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Microtubule-associated protein 4 (MAP-4)

 MAP4_HUMAN              Reviewed;        1152 AA.
P27816; Q13082; Q59FT2; Q68D74; Q6ZUW9; Q86V26; Q96A76; Q96NS9;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 3.
25-OCT-2017, entry version 178.
RecName: Full=Microtubule-associated protein 4;
Short=MAP-4;
Name=MAP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS TYR-427 AND
ILE-628.
PubMed=1718985;
West R.R., Tenbarge K.M., Olmsted J.B.;
"A model for microtubule-associated protein 4 structure. Domains
defined by comparisons of human, mouse, and bovine sequences.";
J. Biol. Chem. 266:21886-21896(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=7857940; DOI=10.1021/bi00007a025;
Chapin S.J., Lue C.M., Yu M.T., Bulinski J.C.;
"Differential expression of alternatively spliced forms of MAP4: a
repertoire of structurally different microtubule-binding domains.";
Biochemistry 34:2289-2301(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-996 (ISOFORM 4).
TISSUE=Cerebellum, and Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
TISSUE=Eye, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-23; 322-356; 436-448; 561-574; 727-738; 810-832;
853-862; 872-888 AND 923-933, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Prostatic adenocarcinoma;
Bienvenut W.V., Ramsay A., Leung H.Y., Zebisch A., Kolch W.;
Submitted (OCT-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 102-1152 (ISOFORM 1).
TISSUE=Brain;
PubMed=1905296;
Chapin S.J., Bulinski J.C.;
"Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
contains a domain homologous to the microtubule-binding domains of
neuronal MAP2 and tau.";
J. Cell Sci. 98:27-36(1991).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1151 (ISOFORM 5).
TISSUE=Liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
PHOSPHORYLATION AT SER-696 AND SER-787, FUNCTION, AND MUTAGENESIS OF
SER-696 AND SER-787.
PubMed=10791892; DOI=10.1247/csf.25.33;
Kitazawa H., Iida J., Uchida A., Haino-Fukushima K., Itoh T.J.,
Hotani H., Ookata K., Murofushi H., Bulinski J.C., Kishimoto T.,
Hisanaga S.;
"Ser787 in the proline-rich region of human MAP4 is a critical
phosphorylation site that reduces its activity to promote tubulin
polymerization.";
Cell Struct. Funct. 25:33-39(2000).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[13]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[14]
INTERACTION WITH SEPT2.
PubMed=16093351; DOI=10.1091/mbc.E05-03-0267;
Kremer B.E., Haystead T., Macara I.G.;
"Mammalian septins regulate microtubule stability through interaction
with the microtubule-binding protein MAP4.";
Mol. Biol. Cell 16:4648-4659(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; THR-521; THR-571
AND SER-1073, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269
(ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571 AND SER-827, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-384, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-337 AND SER-338 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-99; SER-280;
SER-358; SER-384; SER-507; THR-521; THR-571; SER-580; THR-585;
SER-636; SER-825; SER-941 AND SER-1151, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-28 AND SER-269 (ISOFORM 4), VARIANT [LARGE SCALE
ANALYSIS] ILE-628, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1073, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; THR-521; THR-571;
THR-585 AND SER-1151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-14; SER-280; THR-282; THR-354; SER-358;
THR-380; SER-384; SER-507; SER-510; THR-521; THR-526; THR-571;
THR-585; SER-624; SER-636; SER-787; SER-797; SER-825; SER-928;
SER-941; SER-1073 AND SER-1151, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-269 (ISOFORM 4), VARIANT [LARGE SCALE ANALYSIS] ILE-628,
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; THR-282; SER-358;
SER-384; SER-507; THR-521; THR-526; THR-571; SER-636; SER-787;
SER-941; THR-942; SER-1000; SER-1073; SER-1145 AND SER-1151,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803 (ISOFORM 5), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-60; SER-280;
SER-358; SER-384; SER-440; THR-442; SER-507; SER-510; THR-521;
THR-571; SER-580; THR-585; SER-636; SER-696; SER-713; SER-723;
SER-787; SER-825; SER-853; SER-928 AND SER-1073, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-358; SER-384;
SER-636 AND SER-1000, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-269, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-838, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Non-neuronal microtubule-associated protein. Promotes
microtubule assembly. {ECO:0000269|PubMed:10791892}.
