.
DR DMDM; 269849673; -.
DR EPD; P27816; -.
DR jPOST; P27816; -.
DR MassIVE; P27816; -.
DR MaxQB; P27816; -.
DR PaxDb; P27816; -.
DR PeptideAtlas; P27816; -.
DR PRIDE; P27816; -.
DR ProteomicsDB; 54418; -. [P27816-1]
DR ProteomicsDB; 54419; -. [P27816-2]
DR ProteomicsDB; 54420; -. [P27816-3]
DR ProteomicsDB; 54421; -. [P27816-4]
DR ProteomicsDB; 54422; -. [P27816-5]
DR ProteomicsDB; 54423; -. [P27816-6]
DR ProteomicsDB; 54424; -. [P27816-7]
DR Antibodypedia; 29982; 385 antibodies from 29 providers.
DR DNASU; 4134; -.
DR Ensembl; ENST00000360240.10; ENSP00000353375.6; ENSG00000047849.22. [P27816-1]
DR Ensembl; ENST00000395734.7; ENSP00000379083.3; ENSG00000047849.22. [P27816-6]
DR Ensembl; ENST00000434267.5; ENSP00000402767.1; ENSG00000047849.22. [P27816-7]
DR Ensembl; ENST00000439356.2; ENSP00000397414.1; ENSG00000047849.22. [P27816-7]
DR GeneID; 4134; -.
DR KEGG; hsa:4134; -.
DR UCSC; uc003csb.3; human. [P27816-1]
DR CTD; 4134; -.
DR DisGeNET; 4134; -.
DR GeneCards; MAP4; -.
DR HGNC; HGNC:6862; MAP4.
DR HPA; ENSG00000047849; Tissue enhanced (brain, skeletal muscle).
DR MIM; 157132; gene.
DR neXtProt; NX_P27816; -.
DR OpenTargets; ENSG00000047849; -.
DR PharmGKB; PA30608; -.
DR VEuPathDB; HostDB:ENSG00000047849; -.
DR eggNOG; KOG2418; Eukaryota.
DR GeneTree; ENSGT00940000164123; -.
DR HOGENOM; CLU_012370_0_0_1; -.
DR InParanoid; P27816; -.
DR OrthoDB; 1630535at2759; -.
DR PhylomeDB; P27816; -.
DR TreeFam; TF316358; -.
DR PathwayCommons; P27816; -.
DR SignaLink; P27816; -.
DR SIGNOR; P27816; -.
DR BioGRID-ORCS; 4134; 9 hits in 1085 CRISPR screens.
DR ChiTaRS; MAP4; human.
DR GeneWiki; MAP4; -.
DR GenomeRNAi; 4134; -.
DR Pharos; P27816; Tbio.
DR PRO; PR:P27816; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P27816; protein.
DR Bgee; ENSG00000047849; Expressed in dorsal motor nucleus of vagus nerve and 209 other tissues.
DR ExpressionAtlas; P27816; baseline and differential.
DR Genevisible; P27816; HS.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0005930; C:axoneme; IDA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0051301; P:cell division; IMP:MGI.
DR GO; GO:0051294; P:establishment of spindle orientation; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:ARUK-UCL.
DR GO; GO:0051012; P:microtubule sliding; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IMP:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR InterPro; IPR027323; MAP4.
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR PANTHER; PTHR11501:SF16; PTHR11501:SF16; 2.
DR Pfam; PF00418; Tubulin-binding; 4.
DR PROSITE; PS00229; TAU_MAP_1; 4.
