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E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (Antigen NY-CO-7) (CLL-associated antigen KW-8) (Carboxy terminus of Hsp70-interacting protein) (RING-type E3 ubiquitin transferase CHIP) (STIP1 homology and U box-containing protein 1)

 CHIP_HUMAN              Reviewed;         303 AA.
Q9UNE7; A2IDB9; O60526; Q969U2; Q9HBT1;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
22-NOV-2017, entry version 166.
RecName: Full=E3 ubiquitin-protein ligase CHIP {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472};
AltName: Full=Antigen NY-CO-7 {ECO:0000303|PubMed:9610721};
AltName: Full=CLL-associated antigen KW-8 {ECO:0000303|PubMed:12200376};
AltName: Full=Carboxy terminus of Hsp70-interacting protein {ECO:0000303|PubMed:10330192};
AltName: Full=RING-type E3 ubiquitin transferase CHIP {ECO:0000305};
AltName: Full=STIP1 homology and U box-containing protein 1 {ECO:0000312|HGNC:HGNC:11427};
Name=STUB1 {ECO:0000312|HGNC:HGNC:11427};
Synonyms=CHIP {ECO:0000303|PubMed:10330192};
ORFNames=PP1131 {ECO:0000312|EMBL:AAG17211.1};
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 IDENTIFICATION AS
TUMOR-ASSOCIATED ANTIGEN.
TISSUE=Colon carcinoma;
PubMed=9610721;
DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
"Characterization of human colon cancer antigens recognized by
autologous antibodies.";
Int. J. Cancer 76:652-658(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
HSPA8 AND HSPA1A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=10330192; DOI=10.1128/MCB.19.6.4535;
Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y.,
Patterson C.;
"Identification of CHIP, a novel tetratricopeptide repeat-containing
protein that interacts with heat shock proteins and negatively
regulates chaperone functions.";
Mol. Cell. Biol. 19:4535-4545(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION AS
TUMOR-ASSOCIATED ANTIGEN.
PubMed=12200376; DOI=10.1182/blood-2002-02-0513;
Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J.,
Chessia M., Barrett P., Gribben J.G.;
"Identification of tumor-associated antigens in chronic lymphocytic
leukemia by SEREX.";
Blood 100:2123-2131(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Skin;
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).
[9]
PROTEIN SEQUENCE OF 13-30; 56-66; 86-119; 129-140; 155-167; 235-241;
256-263 AND 273-287, PHOSPHORYLATION AT SER-19, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[10]
TISSUE SPECIFICITY.
PubMed=11435423; DOI=10.1074/jbc.M102755200;
Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
"U box proteins as a new family of ubiquitin-protein ligases.";
J. Biol. Chem. 276:33111-33120(2001).
[11]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH HSPA8;
UBE2D1; UBE2D2 AND UBE2D3.
PubMed=11557750; DOI=10.1074/jbc.M101968200;
Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hoehfeld J.,
Patterson C.;
"CHIP is a U-box-dependent E3 ubiquitin ligase: identification of
Hsc70 as a target for ubiquitylation.";
J. Biol. Chem. 276:42938-42944(2001).
[12]
FUNCTION, AND INTERACTION WITH HSP90.
PubMed=11146632; DOI=10.1038/35050618;
Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J.,
Hoehfeld J., Patterson C.;
"The co-chaperone CHIP regulates protein triage decisions mediated by
heat-shock proteins.";
Nat. Cell Biol. 3:93-96(2001).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=15466472; DOI=10.1074/jbc.M406926200;
Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M.,
Patterson C., Pratt W.B., Osawa Y.;
"Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a
chaperone-dependent E3 ligase.";
J. Biol. Chem. 279:52970-52977(2004).
[14]
INTERACTION WITH HSPA1A AND HSPBP1.
PubMed=15215316; DOI=10.1091/mbc.E04-04-0293;
Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and
stimulates the maturation of the cystic fibrosis transmembrane
conductance regulator.";
Mol. Biol. Cell 15:4003-4010(2004).
[15]
INTERACTION WITH BAG2.
PubMed=16169850; DOI=10.1074/jbc.M507986200;
Dai Q., Qian S.B., Li H.-H., McDonough H., Borchers C., Huang D.,
Takayama S., Younger J.M., Ren H.Y., Cyr D.M., Patterson C.;
"Regulation of the cytoplasmic quality control protein degradation
pathway by BAG2.";
J. Biol. Chem. 280:38673-38681(2005).
[16]
INTERACTION WITH UBE2N AND UBE2V1.
PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
Pearl L.H.;
"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
Mol. Cell 20:525-538(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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).
[18]
POLYUBIQUITINATION AT LYS-22; LYS-221 AND LYS-255, AND DOMAIN TPR.
PubMed=18042044; DOI=10.1042/BJ20071338;
Windheim M., Peggie M., Cohen P.;
"Two different classes of E2 ubiquitin-conjugating enzymes are
required for the mono-ubiquitination of proteins and elongation by
polyubiquitin chains with a specific topology.";
Biochem. J. 409:723-729(2008).
[19]
INTERACTION WITH MKKS.
PubMed=18094050; DOI=10.1091/mbc.E07-07-0631;
Hirayama S., Yamazaki Y., Kitamura A., Oda Y., Morito D., Okawa K.,
Kimura H., Cyr D.M., Kubota H., Nagata K.;
"MKKS is a centrosome-shuttling protein degraded by disease-causing
mutations via CHIP-mediated ubiquitination.";
Mol. Biol. Cell 19:899-911(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273,
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]
FUNCTION.
PubMed=19103148; DOI=10.1016/j.abb.2008.12.001;
Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E.,
Correia M.A.;
"CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor
receptor, AMFR) and CHIP E3 ligases.";
Arch. Biochem. Biophys. 483:66-74(2009).
[24]
FUNCTION, 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).
[25]
INTERACTION WITH DNAAF4.
PubMed=19423554; DOI=10.1093/hmg/ddp215;
Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
Kere J.;
"Functional interaction of DYX1C1 with estrogen receptors suggests
involvement of hormonal pathways in dyslexia.";
Hum. Mol. Genet. 18:2802-2812(2009).
[26]
FUNCTION.
PubMed=19567782; DOI=10.1158/1541-7786.MCR-08-0582;
Annamalai B., Liu X., Gopal U., Isaacs J.S.;
"Hsp90 is an essential regulator of EphA2 receptor stability and
signaling: implications for cancer cell migration and metastasis.";
Mol. Cancer Res. 7:1021-1032(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-19, 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-19 AND SER-273, 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-19 AND SER-23, 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]
INTERACTION WITH DNAJB6.
PubMed=22366786; DOI=10.1038/ng.1103;
Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H.,
Screen M., McDonald K., Stajich J.M., Mahjneh I., Vihola A.,
Raheem O., Penttila S., Lehtinen S., Huovinen S., Palmio J., Tasca G.,
Ricci E., Hackman P., Hauser M., Katsanis N., Udd B.;
"Mutations affecting the cytoplasmic functions of the co-chaperone
DNAJB6 cause limb-girdle muscular dystrophy.";
Nat. Genet. 44:450-455(2012).
[33]
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).
[34]
UBIQUITINATION AT LYS-2.
PubMed=23560854; DOI=10.1042/BJ20130244;
Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.;
"Ube2W conjugates ubiquitin to alpha-amino groups of protein N-
termini.";
Biochem. J. 453:137-145(2013).
[35]
FUNCTION, INDUCTION, INTERACTION WITH FOXP3, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-30 AND HIS-260.
PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
"The ubiquitin ligase Stub1 negatively modulates regulatory T cell
suppressive activity by promoting degradation of the transcription
factor Foxp3.";
Immunity 39:272-285(2013).
[36]
FUNCTION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF PRO-269.
PubMed=23990462; DOI=10.1074/jbc.M113.479345;
Matsumura Y., Sakai J., Skach W.R.;
"Endoplasmic reticulum protein quality control is determined by
cooperative interactions between Hsp/c70 protein and the CHIP E3
ligase.";
J. Biol. Chem. 288:31069-31079(2013).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23; SER-25 AND
SER-149, 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).
[38]
FUNCTION, AND INTERACTION WITH SMAD3; HSPA1A; HSPA1B; HSP90AA1 AND
HSP90AB1.
PubMed=24613385; DOI=10.1016/j.bbrc.2014.02.124;
Shang Y., Xu X., Duan X., Guo J., Wang Y., Ren F., He D., Chang Z.;
"Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through
CHIP/Stub1.";
Biochem. Biophys. Res. Commun. 446:387-392(2014).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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).