-!- SUBUNIT: Interacts with SEPT2; this interaction impedes tubulin-
binding. Interacts with TRAF3IP1 (By similarity).
{ECO:0000250|UniProtKB:P27546, ECO:0000269|PubMed:16093351}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-715255, EBI-389883;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P27816-1; Sequence=Displayed;
Name=2;
IsoId=P27816-2; Sequence=VSP_003200;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=P27816-3; Sequence=VSP_032065, VSP_032068, VSP_032072,
VSP_032073, VSP_032074, VSP_032075;
Note=Contains a phosphoserine at position 337. Contains a
phosphoserine at position 338. {ECO:0000244|PubMed:17693683};
Name=4;
IsoId=P27816-4; Sequence=VSP_032066, VSP_032067, VSP_032069,
VSP_032070, VSP_032076;
Note=Contains a phosphothreonine at position 28. Contains a
phosphoserine at position 269. {ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231};
Name=5;
IsoId=P27816-5; Sequence=VSP_032071, VSP_032077, VSP_032079;
Note=Contains a phosphoserine at position 803.
{ECO:0000244|PubMed:21406692};
Name=6;
IsoId=P27816-6; Sequence=VSP_032078;
Note=No experimental confirmation available.;
Name=7;
IsoId=P27816-7; Sequence=VSP_043240, VSP_043241;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by
MAP/microtubule affinity-regulating kinase (MARK1 or MARK2),
causing detachment from microtubules, and their disassembly (By
similarity). Phosphorylation on Ser-787 negatively regulates MAP4
activity to promote microtubule assembly. Isoform 3 is
phosphorylated on Ser-337 and Ser-338. {ECO:0000250,
ECO:0000269|PubMed:10791892}.
-!- SEQUENCE CAUTION:
Sequence=BAD92614.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAP4ID44410ch3p21.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M64571; AAA59553.1; -; mRNA.
EMBL; U19727; AAA67361.1; -; mRNA.
EMBL; AK054696; BAB70795.1; -; mRNA.
EMBL; AK125245; BAC86099.1; -; mRNA.
EMBL; AB209377; BAD92614.1; ALT_INIT; mRNA.
EMBL; AC124916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC139667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64839.1; -; Genomic_DNA.
EMBL; BC008715; AAH08715.1; -; mRNA.
EMBL; BC012794; AAH12794.1; -; mRNA.
EMBL; BC015149; AAH15149.1; -; mRNA.
EMBL; BC051843; AAH51843.1; -; mRNA.
EMBL; CR749544; CAH18346.1; -; mRNA.
CCDS; CCDS33750.1; -. [P27816-1]
CCDS; CCDS46818.1; -. [P27816-6]
CCDS; CCDS46821.1; -. [P27816-7]
PIR; A41206; A33183.
RefSeq; NP_001127836.1; NM_001134364.1. [P27816-6]
RefSeq; NP_002366.2; NM_002375.4. [P27816-1]
RefSeq; NP_112147.2; NM_030885.3. [P27816-7]
UniGene; Hs.517949; -.
ProteinModelPortal; P27816; -.
SMR; P27816; -.
BioGrid; 110306; 62.
IntAct; P27816; 27.
MINT; MINT-1425668; -.
STRING; 9606.ENSP00000353375; -.
DrugBank; DB01248; Docetaxel.
DrugBank; DB01229; Paclitaxel.
iPTMnet; P27816; -.
PhosphoSitePlus; P27816; -.
