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E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)

 HUWE1_HUMAN             Reviewed;        4374 AA.
Q7Z6Z7; O15029; Q4G2Z2; Q5H961; Q6P4D0; Q8NG67; Q9BUI0; Q9HCJ4;
Q9NSL6; Q9P0A9;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 3.
10-OCT-2018, entry version 172.
RecName: Full=E3 ubiquitin-protein ligase HUWE1;
EC=2.3.2.26;
AltName: Full=ARF-binding protein 1;
Short=ARF-BP1;
AltName: Full=HECT, UBA and WWE domain-containing protein 1;
AltName: Full=HECT-type E3 ubiquitin transferase HUWE1;
AltName: Full=Homologous to E6AP carboxyl terminus homologous protein 9;
Short=HectH9;
AltName: Full=Large structure of UREB1;
Short=LASU1;
AltName: Full=Mcl-1 ubiquitin ligase E3;
Short=Mule;
AltName: Full=Upstream regulatory element-binding protein 1;
Short=URE-B1;
Short=URE-binding protein 1;
Name=HUWE1; Synonyms=KIAA0312, KIAA1578, UREB1; ORFNames=HSPC272;
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), FUNCTION, INTERACTION WITH
CDKN2A, AND MUTAGENESIS OF CYS-4341.
PubMed=15989956; DOI=10.1016/j.cell.2005.03.037;
Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.;
"ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor.";
Cell 121:1071-1083(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
CYS-4341.
PubMed=15989957; DOI=10.1016/j.cell.2005.06.009;
Zhong Q., Gao W., Du F., Wang X.;
"Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
polyubiquitination of Mcl-1 and regulates apoptosis.";
Cell 121:1085-1095(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=15767685; DOI=10.1128/MCB.25.7.2819-2831.2005;
Liu Z., Oughtred R., Wing S.S.;
"Characterization of E3Histone, a novel testis ubiquitin protein
ligase which ubiquitinates histones.";
Mol. Cell. Biol. 25:2819-2831(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 959-4374 (ISOFORM 3).
TISSUE=Brain;
Miyazaki K., Okamoto Y., Sakamoto M., Kato C., Ozaki T., Watanabe K.,
Nakagawara A.;
"Homo sapiens LASU1 (large structure of UREB1) mRNA, complete cds.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1166-4374 (ISOFORM 2).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[7]
SEQUENCE REVISION TO 2310.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1246-2418.
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2451-4374.
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3953-4374.
TISSUE=Ovary, and Placenta;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 4029-4374.
Kim J.W., Lee Y., Hong Y.M., Hong M., Choe I.S.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4067-4374.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4320-4374.
TISSUE=Melanoma;
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).
[14]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF TYR-4268 AND
CYS-4341.
PubMed=15567145; DOI=10.1016/j.bbrc.2004.11.004;
Yoon S.Y., Lee Y., Kim J.H., Chung A.-S., Joo J.H., Kim C.-N.,
Kim N.-S., Choe I.S., Kim J.W.;
"Over-expression of human UREB1 in colorectal cancer: HECT domain of
human UREB1 inhibits the activity of tumor suppressor p53 protein.";
Biochem. Biophys. Res. Commun. 326:7-17(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2362, 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 SER-1395; SER-1907;
SER-2362; SER-2887 AND SER-2918, 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]
FUNCTION, AND INTERACTION WITH CDC6.
PubMed=17567951; DOI=10.1091/mbc.E07-02-0173;
Hall J.R., Kow E., Nevis K.R., Lu C.K., Luce K.S., Zhong Q.,
Cook J.G.;
"Cdc6 stability is regulated by the Huwe1 ubiquitin ligase after DNA
damage.";
Mol. Biol. Cell 18:3340-3350(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
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-2362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
FUNCTION, INTERACTION WITH MYCN, AND MUTAGENESIS OF CYS-4341.
PubMed=18488021; DOI=10.1038/ncb1727;
Zhao X., Heng J.I.-T., Guardavaccaro D., Jiang R., Pagano M.,
Guillemot F., Iavarone A., Lasorella A.;
"The HECT-domain ubiquitin ligase Huwe1 controls neural
differentiation and proliferation by destabilizing the N-Myc
oncoprotein.";
Nat. Cell Biol. 10:643-653(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1368; SER-1907;
SER-2362; SER-2365; SER-2887; SER-3662; SER-3919; THR-3924 AND
THR-3927, 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).
[24]
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).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POLB.
PubMed=19713937; DOI=10.1038/emboj.2009.243;
Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J.,
Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G.,
Dianov G.L.;
"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair.";
EMBO J. 28:3207-3215(2009).