[40]
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).
[41]
INTERACTION WITH FLCN AND HSP90AA1.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[42]
FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
PubMed=27708256; DOI=10.1038/ncomms12882;
Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K.,
Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J.,
Seok S.H., Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.;
"ARD1-mediated Hsp70 acetylation balances stress-induced protein
refolding and degradation.";
Nat. Commun. 7:12882-12882(2016).
[43]
VARIANTS SCAR16 ILE-130; CYS-147; PHE-165 AND THR-236, AND INVOLVEMENT
IN SCAR16.
PubMed=24312598; DOI=10.1371/journal.pone.0081884;
Shi Y., Wang J., Li J.D., Ren H., Guan W., He M., Yan W., Zhou Y.,
Hu Z., Zhang J., Xiao J., Su Z., Dai M., Wang J., Jiang H., Guo J.,
Zhou Y., Zhang F., Li N., Du J., Xu Q., Hu Y., Pan Q., Shen L.,
Wang G., Xia K., Zhang Z., Tang B.;
"Identification of CHIP as a novel causative gene for autosomal
recessive cerebellar ataxia.";
PLoS ONE 8:E81884-E81884(2013).
[44]
VARIANT SCAR16 MET-246.
PubMed=24113144; DOI=10.1093/hmg/ddt497;
Shi C.H., Schisler J.C., Rubel C.E., Tan S., Song B., McDonough H.,
Xu L., Portbury A.L., Mao C.Y., True C., Wang R.H., Wang Q.Z.,
Sun S.L., Seminara S.B., Patterson C., Xu Y.M.;
"Ataxia and hypogonadism caused by the loss of ubiquitin ligase
activity of the U box protein CHIP.";
Hum. Mol. Genet. 23:1013-1024(2014).
[45]
VARIANTS SCAR16 ASP-79; THR-79; VAL-123 AND THR-240.
PubMed=24742043; DOI=10.1186/1750-1172-9-57;
Synofzik M., Schuele R., Schulze M., Gburek-Augustat J., Schweizer R.,
Schirmacher A., Kraegeloh-Mann I., Gonzalez M., Young P., Zuechner S.,
Schoels L., Bauer P.;
"Phenotype and frequency of STUB1 mutations: next-generation
screenings in Caucasian ataxia and spastic paraplegia cohorts.";
Orphanet J. Rare Dis. 9:57-64(2014).
[46]
VARIANT SCAR16 GLN-145.
PubMed=24719489; DOI=10.1212/WNL.0000000000000416;
Depondt C., Donatello S., Simonis N., Rai M., van Heurck R.,
Abramowicz M., D'Hooghe M., Pandolfo M.;
"Autosomal recessive cerebellar ataxia of adult onset due to STUB1
mutations.";
Neurology 82:1749-1750(2014).
[47]
VARIANTS SCAR16 LYS-28; SER-65 AND MET-246, AND CHARACTERIZATION OF
VARIANTS SCAR16 LYS-28; SER-65 AND MET-246.
PubMed=25258038; DOI=10.1186/s13023-014-0146-0;
Heimdal K., Sanchez-Guixe M., Aukrust I., Bollerslev J., Bruland O.,
Jablonski G.E., Erichsen A.K., Gude E., Koht J.A., Erdal S.,
Fiskerstrand T., Haukanes B.I., Boman H., Bjoerkhaug L.,
Tallaksen C.M., Knappskog P.M., Johansson S.;
"STUB1 mutations in autosomal recessive ataxias - evidence for
mutation-specific clinical heterogeneity.";
Orphanet J. Rare Dis. 9:146-146(2014).
-!- FUNCTION: E3 ubiquitin-protein ligase which targets misfolded
chaperone substrates towards proteasomal degradation. Collaborates
with ATXN3 in the degradation of misfolded chaperone substrates:
ATXN3 restricting the length of ubiquitin chain attached to
STUB1/CHIP substrates and preventing further chain extension.
Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the
activity of several chaperone complexes, including Hsp70, Hsc70
and Hsp90. Mediates transfer of non-canonical short ubiquitin
chains to HSPA8 that have no effect on HSPA8 degradation. Mediates
polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41',
'Lys-61' and 'Lys-81', thereby playing a role in base-excision
repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-
BP1-dependent monoubiquitination and leading to POLB-degradation
by the proteasome. Mediates polyubiquitination of CYP3A4.