SwissPalm; P27816; -.
BioMuta; MAP4; -.
DMDM; 269849673; -.
EPD; P27816; -.
MaxQB; P27816; -.
PaxDb; P27816; -.
PeptideAtlas; P27816; -.
PRIDE; P27816; -.
DNASU; 4134; -.
Ensembl; ENST00000360240; ENSP00000353375; ENSG00000047849. [P27816-1]
Ensembl; ENST00000395734; ENSP00000379083; ENSG00000047849. [P27816-6]
Ensembl; ENST00000434267; ENSP00000402767; ENSG00000047849. [P27816-7]
Ensembl; ENST00000439356; ENSP00000397414; ENSG00000047849. [P27816-7]
GeneID; 4134; -.
KEGG; hsa:4134; -.
UCSC; uc003csb.3; human. [P27816-1]
CTD; 4134; -.
DisGeNET; 4134; -.
EuPathDB; HostDB:ENSG00000047849.21; -.
GeneCards; MAP4; -.
HGNC; HGNC:6862; MAP4.
HPA; HPA038149; -.
HPA; HPA038150; -.
MIM; 157132; gene.
neXtProt; NX_P27816; -.
OpenTargets; ENSG00000047849; -.
PharmGKB; PA30608; -.
eggNOG; ENOG410IG6M; Eukaryota.
eggNOG; ENOG4111J07; LUCA.
GeneTree; ENSGT00530000063491; -.
HOGENOM; HOG000139406; -.
HOVERGEN; HBG006323; -.
InParanoid; P27816; -.
KO; K10431; -.
PhylomeDB; P27816; -.
TreeFam; TF316358; -.
SIGNOR; P27816; -.
ChiTaRS; MAP4; human.
GeneWiki; MAP4; -.
GenomeRNAi; 4134; -.
PMAP-CutDB; P27816; -.
PRO; PR:P27816; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000047849; -.
CleanEx; HS_MAP4; -.
ExpressionAtlas; P27816; baseline and differential.
Genevisible; P27816; HS.
GO; GO:0005930; C:axoneme; IDA:GO_Central.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
GO; GO:0072686; C:mitotic spindle; IDA:MGI.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
GO; GO:0051301; P:cell division; IMP:MGI.
GO; GO:0051294; P:establishment of spindle orientation; IMP:MGI.
GO; GO:0051012; P:microtubule sliding; IMP:MGI.
GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IMP:GO_Central.
GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
InterPro; IPR001084; MAP_tubulin-bd_rpt.
Pfam; PF00418; Tubulin-binding; 4.
PROSITE; PS00229; TAU_MAP_1; 4.
PROSITE; PS51491; TAU_MAP_2; 4.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Isopeptide bond; Microtubule;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 1152 Microtubule-associated protein 4.
/FTId=PRO_0000072751.
REPEAT 248 261 1.
REPEAT 262 275 2.
REPEAT 276 289 3.
REPEAT 290 303 4.
REPEAT 304 317 5.
REPEAT 318 331 6.
REPEAT 332 345 7.
REPEAT 346 351 8; truncated.
REPEAT 352 377 26 residues 1.
REPEAT 378 403 26 residues 2.
REPEAT 408 421 9.
REPEAT 422 433 10.
REPEAT 434 447 11.
REPEAT 448 461 12.
REPEAT 462 475 13.
REPEAT 476 489 14.
REPEAT 490 503 15.
REPEAT 504 517 16.
REPEAT 532 545 17.
REPEAT 923 953 Tau/MAP 1.
REPEAT 992 1022 Tau/MAP 2.
REPEAT 1023 1053 Tau/MAP 3.
REPEAT 1054 1085 Tau/MAP 4.
REGION 248 545 17 X 14 AA tandem repeats.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000250|UniProtKB:P27546}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 282 282 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 354 354 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 380 380 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 442 442 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 521 521 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 526 526 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 571 571 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 585 585 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000250|UniProtKB:P27546}.