[26]
FUNCTION, AND INTERACTION WITH PA2G4.
PubMed=19037095; DOI=10.1091/mbc.E08-09-0983;
Liu Z., Oh S.M., Okada M., Liu X., Cheng D., Peng J., Brat D.J.,
Sun S.Y., Zhou W., Gu W., Ye K.;
"Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor.";
Mol. Biol. Cell 20:757-768(2009).
[27]
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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1370; SER-1395;
SER-1907; SER-2362; SER-2391; SER-2595; SER-2619; THR-2751; SER-2887;
SER-3116; SER-3752; SER-3757; SER-3808; SER-3816; SER-3919 AND
THR-3924, 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1368;
SER-1395; THR-1722; SER-1907; SER-2362; SER-2365; SER-2595; SER-3127;
SER-3662; SER-3757; SER-3760 AND SER-3919, 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).
[30]
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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1907; SER-2362
AND SER-2365, 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).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1368; SER-1382;
SER-1395; THR-1722; SER-1907; SER-2266; SER-2362; SER-2365; SER-2527;
SER-2532; SER-2535; THR-2554; SER-2595; SER-2887; SER-2888; THR-2889;
SER-3116; SER-3117; SER-3122; SER-3127; SER-3135; SER-3555; SER-3662;
SER-3752; SER-3757; SER-3760; SER-3808; SER-3816; SER-3827 AND
THR-3830, 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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740; SER-1368; SER-1395;
THR-2035; SER-2584; SER-2826; SER-2833; SER-2835; SER-2861; SER-3757;
SER-3759; SER-3816; SER-3827; SER-3906; SER-3919; THR-3924 AND
THR-3927, 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).
[34]
STRUCTURE BY NMR OF 1317-1356.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-074, a human UBA domain.";
Submitted (FEB-2009) to the PDB data bank.
[35]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4005-4374.
Structural genomics consortium (SGC);
"Hect domain of human huwe1/mule.";
Submitted (MAY-2009) to the PDB data bank.
[36]
VARIANTS MRXST HIS-2981; TRP-4013 AND CYS-4187, INVOLVEMENT IN MRX17,
AND INVOLVEMENT IN MRXST.
PubMed=18252223; DOI=10.1016/j.ajhg.2007.11.002;
Froyen G., Corbett M., Vandewalle J., Jarvela I., Lawrence O.,
Meldrum C., Bauters M., Govaerts K., Vandeleur L., Van Esch H.,
Chelly J., Sanlaville D., van Bokhoven H., Ropers H.-H.,
Laumonnier F., Ranieri E., Schwartz C.E., Abidi F., Tarpey P.S.,
Futreal P.A., Whibley A., Raymond F.L., Stratton M.R., Fryns J.-P.,
Scott R., Peippo M., Sipponen M., Partington M., Mowat D., Field M.,
Hackett A., Marynen P., Turner G., Gecz J.;
"Submicroscopic duplications of the hydroxysteroid dehydrogenase
HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental
retardation.";
Am. J. Hum. Genet. 82:432-443(2008).
[37]
VARIANT ASP-950.
PubMed=23092983; DOI=10.1038/tp.2012.102;
Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B.,
Cohen D., Faudet A., Bouteiller D., Gilleron M., Jacquette A.,
Whalen S., Afenjar A., Perisse D., Laurent C., Dupuits C., Gautier C.,
Gerard M., Huguet G., Caillet S., Leheup B., Leboyer M., Gillberg C.,
Delorme R., Bourgeron T., Brice A., Depienne C.;
"Analysis of the chromosome X exome in patients with autism spectrum
disorders identified novel candidate genes, including TMLHE.";
Transl. Psychiatry 2:E179-E179(2012).
-!- FUNCTION: E3 ubiquitin-protein ligase which mediates
ubiquitination and subsequent proteasomal degradation of target
proteins. Regulates apoptosis by catalyzing the polyubiquitination
and degradation of MCL1. Mediates monoubiquitination of DNA
polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby
playing a role in base-excision repair. Also ubiquitinates the
p53/TP53 tumor suppressor and core histones including H1, H2A,
H2B, H3 and H4. Binds to an upstream initiator-like sequence in
the preprodynorphin gene. Regulates neural differentiation and
proliferation by catalyzing the polyubiquitination and degradation
of MYCN. May regulate abundance of CDC6 after DNA damage by
polyubiquitinating and targeting CDC6 to degradation. Mediates
polyubiquitination of isoform 2 of PA2G4.
{ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685,
ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957,
ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021,
ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with isoform p14ARF of CDKN2A which strongly
inhibits HUWE1 ubiquitin ligase activity. Interacts with MYCN,
POLB and CDC6. Interacts with isoform 2 of PA2G4.
{ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:17567951,
ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095,
ECO:0000269|PubMed:19713937}.
-!- INTERACTION:
Q8N726:CDKN2A; NbExp=5; IntAct=EBI-625934, EBI-625922;
P04792:HSPB1; NbExp=3; IntAct=EBI-625934, EBI-352682;
Q07820:MCL1; NbExp=6; IntAct=EBI-625934, EBI-1003422;
P20393:NR1D1; NbExp=3; IntAct=EBI-625934, EBI-2811738;
P04637:TP53; NbExp=3; IntAct=EBI-625934, EBI-366083;
Q13107:USP4; NbExp=4; IntAct=EBI-625934, EBI-723290;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19713937}.
Nucleus {ECO:0000269|PubMed:19713937}. Note=Mainly expressed in
the cytoplasm of most tissues, except in the nucleus of
spermatogonia, primary spermatocytes and neuronal cells (By
similarity). Predominantly cytosolic or perinuclear in some
colorectal carcinoma cells. {ECO:0000250|UniProtKB:Q7TMY8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=LASU1, Large structure of UREB1;
IsoId=Q7Z6Z7-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z6Z7-2; Sequence=VSP_011146;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7Z6Z7-3; Sequence=VSP_015272;
-!- TISSUE SPECIFICITY: Weakly expressed in heart, brain and placenta
but not in other tissues. Expressed in a number of cell lines,
predominantly in those from colorectal carcinomas.
{ECO:0000269|PubMed:15567145}.
-!- DOMAIN: The HECT domain mediates inhibition of the transcriptional
activity of p53.
-!- PTM: Phosphorylated on tyrosine; phosphorylation is probably
required for its ability to inhibit TP53 transactivation.
{ECO:0000250|UniProtKB:Q7TMY8}.
-!- DISEASE: Mental retardation, X-linked, syndromic, Turner type
(MRXST) [MIM:300706]: A syndrome characterized by the association
of mental retardation with macrocephaly and variable contractures.
{ECO:0000269|PubMed:18252223}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Mental retardation, X-linked 17 (MRX17) [MIM:300705]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:18252223}.
Note=The gene represented in this entry is involved in disease
pathogenesis. A chromosomal microduplication involving HSD17B10
and HUWE1 has been found in patients with mental retardation.
-!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC62492.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF28950.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAF28950.1; Type=Frameshift; Positions=4356; Evidence={ECO:0000305};
Sequence=BAB13404.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA, contains the C-terminal part of ATP5ME.; Evidence={ECO:0000305};
Sequence=BAC06833.1; Type=Frameshift; Positions=982, 1055; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY772009; AAV90838.1; -; mRNA.
EMBL; DQ097177; AAY98258.1; -; mRNA.
EMBL; AY929612; AAX24125.1; -; mRNA.
EMBL; AL592046; CAI39580.1; -; Genomic_DNA.
EMBL; Z94044; CAI39580.1; JOINED; Genomic_DNA.
EMBL; Z97054; CAI39580.1; JOINED; Genomic_DNA.
EMBL; Z94044; CAI42354.1; -; Genomic_DNA.
EMBL; AL592046; CAI42354.1; JOINED; Genomic_DNA.
EMBL; Z97054; CAI42354.1; JOINED; Genomic_DNA.
EMBL; Z97054; CAI42654.1; -; Genomic_DNA.
EMBL; AL592046; CAI42654.1; JOINED; Genomic_DNA.
EMBL; Z94044; CAI42654.1; JOINED; Genomic_DNA.
EMBL; AB071605; BAC06833.1; ALT_FRAME; mRNA.
EMBL; AB002310; BAA20771.3; -; mRNA.
EMBL; AB046798; BAB13404.1; ALT_SEQ; mRNA.
EMBL; AF161390; AAF28950.1; ALT_SEQ; mRNA.
EMBL; BC002602; AAH02602.2; -; mRNA.
EMBL; BC063505; AAH63505.1; -; mRNA.
EMBL; AF057569; AAC62492.1; ALT_INIT; mRNA.
EMBL; CR456813; CAG33094.1; -; mRNA.
EMBL; AL162050; CAB82393.1; -; mRNA.
CCDS; CCDS35301.1; -. [Q7Z6Z7-1]
PIR; T47165; T47165.