DR PROSITE; PS51491; TAU_MAP_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1152
FT /note="Microtubule-associated protein 4"
FT /id="PRO_0000072751"
FT REPEAT 248..261
FT /note="1"
FT REPEAT 262..275
FT /note="2"
FT REPEAT 276..289
FT /note="3"
FT REPEAT 290..303
FT /note="4"
FT REPEAT 304..317
FT /note="5"
FT REPEAT 318..331
FT /note="6"
FT REPEAT 332..345
FT /note="7"
FT REPEAT 346..351
FT /note="8; truncated"
FT REPEAT 352..377
FT /note="26 residues 1"
FT REPEAT 378..403
FT /note="26 residues 2"
FT REPEAT 408..421
FT /note="9"
FT REPEAT 422..433
FT /note="10"
FT REPEAT 434..447
FT /note="11"
FT REPEAT 448..461
FT /note="12"
FT REPEAT 462..475
FT /note="13"
FT REPEAT 476..489
FT /note="14"
FT REPEAT 490..503
FT /note="15"
FT REPEAT 504..517
FT /note="16"
FT REPEAT 532..545
FT /note="17"
FT REPEAT 923..953
FT /note="Tau/MAP 1"
FT REPEAT 992..1022
FT /note="Tau/MAP 2"
FT REPEAT 1023..1053
FT /note="Tau/MAP 3"
FT REPEAT 1054..1085
FT /note="Tau/MAP 4"
FT REGION 50..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..545
FT /note="17 X 14 AA tandem repeats"
FT REGION 362..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10791892,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10791892,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 942
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 838
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032065"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032066"
FT VAR_SEQ 83..221
FT /note="LLANGGHGVEGSDTTGSPTEFLEEKMAYQEYPNSQNWPEDTNFCFQPEQVVD
FT PIQTDPFKMYHDDDLADLVFPSSATADTSIFAGQNDPLKDSYGMSPCNTAVVPQGWSVE
FT ALNSPHSESFVSPEAVAEPPQPTAVPLE -> METTGDQGIEGMAYMDENRNITFTCPR
FT TPSELINKSSPLEVLGSAACEKLPTPTPQVVKEGDSFPDT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032067"
FT VAR_SEQ 98..99
FT /note="GS -> EA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043240"
FT VAR_SEQ 100..1152
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043241"
FT VAR_SEQ 152..437
FT /note="LVFPSSATADTSIFAGQNDPLKDSYGMSPCNTAVVPQGWSVEALNSPHSESF
FT VSPEAVAEPPQPTAVPLELAKEIEMASEERPPAQALEIMMGLKTTDMAPSKETEMALAK
FT DMALATKTEVALAKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVALVKDVR
FT WPTETDVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKMDLAPSKDMGPPKENKKET
FT ERASPIKMDLAPSKDMGPPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVA
FT -> MSLSDKQTASLTAAYGQLSKGKPAECRMDSPKEISQAGFEWQRTEGKLNEIGLNVS
FT MDGQPKDGLVKNASFLEQNKLCFFEGKLDKELSIEMQDKDCQEASGHLESRYVISETCH
FT PLEGNSVHQKTSEFHLGLIEGPDKNKTIPVQGKVAGKNGLETKSQSDLDFPGAADIPTR
FT YVKEQETSVWNPSFHPVAQGSLGSREATPGEMENSITPGCPVIGVVNDNSEQLKCESPL
FT LVSLAHPAPIIEHSPTTIPPITMVFTQEHLNASCHIRDHDKELEK (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032068"
FT VAR_SEQ 225..271
FT /note="EIEMASEERPPAQALEIMMGLKTTDMAPSKETEMALAKDMALATKTE -> N
FT GQEIAPAQISKSLMVDNYTKDGVPGQERPKGPSAVVPSTSTGG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032069"
FT VAR_SEQ 275..666
FT /note="AKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVALVKDVRWPTET
FT DVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKMDLAPSKDMGPPKENKKETERASP
FT IKMDLAPSKDMGPPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVALSSETEV
FT ALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETEIAPAKDVAPSTVKEVGLL
FT KDMSPLSETEMALGKDVTPPPETEVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKDG
FT VLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLESLQDVGQSAAPTF
FT MISPETVTGTGKKCSLPAEEDSVLEKLGERKPCNSQPSELSSETS -> PITTAIETVN
FT IHGDHSLKNKAELADSMKNEAGIDEGHVIGESESVHSGASKHSVEKVTELAKGHLLPGV
FT PVEDQSLPGEARALEGYADRGNFPAHPVNEEKETKEGSVAVQIPDLLEDKAQKLSFCED
FT QNAQDRNSKGSDSLNKKVDLTLLSPKSENDKLKEISLACKITELESVSLPTPEIQSDFL
FT HSKVEAPPSEVADTLVIMTASKGVRLPEPKDKILETPQKMTEKSESKTPGEGKKEDKSR
FT MAEPMKGYMRPTKSRGLTPLLPKSTIQEQERHKQLKSA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032070"
FT VAR_SEQ 322..666
FT /note="WPTETDVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKMDLAPSKDMGPP
FT KENKKETERASPIKMDLAPSKDMGPPKENKIVPAKDLVLLSEIEVAQANDIISSTEISS
FT AEKVALSSETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETEIAPAKD
FT VAPSTVKEVGLLKDMSPLSETEMALGKDVTPPPETEVVLIKNVCLPPEMEVALTEDQVP
FT ALKTEAPLAKDGVLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLES
FT LQDVGQSAAPTFMISPETVTGTGKKCSLPAEEDSVLEKLGERKPCNSQPSELSSETS
FT -> LPEPKDKILETPQKMTEKSESKTPGEGKKEDKSRMAEPMKGYMRPTKSRGLTPLLP
FT KSTIQEQERHKQLKSA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032071"
FT VAR_SEQ 441..631
FT /note="ETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETEIAPAKDV
FT APSTVKEVGLLKDMSPLSETEMALGKDVTPPPETEVVLIKNVCLPPEMEVALTEDQVPA
FT LKTEAPLAKDGVLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLESL
FT QDVGQSAAPTFMISPETVTGT -> TEEAVLNQAPQQKKAVRRALSECSHLSVPPAVNL
FT ADKYPELPAREEPSSGLLPPPSSPMPSPTPGKLGAPAMKRSMTVGEEQTASYKLSPGKL
FT PILSTKEIPPFICEEPVAKKREELAHFSNSSSNSGKKELGTAGLYLHSKLEQIPEGSSK
FT EKGQEDFSETRIDSCSQVCQRGEKQPGQTALA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032072"
FT VAR_SEQ 558..730
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003200"
FT VAR_SEQ 635..666
FT /note="CSLPAEEDSVLEKLGERKPCNSQPSELSSETS -> EIEVTATQSTPSFLFE
FT KPPRD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032073"
FT VAR_SEQ 703..716
FT /note="PLATTQPAKTSTSK -> VGARMVVIFYCHNF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032074"
FT VAR_SEQ 717..1152
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032075"
FT VAR_SEQ 939..953
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032076"
FT VAR_SEQ 954..1022
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032077"
FT VAR_SEQ 1088..1152
FT /note="TEGGGSEAPLCPGPPAGEEPAISEAAPEAGAPTSASGLNGHPTLSGGGDQRE
FT AQTLDSQIQETSI -> IETYRLTFRANARARTDHGADIVSRPPHFPGGPNSGSRVLGP
FT LSRAVH (in isoform 6)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_032078"
FT VAR_SEQ 1151..1152
FT /note="SI -> N (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032079"
FT VARIANT 23
FT /note="R -> Q (in dbSNP:rs11711953)"
FT /id="VAR_039566"
FT VARIANT 366
FT /note="P -> L (in dbSNP:rs13097415)"
FT /id="VAR_039567"
FT VARIANT 367
FT /note="S -> P (in dbSNP:rs13096947)"
FT /id="VAR_039568"
FT VARIANT 409
FT /note="D -> G (in dbSNP:rs13076542)"
FT /id="VAR_039569"
FT VARIANT 427
FT /note="S -> Y (in dbSNP:rs1060407)"
FT /evidence="ECO:0000269|PubMed:1718985"
FT /id="VAR_020361"
FT VARIANT 441
FT /note="E -> Q (in dbSNP:rs2230169)"
FT /id="VAR_020362"
FT VARIANT 628
FT /note="V -> I (in dbSNP:rs1137524)"
FT /evidence="ECO:0000269|PubMed:1718985,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT /id="VAR_039570"
FT VARIANT 994
FT /note="I -> V (in dbSNP:rs35736893)"
FT /id="VAR_039571"
FT MUTAGEN 696
FT /note="S->E: No change in microtubule binding; no change in
FT microtubule polymerization activity."