MOD_RES 687 687 Phosphothreonine.
{ECO:0000250|UniProtKB:P27546}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10791892}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10791892}.
MOD_RES 797 797 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 827 827 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 928 928 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 942 942 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1000 1000 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 1073 1073 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1145 1145 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1151 1151 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 838 838 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 151 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032065.
VAR_SEQ 1 82 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032066.
VAR_SEQ 83 221 LLANGGHGVEGSDTTGSPTEFLEEKMAYQEYPNSQNWPEDT
NFCFQPEQVVDPIQTDPFKMYHDDDLADLVFPSSATADTSI
FAGQNDPLKDSYGMSPCNTAVVPQGWSVEALNSPHSESFVS
PEAVAEPPQPTAVPLE -> METTGDQGIEGMAYMDENRNI
TFTCPRTPSELINKSSPLEVLGSAACEKLPTPTPQVVKEGD
SFPDT (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032067.
VAR_SEQ 98 99 GS -> EA (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043240.
VAR_SEQ 100 1152 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043241.
VAR_SEQ 152 437 LVFPSSATADTSIFAGQNDPLKDSYGMSPCNTAVVPQGWSV
EALNSPHSESFVSPEAVAEPPQPTAVPLELAKEIEMASEER
PPAQALEIMMGLKTTDMAPSKETEMALAKDMALATKTEVAL
AKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVA
LVKDVRWPTETDVSSAKNVVLPTETEVAPAKDVTLLKETER
ASPIKMDLAPSKDMGPPKENKKETERASPIKMDLAPSKDMG
PPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVA
-> MSLSDKQTASLTAAYGQLSKGKPAECRMDSPKEISQAG
FEWQRTEGKLNEIGLNVSMDGQPKDGLVKNASFLEQNKLCF
FEGKLDKELSIEMQDKDCQEASGHLESRYVISETCHPLEGN
SVHQKTSEFHLGLIEGPDKNKTIPVQGKVAGKNGLETKSQS
DLDFPGAADIPTRYVKEQETSVWNPSFHPVAQGSLGSREAT
PGEMENSITPGCPVIGVVNDNSEQLKCESPLLVSLAHPAPI
IEHSPTTIPPITMVFTQEHLNASCHIRDHDKELEK (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032068.
VAR_SEQ 225 271 EIEMASEERPPAQALEIMMGLKTTDMAPSKETEMALAKDMA
LATKTE -> NGQEIAPAQISKSLMVDNYTKDGVPGQERPK
GPSAVVPSTSTGG (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032069.
VAR_SEQ 275 666 AKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVA
LVKDVRWPTETDVSSAKNVVLPTETEVAPAKDVTLLKETER
ASPIKMDLAPSKDMGPPKENKKETERASPIKMDLAPSKDMG
PPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVAL
SSETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMA
QLPETEIAPAKDVAPSTVKEVGLLKDMSPLSETEMALGKDV
TPPPETEVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKD
GVLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGIS
EDSHLESLQDVGQSAAPTFMISPETVTGTGKKCSLPAEEDS
VLEKLGERKPCNSQPSELSSETS -> PITTAIETVNIHGD
HSLKNKAELADSMKNEAGIDEGHVIGESESVHSGASKHSVE
KVTELAKGHLLPGVPVEDQSLPGEARALEGYADRGNFPAHP
VNEEKETKEGSVAVQIPDLLEDKAQKLSFCEDQNAQDRNSK
GSDSLNKKVDLTLLSPKSENDKLKEISLACKITELESVSLP
TPEIQSDFLHSKVEAPPSEVADTLVIMTASKGVRLPEPKDK
ILETPQKMTEKSESKTPGEGKKEDKSRMAEPMKGYMRPTKS
RGLTPLLPKSTIQEQERHKQLKSA (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032070.