RefSeq; NP_113584.3; NM_031407.6. [Q7Z6Z7-1]
RefSeq; XP_005262022.1; XM_005261965.3. [Q7Z6Z7-1]
UniGene; Hs.136905; -.
PDB; 2EKK; NMR; -; A=1317-1356.
PDB; 2MUL; NMR; -; A=2951-3003.
PDB; 3G1N; X-ray; 2.60 A; A/B=4005-4374.
PDB; 3H1D; X-ray; 1.89 A; A=3993-4374.
PDB; 5C6H; X-ray; 2.05 A; B/D/F/H/J/L/N/P/R/T/V/X=1969-1994.
PDB; 5LP8; X-ray; 2.70 A; A/B=3951-4374.
PDB; 6FYH; X-ray; 2.91 A; A=4255-4374.
PDBsum; 2EKK; -.
PDBsum; 2MUL; -.
PDBsum; 3G1N; -.
PDBsum; 3H1D; -.
PDBsum; 5C6H; -.
PDBsum; 5LP8; -.
PDBsum; 6FYH; -.
ProteinModelPortal; Q7Z6Z7; -.
SMR; Q7Z6Z7; -.
BioGrid; 115385; 479.
CORUM; Q7Z6Z7; -.
DIP; DIP-34362N; -.
ELM; Q7Z6Z7; -.
IntAct; Q7Z6Z7; 90.
MINT; Q7Z6Z7; -.
STRING; 9606.ENSP00000262854; -.
CarbonylDB; Q7Z6Z7; -.
iPTMnet; Q7Z6Z7; -.
PhosphoSitePlus; Q7Z6Z7; -.
BioMuta; HUWE1; -.
DMDM; 73915353; -.
EPD; Q7Z6Z7; -.
MaxQB; Q7Z6Z7; -.
PaxDb; Q7Z6Z7; -.
PeptideAtlas; Q7Z6Z7; -.
PRIDE; Q7Z6Z7; -.
ProteomicsDB; 69472; -.
ProteomicsDB; 69473; -. [Q7Z6Z7-2]
ProteomicsDB; 69474; -. [Q7Z6Z7-3]
Ensembl; ENST00000262854; ENSP00000262854; ENSG00000086758. [Q7Z6Z7-1]
Ensembl; ENST00000342160; ENSP00000340648; ENSG00000086758. [Q7Z6Z7-1]
Ensembl; ENST00000612484; ENSP00000479451; ENSG00000086758. [Q7Z6Z7-3]
GeneID; 10075; -.
KEGG; hsa:10075; -.
UCSC; uc033eew.2; human. [Q7Z6Z7-1]
CTD; 10075; -.
DisGeNET; 10075; -.
EuPathDB; HostDB:ENSG00000086758.15; -.
GeneCards; HUWE1; -.
HGNC; HGNC:30892; HUWE1.
HPA; CAB022718; -.
HPA; HPA002548; -.
MalaCards; HUWE1; -.
MIM; 300697; gene.
MIM; 300705; phenotype.
MIM; 300706; phenotype.
neXtProt; NX_Q7Z6Z7; -.
OpenTargets; ENSG00000086758; -.
Orphanet; 85328; X-linked intellectual disability, Turner type.
PharmGKB; PA128394567; -.
eggNOG; KOG0939; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00850000132302; -.
HOVERGEN; HBG080254; -.
InParanoid; Q7Z6Z7; -.
KO; K10592; -.
OMA; GDLYHWI; -.
OrthoDB; EOG091G01V1; -.
PhylomeDB; Q7Z6Z7; -.
TreeFam; TF323417; -.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; HUWE1; human.
EvolutionaryTrace; Q7Z6Z7; -.
GeneWiki; HUWE1; -.
GenomeRNAi; 10075; -.
PRO; PR:Q7Z6Z7; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000086758; Expressed in 239 organ(s), highest expression level in lung.
ExpressionAtlas; Q7Z6Z7; baseline and differential.
Genevisible; Q7Z6Z7; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006284; P:base-excision repair; IMP:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0016574; P:histone ubiquitination; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
CDD; cd00078; HECTc; 1.
Gene3D; 3.30.720.50; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR025527; DUF4414.
InterPro; IPR010309; E3_Ub_ligase_DUF908.
InterPro; IPR010314; E3_Ub_ligase_DUF913.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR004170; WWE-dom.
InterPro; IPR037197; WWE_dom_sf.
Pfam; PF14377; DUF4414; 1.
Pfam; PF06012; DUF908; 1.
Pfam; PF06025; DUF913; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00627; UBA; 1.