Ubiquitinates EPHA2 and may regulate the receptor stability and
activity through proteasomal degradation. Acts as a co-chaperone
for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-
mediated protein degradation (PubMed:27708256). Negatively
regulates the suppressive function of regulatory T-cells (Treg)
during inflammation by mediating the ubiquitination and
degradation of FOXP3 in a HSPA1A/B-dependent manner
(PubMed:23973223). Negatively regulates TGF-beta signaling by
modulating the basal level of SMAD3 via ubiquitin-mediated
degradation (PubMed:24613385). {ECO:0000269|PubMed:10330192,
ECO:0000269|PubMed:11146632, ECO:0000269|PubMed:11557750,
ECO:0000269|PubMed:15466472, ECO:0000269|PubMed:19103148,
ECO:0000269|PubMed:19567782, ECO:0000269|PubMed:19713937,
ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:23990462,
ECO:0000269|PubMed:24613385}.
-!- 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. {ECO:0000269|PubMed:11557750,
ECO:0000269|PubMed:15466472}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with BAG2
(PubMed:16169850). Interacts with E2 ubiquitin conjugating enzymes
UBE2D1, UBE2D2 and UBE2D3 (PubMed:11557750). Detected in a ternary
complex containing STUB1, HSPA1A and HSPBP1 (PubMed:15215316).
Interacts with MKKS (PubMed:18094050). Interacts with DNAAF4
(PubMed:19423554). Interacts with POLB (PubMed:19713937).
Interacts (when monoubiquitinated) with ATXN3. Interacts with
UBE2W. Interacts (via the U-box domain) with the UBE2V2-UBE2N
heterodimer; the complex has a specific 'Lys-63'-linked
polyubiquitination activity (By similarity). Interacts with DNAJB6
(PubMed:22366786). Interacts with FOXP3 (PubMed:23973223).
Interacts with FLCN (PubMed:27353360). Interacts with HSP90AA1
(PubMed:27353360, PubMed:24613385). Interacts with HSP90
(PubMed:11146632). Interacts with UBE2N and UBE2V1
(PubMed:16307917). Interacts (via TPR repeats) with the C-terminal
domain of HSPA1A (PubMed:10330192). Interacts with the non-
acetylated form of HSPA1A and HSPA1B (PubMed:27708256). Interacts
(via TPR repeats) with the C-terminal domain of HSPA8
(PubMed:10330192, PubMed:11557750, PubMed:23990462,
PubMed:27708256). Interacts with SMAD3 and HSP90AB1
(PubMed:24613385). {ECO:0000250|UniProtKB:Q9WUD1,
ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11146632,
ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15215316,
ECO:0000269|PubMed:16169850, ECO:0000269|PubMed:16307917,
ECO:0000269|PubMed:18094050, ECO:0000269|PubMed:19423554,
ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:22366786,
ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:23990462,
ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27353360,
ECO:0000269|PubMed:27708256}.