VAR_SEQ 322 666 WPTETDVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKM
DLAPSKDMGPPKENKKETERASPIKMDLAPSKDMGPPKENK
IVPAKDLVLLSEIEVAQANDIISSTEISSAEKVALSSETEV
ALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETE
IAPAKDVAPSTVKEVGLLKDMSPLSETEMALGKDVTPPPET
EVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKDGVLTLA
NNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLE
SLQDVGQSAAPTFMISPETVTGTGKKCSLPAEEDSVLEKLG
ERKPCNSQPSELSSETS -> LPEPKDKILETPQKMTEKSE
SKTPGEGKKEDKSRMAEPMKGYMRPTKSRGLTPLLPKSTIQ
EQERHKQLKSA (in isoform 5).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032071.
VAR_SEQ 441 631 ETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQL
PETEIAPAKDVAPSTVKEVGLLKDMSPLSETEMALGKDVTP
PPETEVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKDGV
LTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISED
SHLESLQDVGQSAAPTFMISPETVTGT -> TEEAVLNQAP
QQKKAVRRALSECSHLSVPPAVNLADKYPELPAREEPSSGL
LPPPSSPMPSPTPGKLGAPAMKRSMTVGEEQTASYKLSPGK
LPILSTKEIPPFICEEPVAKKREELAHFSNSSSNSGKKELG
TAGLYLHSKLEQIPEGSSKEKGQEDFSETRIDSCSQVCQRG
EKQPGQTALA (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032072.
VAR_SEQ 558 730 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_003200.
VAR_SEQ 635 666 CSLPAEEDSVLEKLGERKPCNSQPSELSSETS -> EIEVT
ATQSTPSFLFEKPPRD (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032073.
VAR_SEQ 703 716 PLATTQPAKTSTSK -> VGARMVVIFYCHNF (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032074.
VAR_SEQ 717 1152 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032075.
VAR_SEQ 939 953 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032076.
VAR_SEQ 954 1022 Missing (in isoform 5).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032077.
VAR_SEQ 1088 1152 TEGGGSEAPLCPGPPAGEEPAISEAAPEAGAPTSASGLNGH
PTLSGGGDQREAQTLDSQIQETSI -> IETYRLTFRANAR
ARTDHGADIVSRPPHFPGGPNSGSRVLGPLSRAVH (in
isoform 6). {ECO:0000303|Ref.4}.
/FTId=VSP_032078.
VAR_SEQ 1151 1152 SI -> N (in isoform 5).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032079.
VARIANT 23 23 R -> Q (in dbSNP:rs11711953).
/FTId=VAR_039566.
VARIANT 366 366 P -> L (in dbSNP:rs13097415).
/FTId=VAR_039567.
VARIANT 367 367 S -> P (in dbSNP:rs13096947).
/FTId=VAR_039568.
VARIANT 409 409 D -> G (in dbSNP:rs13076542).
/FTId=VAR_039569.
VARIANT 427 427 S -> Y (in dbSNP:rs1060407).
{ECO:0000269|PubMed:1718985}.
/FTId=VAR_020361.
VARIANT 441 441 E -> Q (in dbSNP:rs2230169).
/FTId=VAR_020362.
VARIANT 628 628 V -> I (in dbSNP:rs1137524).
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:1718985}.
/FTId=VAR_039570.
VARIANT 994 994 I -> V (in dbSNP:rs35736893).
/FTId=VAR_039571.
MUTAGEN 696 696 S->E: No change in microtubule binding;
no change in microtubule polymerization
activity. {ECO:0000269|PubMed:10791892}.
MUTAGEN 787 787 S->E: No change in microtubule binding;
reduced microtubule polymerization
activity. {ECO:0000269|PubMed:10791892}.
CONFLICT 160 160 A -> R (in Ref. 1; AAA59553).
{ECO:0000305}.
CONFLICT 319 319 D -> G (in Ref. 10; CAH18346).
{ECO:0000305}.