Pfam; PF02825; WWE; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00165; UBA; 1.
SUPFAM; SSF117839; SSF117839; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS50030; UBA; 1.
PROSITE; PS50918; WWE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Differentiation; Disease mutation; DNA damage; DNA repair;
DNA-binding; Mental retardation; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 4374 E3 ubiquitin-protein ligase HUWE1.
/FTId=PRO_0000120340.
DOMAIN 1316 1355 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 1370 1389 UIM. {ECO:0000305}.
DOMAIN 1603 1680 WWE. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
DOMAIN 4038 4374 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
COMPBIAS 2295 2469 Glu-rich.
COMPBIAS 2427 2490 Asp-rich.
COMPBIAS 3483 3550 Thr-rich.
ACT_SITE 4341 4341 Glycyl thioester intermediate.
MOD_RES 648 648 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TMY8}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TMY8}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1084 1084 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1368 1368 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1370 1370 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1382 1382 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1395 1395 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1722 1722 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1907 1907 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2035 2035 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2266 2266 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2267 2267 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q7TMY8}.
MOD_RES 2362 2362 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2365 2365 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2391 2391 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2527 2527 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2532 2532 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2535 2535 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2554 2554 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2584 2584 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2595 2595 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2619 2619 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2751 2751 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2826 2826 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2833 2833 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2835 2835 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2861 2861 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2887 2887 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2888 2888 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2889 2889 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2918 2918 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 3116 3116 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 3117 3117 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3122 3122 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3127 3127 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 3135 3135 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3149 3149 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q7TMY8}.
MOD_RES 3555 3555 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3662 3662 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 3752 3752 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 3757 3757 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 3759 3759 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 3760 3760 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 3808 3808 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 3816 3816 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 3827 3827 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 3830 3830 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3906 3906 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 3919 3919 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 3924 3924 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 3927 3927 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 4271 4271 Phosphotyrosine.
{ECO:0000250|UniProtKB:P51593}.
VAR_SEQ 982 990 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_015272.
VAR_SEQ 3016 3031 Missing (in isoform 2).
{ECO:0000303|PubMed:9205841}.
/FTId=VSP_011146.
VARIANT 483 483 N -> S (in dbSNP:rs41307640).
/FTId=VAR_061986.
VARIANT 950 950 V -> D (found in patients with autism
spectrum disorders; unknown pathological
significance).
{ECO:0000269|PubMed:23092983}.
/FTId=VAR_076253.
VARIANT 2981 2981 R -> H (in MRXST; dbSNP:rs121918526).
{ECO:0000269|PubMed:18252223}.
/FTId=VAR_045670.
VARIANT 4013 4013 R -> W (in MRXST; dbSNP:rs121918525).
{ECO:0000269|PubMed:18252223}.
/FTId=VAR_045671.
VARIANT 4187 4187 R -> C (in MRXST; dbSNP:rs121918527).
{ECO:0000269|PubMed:18252223}.
/FTId=VAR_045672.
MUTAGEN 4268 4268 Y->S: Loss of activity.
{ECO:0000269|PubMed:15567145}.
MUTAGEN 4341 4341 C->A,D: Loss of activity.
{ECO:0000269|PubMed:15567145,
ECO:0000269|PubMed:15989956,
ECO:0000269|PubMed:15989957,
ECO:0000269|PubMed:18488021}.
CONFLICT 1111 1111 K -> N (in Ref. 5; BAC06833).
{ECO:0000305}.
CONFLICT 1124 1124 P -> L (in Ref. 1; AAV90838 and 5;
BAC06833). {ECO:0000305}.
CONFLICT 1190 1190 D -> H (in Ref. 5; BAC06833).
{ECO:0000305}.
CONFLICT 1962 1962 Missing (in Ref. 6; BAA20771).
{ECO:0000305}.
CONFLICT 2525 2525 H -> Y (in Ref. 5; BAC06833 and 9;
AAF28950). {ECO:0000305}.
CONFLICT 4022 4022 R -> L (in Ref. 10; AAH02602).
{ECO:0000305}.
HELIX 1319 1329 {ECO:0000244|PDB:2EKK}.
HELIX 1332 1341 {ECO:0000244|PDB:2EKK}.
HELIX 1345 1353 {ECO:0000244|PDB:2EKK}.
HELIX 1976 1991 {ECO:0000244|PDB:5C6H}.
HELIX 2958 2960 {ECO:0000244|PDB:2MUL}.
HELIX 2970 2975 {ECO:0000244|PDB:2MUL}.