-!- INTERACTION:
A8K1F4:-; NbExp=2; IntAct=EBI-357085, EBI-9357094;
Q96AP0:ACD; NbExp=2; IntAct=EBI-357085, EBI-717666;
P31749:AKT1; NbExp=5; IntAct=EBI-15687717, EBI-296087;
Q86WG3:ATCAY; NbExp=4; IntAct=EBI-357085, EBI-1783328;
Q99933:BAG1; NbExp=2; IntAct=EBI-357085, EBI-1030678;
O95816:BAG2; NbExp=4; IntAct=EBI-357085, EBI-355275;
O95817:BAG3; NbExp=3; IntAct=EBI-357085, EBI-747185;
Q9NRJ3:CCL28; NbExp=3; IntAct=EBI-357085, EBI-7783254;
P00533:EGFR; NbExp=3; IntAct=EBI-357085, EBI-297353;
Q9BZS1:FOXP3; NbExp=7; IntAct=EBI-357085, EBI-983719;
P07900:HSP90AA1; NbExp=9; IntAct=EBI-357085, EBI-296047;
P08238:HSP90AB1; NbExp=5; IntAct=EBI-357085, EBI-352572;
P08107:HSPA1B; NbExp=5; IntAct=EBI-357085, EBI-629985;
P11142:HSPA8; NbExp=5; IntAct=EBI-357085, EBI-351896;
P11142-1:HSPA8; NbExp=4; IntAct=EBI-15687717, EBI-351908;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-15687717, EBI-5323863;
Q9Y2U5:MAP3K2; NbExp=9; IntAct=EBI-357085, EBI-357393;
P10636:MAPT; NbExp=5; IntAct=EBI-15687717, EBI-366182;
Q96PB7:OLFM3; NbExp=3; IntAct=EBI-357085, EBI-10292253;
Q9BVN2:RUSC1; NbExp=3; IntAct=EBI-357085, EBI-6257312;
Q99757:TXN2; NbExp=3; IntAct=EBI-357085, EBI-2932492;
P61088:UBE2N; NbExp=5; IntAct=EBI-357085, EBI-1052908;
Q7Z7E8:UBE2Q1; NbExp=3; IntAct=EBI-357085, EBI-1783287;
P12504:vif (xeno); NbExp=2; IntAct=EBI-357085, EBI-779991;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10330192,
ECO:0000269|PubMed:23973223}. Nucleus
{ECO:0000269|PubMed:23973223}. Note=Translocates to the nucleus in
response to inflammatory signals in regulatory T-cells (Treg).
{ECO:0000269|PubMed:23973223}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UNE7-1; Sequence=Displayed;
Name=2;
IsoId=Q9UNE7-2; Sequence=VSP_015947;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart,
pancreas, brain and placenta. Detected in kidney, liver and lung.
{ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11435423}.
-!- INDUCTION: Up-regulated by inflammatory signals in regulatory T-
cells (Treg). {ECO:0000269|PubMed:23973223}.
-!- DOMAIN: The U-box domain is required for the ubiquitin protein
ligase activity. {ECO:0000250|UniProtKB:Q9WUD1}.
-!- DOMAIN: The TPR domain is essential for ubiquitination mediated by
UBE2D1. {ECO:0000269|PubMed:18042044}.
-!- PTM: Monoubiquitinated at Lys-2 following cell stress by UBE2W,
promoting the interaction with ATXN3 (By similarity). Auto-
ubiquitinated; mediated by UBE2D1 and UBE2D2. {ECO:0000250,
ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:23560854}.
-!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16)
[MIM:615768]: Spinocerebellar ataxia defines a clinically and
genetically heterogeneous group of cerebellar disorders. Patients
show progressive incoordination of gait and often poor
coordination of hands, speech and eye movements, due to
degeneration of the cerebellum with variable involvement of the
brainstem and spinal cord. SCAR16 is characterized by truncal and
limb ataxia resulting in gait instability. Additionally, patients
may show dysarthria, nystagmus, spasticity of the lower limbs, and
mild peripheral sensory neuropathy. {ECO:0000269|PubMed:24113144,
ECO:0000269|PubMed:24312598, ECO:0000269|PubMed:24719489,
ECO:0000269|PubMed:24742043, ECO:0000269|PubMed:25258038}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Antibodies against STUB1 are found in patients with
chronic lymphocytic leukemia (CLL) and in colorectal cancer
patients.
-----------------------------------------------------------------------
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EMBL; AF039689; AAC18038.1; -; mRNA.
EMBL; AF129085; AAD33400.1; -; mRNA.
EMBL; AF432221; AAL99927.1; -; mRNA.
EMBL; AF217968; AAG17211.1; -; mRNA.
EMBL; AE006464; AAK61242.1; -; Genomic_DNA.
EMBL; Z92544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85758.1; -; Genomic_DNA.
EMBL; BC007545; AAH07545.1; -; mRNA.
EMBL; BC017178; AAH17178.1; -; mRNA.
EMBL; BC022788; AAH22788.1; -; mRNA.
EMBL; BC063617; AAH63617.1; -; mRNA.
CCDS; CCDS10419.1; -. [Q9UNE7-1]
CCDS; CCDS76797.1; -. [Q9UNE7-2]
RefSeq; NP_001280126.1; NM_001293197.1. [Q9UNE7-2]
RefSeq; NP_005852.2; NM_005861.3. [Q9UNE7-1]
UniGene; Hs.592081; -.