CONFLICT 1109 1109 I -> V (in Ref. 10; CAH18346).
{ECO:0000305}.
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


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EIAAB35342 Fam82b,Microtubule-associated protein,Mouse,mRMD-1,Mus musculus,Protein FAM82B,Regulator of microtubule dynamics protein 1,RMD-1
EIAAB25789 Cardiac zipper protein,CAZIP,Homo sapiens,Human,KIAA0774,Microtubule plus-end tracking protein TIP150,Microtubule-associated tumor suppressor candidate 2,MTUS2,TIP150,Tracking protein of 150 kDa
EIAAB25788 Cardiac zipper protein,Cazip,Kiaa0774,Microtubule plus-end tracking protein TIP150,Microtubule-associated tumor suppressor candidate 2 homolog,Mouse,Mtus2,Mus musculus,Tip150,Tracking protein of 150 k
EIAAB12889 Echinoderm microtubule-associated protein-like 5-like,Echinoderm microtubule-associated protein-like 6,EMAP-6,EML5L,EML6,Homo sapiens,Human
EIAAB12890 Echinoderm microtubule-associated protein-like 5-like,Echinoderm microtubule-associated protein-like 6,EMAP-6,Eml5l,Eml6,Mouse,Mus musculus
6242-0039 RABBIT ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN 2 (+ TAU), Product Type Polyclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN 2 , Target Species Bovine, Host Rabbit, Format Purified, 0.2 ml
SCH-6242-0039 RABBIT ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN 2 (+ TAU), Product Type Polyclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN 2 , Target Species Bovine, Host Rabbit, Format Purified, 0.2 ml
6242-0206 MOUSE ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN TAU, Product Type Monoclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN TAU, Target Species Bovine, Host Mouse, Format Ascites, Isotypes 0.1 ml
SCH-6242-0206 MOUSE ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN TAU, Product Type Monoclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN TAU, Target Species Bovine, Host Mouse, Format Ascites, Isotypes 0.1 ml
EIAAB44014 CEV14,Clonal evolution-related gene on chromosome 14 protein,GMAP-210,Golgi-associated microtubule-binding protein 210,Homo sapiens,Human,Thyroid receptor-interacting protein 11,TR-interacting protein
SEQ641Ra ELISA Kit for Echinoderm Microtubule Associated Protein Like Protein 2 (EML2) Rattus norvegicus (Rat) 96T
orb81209 Human Microtubule-Associated Protein Light Chain Alpha protein Proteins 5
bs-1847P Peptides: MAP1A_Mtap1a(microtubule associated protein 1A) Protein Length:12-25 amino acids. 200ug lyophilized
bs-1369P Peptides: MAP-2(microtubule associated protein 2) Protein Length:12-25 amino acids. 200ug lyophilized
E-EL-M1121 Mouse MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-Ch2091 Chicken MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-P1842 Porcine MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-MK1019 Monkey MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-H0948 Human MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
SEQ641Hu ELISA Kit for Echinoderm Microtubule Associated Protein Like Protein 2 (EML2) Homo sapiens (Human) 96T
E84641Ra ELISA Kit for Echinoderm Microtubule Associated Protein Like Protein 2 (EML2) Organism: Rattus norvegicus (Rat) 96T
EIAAB35353 Cerebral protein 10,FAM82A2,FAM82C,Homo sapiens,hRMD-3,hucep-10,Human,Protein FAM82A2,Protein FAM82C,Protein tyrosine phosphatase-interacting protein 51,PTPIP51,Regulator of microtubule dynamics prote
MC-734 MAP 2a,b,c (Microtubule Associated Protein) 100 ug
MC-734 MAP 2a,b,c (Microtubule Associated Protein) 100 ug
bs-1534P Peptides: MAP1LC3A(microtubule-associated protein 1 light chain 3) Protein Length:12-25 amino acids. 200ug lyophilized


 

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