HELIX 2978 2988 {ECO:0000244|PDB:2MUL}.
HELIX 3952 3972 {ECO:0000244|PDB:5LP8}.
TURN 3977 3979 {ECO:0000244|PDB:5LP8}.
HELIX 3983 3991 {ECO:0000244|PDB:5LP8}.
HELIX 3994 4008 {ECO:0000244|PDB:3H1D}.
TURN 4009 4011 {ECO:0000244|PDB:3H1D}.
STRAND 4016 4021 {ECO:0000244|PDB:3H1D}.
HELIX 4023 4025 {ECO:0000244|PDB:3H1D}.
HELIX 4026 4034 {ECO:0000244|PDB:3H1D}.
HELIX 4041 4043 {ECO:0000244|PDB:3H1D}.
STRAND 4044 4050 {ECO:0000244|PDB:3H1D}.
HELIX 4061 4072 {ECO:0000244|PDB:3H1D}.
HELIX 4076 4078 {ECO:0000244|PDB:3H1D}.
STRAND 4080 4083 {ECO:0000244|PDB:3H1D}.
TURN 4085 4087 {ECO:0000244|PDB:3G1N}.
STRAND 4088 4093 {ECO:0000244|PDB:3H1D}.
HELIX 4095 4099 {ECO:0000244|PDB:3G1N}.
HELIX 4103 4120 {ECO:0000244|PDB:3H1D}.
HELIX 4130 4137 {ECO:0000244|PDB:3H1D}.
HELIX 4143 4145 {ECO:0000244|PDB:3H1D}.
HELIX 4146 4149 {ECO:0000244|PDB:3H1D}.
HELIX 4151 4162 {ECO:0000244|PDB:3H1D}.
HELIX 4165 4167 {ECO:0000244|PDB:3H1D}.
STRAND 4168 4170 {ECO:0000244|PDB:3H1D}.
STRAND 4172 4175 {ECO:0000244|PDB:3H1D}.
TURN 4176 4178 {ECO:0000244|PDB:3H1D}.
STRAND 4181 4183 {ECO:0000244|PDB:3H1D}.
HELIX 4186 4189 {ECO:0000244|PDB:3H1D}.
STRAND 4193 4197 {ECO:0000244|PDB:3H1D}.
TURN 4200 4202 {ECO:0000244|PDB:3H1D}.
HELIX 4203 4215 {ECO:0000244|PDB:3H1D}.
HELIX 4217 4219 {ECO:0000244|PDB:3H1D}.
HELIX 4220 4233 {ECO:0000244|PDB:3H1D}.
HELIX 4236 4239 {ECO:0000244|PDB:3H1D}.
HELIX 4244 4252 {ECO:0000244|PDB:3H1D}.
HELIX 4259 4264 {ECO:0000244|PDB:3H1D}.
STRAND 4266 4271 {ECO:0000244|PDB:3H1D}.
HELIX 4276 4287 {ECO:0000244|PDB:3H1D}.
HELIX 4290 4301 {ECO:0000244|PDB:3H1D}.
STRAND 4302 4304 {ECO:0000244|PDB:3H1D}.
HELIX 4311 4313 {ECO:0000244|PDB:3H1D}.
STRAND 4317 4320 {ECO:0000244|PDB:3H1D}.
STRAND 4323 4328 {ECO:0000244|PDB:3H1D}.
STRAND 4337 4339 {ECO:0000244|PDB:3H1D}.
HELIX 4340 4342 {ECO:0000244|PDB:3H1D}.
STRAND 4344 4348 {ECO:0000244|PDB:3H1D}.
HELIX 4353 4365 {ECO:0000244|PDB:3H1D}.
STRAND 4370 4372 {ECO:0000244|PDB:5LP8}.