PDB; 4KBQ; X-ray; 2.91 A; A/B=21-154.
PDBsum; 4KBQ; -.
ProteinModelPortal; Q9UNE7; -.
SMR; Q9UNE7; -.
BioGrid; 115563; 270.
CORUM; Q9UNE7; -.
DIP; DIP-29752N; -.
IntAct; Q9UNE7; 147.
MINT; MINT-1132706; -.
STRING; 9606.ENSP00000219548; -.
iPTMnet; Q9UNE7; -.
PhosphoSitePlus; Q9UNE7; -.
BioMuta; STUB1; -.
DMDM; 78099173; -.
EPD; Q9UNE7; -.
PaxDb; Q9UNE7; -.
PeptideAtlas; Q9UNE7; -.
PRIDE; Q9UNE7; -.
DNASU; 10273; -.
Ensembl; ENST00000219548; ENSP00000219548; ENSG00000103266. [Q9UNE7-1]
Ensembl; ENST00000564370; ENSP00000456875; ENSG00000103266. [Q9UNE7-2]
Ensembl; ENST00000565677; ENSP00000457228; ENSG00000103266. [Q9UNE7-2]
GeneID; 10273; -.
KEGG; hsa:10273; -.
UCSC; uc002cit.4; human. [Q9UNE7-1]
CTD; 10273; -.
DisGeNET; 10273; -.
EuPathDB; HostDB:ENSG00000103266.10; -.
GeneCards; STUB1; -.
H-InvDB; HIX0012661; -.
HGNC; HGNC:11427; STUB1.
HPA; CAB037202; -.
HPA; CAB037209; -.
HPA; HPA041222; -.
HPA; HPA043531; -.
MalaCards; STUB1; -.
MIM; 607207; gene.
MIM; 615768; phenotype.
neXtProt; NX_Q9UNE7; -.
OpenTargets; ENSG00000103266; -.
Orphanet; 1173; Cerebellar ataxia - hypogonadism.
PharmGKB; PA36227; -.
eggNOG; KOG4642; Eukaryota.
eggNOG; ENOG410ZC2R; LUCA.
GeneTree; ENSGT00730000111218; -.
HOGENOM; HOG000163725; -.
HOVERGEN; HBG053046; -.
InParanoid; Q9UNE7; -.
KO; K09561; -.
OMA; TNATYFT; -.
OrthoDB; EOG091G0FJB; -.
PhylomeDB; Q9UNE7; -.
TreeFam; TF313937; -.
BRENDA; 2.3.2.B10; 2681.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q9UNE7; -.
SIGNOR; Q9UNE7; -.
UniPathway; UPA00143; -.
ChiTaRS; STUB1; human.
GeneWiki; STUB1; -.
GenomeRNAi; 10273; -.
PRO; PR:Q9UNE7; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103266; -.
CleanEx; HS_STUB1; -.
ExpressionAtlas; Q9UNE7; baseline and differential.
Genevisible; Q9UNE7; HS.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0031371; C:ubiquitin conjugating enzyme complex; TAS:HGNC.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030544; F:Hsp70 protein binding; IDA:HGNC.
GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
GO; GO:0051787; F:misfolded protein binding; IDA:BHF-UCL.
GO; GO:0030674; F:protein binding, bridging; TAS:HGNC.
GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
GO; GO:0046332; F:SMAD binding; IDA:HGNC.
GO; GO:0030911; F:TPR domain binding; IDA:HGNC.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:1904264; F:ubiquitin protein ligase activity involved in ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISS:UniProtKB.
GO; GO:0071218; P:cellular response to misfolded protein; IDA:BHF-UCL.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; IDA:BHF-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:HGNC.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:HGNC.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0051604; P:protein maturation; TAS:HGNC.
GO; GO:0000209; P:protein polyubiquitination; IDA:HGNC.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:BHF-UCL.
GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0031943; P:regulation of glucocorticoid metabolic process; IDA:HGNC.
GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IDA:HGNC.
Gene3D; 1.25.40.10; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF04564; U-box; 1.
SMART; SM00028; TPR; 3.
SMART; SM00504; Ubox; 1.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
PROSITE; PS51698; U_BOX; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
Isopeptide bond; Neurodegeneration; Nucleus; Phosphoprotein;
Reference proteome; Repeat; TPR repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 303 E3 ubiquitin-protein ligase CHIP.