FT /evidence="ECO:0000269|PubMed:10791892"
FT MUTAGEN 787
FT /note="S->E: No change in microtubule binding; reduced
FT microtubule polymerization activity."
FT /evidence="ECO:0000269|PubMed:10791892"
FT CONFLICT 160
FT /note="A -> R (in Ref. 1; AAA59553)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="D -> G (in Ref. 10; CAH18346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="I -> V (in Ref. 10; CAH18346)"
FT /evidence="ECO:0000305"
FT MOD_RES P27816-3:337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683"
FT MOD_RES P27816-3:338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683"
FT MOD_RES P27816-4:28
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P27816-4:269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES P27816-5:803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
SQ SEQUENCE 1152 AA; 121005 MW; 061A69AC18593339 CRC64;
MADLSLADAL TEPSPDIEGE IKRDFIATLE AEAFDDVVGE TVGKTDYIPL LDVDEKTGNS
ESKKKPCSET SQIEDTPSSK PTLLANGGHG VEGSDTTGSP TEFLEEKMAY QEYPNSQNWP
EDTNFCFQPE QVVDPIQTDP FKMYHDDDLA DLVFPSSATA DTSIFAGQND PLKDSYGMSP
CNTAVVPQGW SVEALNSPHS ESFVSPEAVA EPPQPTAVPL ELAKEIEMAS EERPPAQALE
IMMGLKTTDM APSKETEMAL AKDMALATKT EVALAKDMES PTKLDVTLAK DMQPSMESDM
ALVKDMELPT EKEVALVKDV RWPTETDVSS AKNVVLPTET EVAPAKDVTL LKETERASPI
KMDLAPSKDM GPPKENKKET ERASPIKMDL APSKDMGPPK ENKIVPAKDL VLLSEIEVAQ
ANDIISSTEI SSAEKVALSS ETEVALARDM TLPPETNVIL TKDKALPLEA EVAPVKDMAQ
LPETEIAPAK DVAPSTVKEV GLLKDMSPLS ETEMALGKDV TPPPETEVVL IKNVCLPPEM
EVALTEDQVP ALKTEAPLAK DGVLTLANNV TPAKDVPPLS ETEATPVPIK DMEIAQTQKG
ISEDSHLESL QDVGQSAAPT FMISPETVTG TGKKCSLPAE EDSVLEKLGE RKPCNSQPSE
LSSETSGIAR PEEGRPVVSG TGNDITTPPN KELPPSPEKK TKPLATTQPA KTSTSKAKTQ
PTSLPKQPAP TTIGGLNKKP MSLASGLVPA APPKRPAVAS ARPSILPSKD VKPKPIADAK
APEKRASPSK PASAPASRSG SKSTQTVAKT TTAAAVASTG PSSRSPSTLL PKKPTAIKTE
GKPAEVKKMT AKSVPADLSR PKSTSTSSMK KTTTLSGTAP AAGVVPSRVK ATPMPSRPST
TPFIDKKPTS AKPSSTTPRL SRLATNTSAP DLKNVRSKVG STENIKHQPG GGRAKVEKKT
EAAATTRKPE SNAVTKTAGP IASAQKQPAG KVQIVSKKVS YSHIQSKCGS KDNIKHVPGG
GNVQIQNKKV DISKVSSKCG SKANIKHKPG GGDVKIESQK LNFKEKAQAK VGSLDNVGHL
PAGGAVKTEG GGSEAPLCPG PPAGEEPAIS EAAPEAGAPT SASGLNGHPT LSGGGDQREA
QTLDSQIQET SI