SEQUENCE 4374 AA; 481891 MW; FA9D3A7712F6393B CRC64;
MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR
FDGILADAGQ TVENMSWMLV CDRPEREQLK MLLLAVLNFT ALLIEYSFSR HLYSSIEHLT
TLLASSDMQV VLAVLNLLYV FSKRSNYITR LGSDKRTPLL TRLQHLAESW GGKENGFGLA
ECCRDLHMMK YPPSATTLHF EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM
ESLTKMYSIP KDKQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI
LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT GTASYHGFLP
VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG EALVSCGMME ALLKVIKFLG
DEQDQITFVT RAVRVVDLIT NLDMAAFQSH SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ
RPNTTQEGEE METDMDGVQC IPQRAALLKS MLNFLKKAIQ DPAFSDGIRH VMDGSLPTSL
KHIISNAEYY GPSLFLLATE VVTVFVFQEP SLLSSLQDNG LTDVMLHALL IKDVPATREV
LGSLPNVFSA LCLNARGLQS FVQCQPFERL FKVLLSPDYL PAMRRRRSSD PLGDTASNLG
SAVDELMRHQ PTLKTDATTA IIKLLEEICN LGRDPKYICQ KPSIQKADGT ATAPPPRSNH
AAEEASSEDE EEEEVQAMQS FNSTQQNETE PNQQVVGTEE RIPIPLMDYI LNVMKFVESI
LSNNTTDDHC QEFVNQKGLL PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV
LQEGLLQLDS ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQAT PLLHALTAAH
AYIMMFVHTC RVGQSEIRSI SVNQWGSQLG LSVLSKLSQL YCSLVWESTV LLSLCTPNSL
PSGCEFGQAD MQKLVPKDEK AGTTQGGKRS DGEQDGAAGS MDASTQGLLE GIGLDGDTLA
PMETDEPTAS DSKGKSKITP AMAARIKQIK PLLSASSRLG RALAELFGLL VKLCVGSPVR
QRRSHHAAST TTAPTPAARS TASALTKLLT KGLSWQPPPY TPTPRFRLTF FICSVGFTSP
MLFDERKYPY HLMLQKFLCS GGHNALFETF NWALSMGGKV PVSEGLEHSD LPDGTGEFLD
AWLMLVEKMV NPTTVLESPH SLPAKLPGGV QNFPQFSALR FLVVTQKAAF TCIKNLWNRK
PLKVYGGRMA ESMLAILCHI LRGEPVIRER LSKEKEGSRG EEDTGQEEGG SRREPQVNQQ
QLQQLMDMGF TREHAMEALL NTSTMEQATE YLLTHPPPIM GGVVRDLSMS EEDQMMRAIA
MSLGQDIPMD QRAESPEEVA CRKEEEERKA REKQEEEEAK CLEKFQDADP LEQDELHTFT
DTMLPGCFHL LDELPDTVYR VCDLIMTAIK RNGADYRDMI LKQVVNQVWE AADVLIKAAL
PLTTSDTKTV SEWISQMATL PQASNLATRI LLLTLLFEEL KLPCAWVVES SGILNVLIKL
LEVVQPCLQA AKEQKEVQTP KWITPVLLLI DFYEKTAISS KRRAQMTKYL QSNSNNWRWF
DDRSGRWCSY SASNNSTIDS AWKSGETSVR FTAGRRRYTV QFTTMVQVNE ETGNRRPVML
TLLRVPRLNK NSKNSNGQEL EKTLEESKEM DIKRKENKGN DTPLALESTN TEKETSLEET
KIGEILIQGL TEDMVTVLIR ACVSMLGVPV DPDTLHATLR LCLRLTRDHK YAMMFAELKS
TRMILNLTQS SGFNGFTPLV TLLLRHIIED PCTLRHTMEK VVRSAATSGA GSTTSGVVSG
SLGSREINYI LRVLGPAACR NPDIFTEVAN CCIRIALPAP RGSGTASDDE FENLRIKGPN
AVQLVKTTPL KPSPLPVIPD TIKEVIYDML NALAAYHAPE EADKSDPKPG VMTQEVGQLL
QDMGDDVYQQ YRSLTRQSSD FDTQSGFSIN SQVFAADGAS TETSASGTSQ GEASTPEESR
DGKKDKEGDR ASEEGKQKGK GSKPLMPTST ILRLLAELVR SYVGIATLIA NYSYTVGQSE
LIKEDCSVLA FVLDHLLPHT QNAEDKDTPA LARLFLASLA AAGSGTDAQV ALVNEVKAAL
GRALAMAEST EKHARLQAVM CIISTIMESC PSTSSFYSSA TAKTQHNGMN NIIRLFLKKG
LVNDLARVPH SLDLSSPNMA NTVNAALKPL ETLSRIVNQP SSLFGSKSAS SKNKSEQDAQ
GASQDSSSNQ QDPGEPGEAE VQEEDHDVTQ TEVADGDIMD GEAETDSVVI AGQPEVLSSQ
EMQVENELED LIDELLERDG GSGNSTIIVS RSGEDESQED VLMDEAPSNL SQASTLQANR
EDSMNILDPE DEEEHTQEED SSGSNEDEDD SQDEEEEEEE DEEDDQEDDE GEEGDEDDDD
DGSEMELDED YPDMNASPLV RFERFDREDD LIIEFDNMFS SATDIPPSPG NIPTTHPLMV
RHADHSSLTL GSGSSTTRLT QGIGRSQRTL RQLTANTGHT IHVHYPGNRQ PNPPLILQRL
LGPSAAADIL QLSSSLPLQS RGRARLLVGN DDVHIIARSD DELLDDFFHD QSTATSQAGT
LSSIPTALTR WTEECKVLDA ESMHDCVSVV KVSIVNHLEF LRDEELEERR EKRRKQLAEE
ETKITDKGKE DKENRDQSAQ CTASKSNDST EQNLSDGTPM PDSYPTTPSS TDAATSESKE
TLGTLQSSQQ QPTLPTPPAL GEVPQELQSP AGEGGSSTQL LMPVEPEELG PTRPSGEAET
TQMELSPAPT ITSLSPERAE DSDALTAVSS QLEGSPMDTS SLASCTLEEA VGDTSAAGSS
EQPRAGSSTP GDAPPAVAEV QGRSDGSGES AQPPEDSSPP ASSESSSTRD SAVAISGADS
RGILEEPLPS TSSEEEDPLA GISLPEGVDP SFLAALPDDI RREVLQNQLG IRPPTRTAPS
TNSSAPAVVG NPGVTEVSPE FLAALPPAIQ EEVLAQQRAE QQRRELAQNA SSDTPMDPVT
FIQTLPSDLR RSVLEDMEDS VLAVMPPDIA AEAQALRREQ EARQRQLMHE RLFGHSSTSA
LSAILRSPAF TSRLSGNRGV QYTRLAVQRG GTFQMGGSSS HNRPSGSNVD TLLRLRGRLL
LDHEALSCLL VLLFVDEPKL NTSRLHRVLR NLCYHAQTRH WVIRSLLSIL QRSSESELCI
ETPKLTTSEE KGKKSSKSCG SSSHENRPLD LLHKMESKSS NQLSWLSVSM DAALGCRTNI
FQIQRSGGRK HTEKHASGGS TVHIHPQAAP VVCRHVLDTL IQLAKVFPSH FTQQRTKETN
CESDRERGNK ACSPCSSQSS SSGICTDFWD LLVKLDNMNV SRKGKNSVKS VPVSAGGEGE
TSPYSLEASP LGQLMNMLSH PVIRRSSLLT EKLLRLLSLI SIALPENKVS EAQANSGSGA
SSTTTATSTT STTTTTAAST TPTPPTAPTP VTSAPALVAA TAISTIVVAA STTVTTPTTA
TTTVSISPTT KGSKSPAKVS DGGSSSTDFK MVSSGLTENQ LQLSVEVLTS HSCSEEGLED
AANVLLQLSR GDSGTRDTVL KLLLNGARHL GYTLCKQIGT LLAELREYNL EQQRRAQCET
LSPDGLPEEQ PQTTKLKGKM QSRFDMAENV VIVASQKRPL GGRELQLPSM SMLTSKTSTQ
KFFLRVLQVI IQLRDDTRRA NKKAKQTGRL GSSGLGSASS IQAAVRQLEA EADAIIQMVR
EGQRARRQQQ AATSESSQSE ASVRREESPM DVDQPSPSAQ DTQSIASDGT PQGEKEKEER
PPELPLLSEQ LSLDELWDML GECLKELEES HDQHAVLVLQ PAVEAFFLVH ATERESKPPV
RDTRESQLAH IKDEPPPLSP APLTPATPSS LDPFFSREPS SMHISSSLPP DTQKFLRFAE
THRTVLNQIL RQSTTHLADG PFAVLVDYIR VLDFDVKRKY FRQELERLDE GLRKEDMAVH
VRRDHVFEDS YRELHRKSPE EMKNRLYIVF EGEEGQDAGG LLREWYMIIS REMFNPMYAL
FRTSPGDRVT YTINPSSHCN PNHLSYFKFV GRIVAKAVYD NRLLECYFTR SFYKHILGKS
VRYTDMESED YHFYQGLVYL LENDVSTLGY DLTFSTEVQE FGVCEVRDLK PNGANILVTE
ENKKEYVHLV CQMRMTGAIR KQLAAFLEGF YEIIPKRLIS IFTEQELELL ISGLPTIDID
DLKSNTEYHK YQSNSIQIQW FWRALRSFDQ ADRAKFLQFV TGTSKVPLQG FAALEGMNGI
QKFQIHRDDR STDRLPSAHT CFNQLDLPAY ESFEKLRHML LLAIQECSEG FGLA


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