/FTId=PRO_0000106329.
REPEAT 26 59 TPR 1.
REPEAT 60 93 TPR 2.
REPEAT 95 127 TPR 3.
DOMAIN 226 300 U-box.
MOD_RES 19 19 Phosphoserine.
{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,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.9}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
CROSSLNK 2 2 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23560854}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18042044}.
CROSSLNK 221 221 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18042044}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18042044}.
VAR_SEQ 1 72 Missing (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_015947.
VARIANT 28 28 E -> K (in SCAR16; reduces protein level;
does not reduce ubiquitin ligase activity
and autoubiquitination).
{ECO:0000269|PubMed:25258038}.
/FTId=VAR_072348.
VARIANT 65 65 N -> S (in SCAR16; reduces protein level;
reduces ubiquitin ligase activity; does
not change autoubiquitination;
dbSNP:rs690016544).
{ECO:0000269|PubMed:25258038}.
/FTId=VAR_072349.
VARIANT 79 79 A -> D (in SCAR16; dbSNP:rs587777347).
{ECO:0000269|PubMed:24742043}.
/FTId=VAR_071293.
VARIANT 79 79 A -> T (in SCAR16; dbSNP:rs587777346).
{ECO:0000269|PubMed:24742043}.
/FTId=VAR_071294.
VARIANT 123 123 L -> V (in SCAR16; dbSNP:rs587777344).
{ECO:0000269|PubMed:24742043}.
/FTId=VAR_071295.
VARIANT 130 130 N -> I (in SCAR16; dbSNP:rs587777341).
{ECO:0000269|PubMed:24312598}.
/FTId=VAR_071296.
VARIANT 145 145 K -> Q (in SCAR16; dbSNP:rs146251364).
{ECO:0000269|PubMed:24719489}.
/FTId=VAR_072350.
VARIANT 147 147 W -> C (in SCAR16; dbSNP:rs587777342).
{ECO:0000269|PubMed:24312598}.
/FTId=VAR_071297.
VARIANT 165 165 L -> F (in SCAR16; dbSNP:rs587777340).
{ECO:0000269|PubMed:24312598}.
/FTId=VAR_071298.
VARIANT 236 236 S -> T (in SCAR16).
{ECO:0000269|PubMed:24312598}.
/FTId=VAR_071299.
VARIANT 240 240 M -> T (in SCAR16; dbSNP:rs587777345).
{ECO:0000269|PubMed:24742043}.
/FTId=VAR_071300.
VARIANT 246 246 T -> M (in SCAR16; inhibits ubiquitin
ligase activity and autoubiquitination;
dbSNP:rs587777343).
{ECO:0000269|PubMed:24113144,
ECO:0000269|PubMed:25258038}.
/FTId=VAR_071301.
MUTAGEN 30 30 K->A: Loss of interaction with FOXP3 and
its ability to ubiquitinate FOXP3. Loss
of interaction with SMAD3, HSPA8,
HSP90AA1 and HSP90AB1.
{ECO:0000269|PubMed:23973223,
ECO:0000269|PubMed:24613385}.
MUTAGEN 260 260 H->Q: Loss of ability to ubiquitinate
FOXP3. {ECO:0000269|PubMed:23973223}.
MUTAGEN 269 269 P->A: Abolishes E3 ligase activity.
{ECO:0000269|PubMed:23990462}.
CONFLICT 52 52 A -> V (in Ref. 2; AAD33400).
{ECO:0000305}.
CONFLICT 272 272 R -> G (in Ref. 1; AAC18038).
{ECO:0000305}.
CONFLICT 280 280 L -> F (in Ref. 1; AAC18038).
{ECO:0000305}.
HELIX 26 38 {ECO:0000244|PDB:4KBQ}.
HELIX 42 55 {ECO:0000244|PDB:4KBQ}.
HELIX 60 72 {ECO:0000244|PDB:4KBQ}.
HELIX 76 89 {ECO:0000244|PDB:4KBQ}.
HELIX 94 106 {ECO:0000244|PDB:4KBQ}.
HELIX 110 126 {ECO:0000244|PDB:4KBQ}.
HELIX 134 147 {ECO:0000244|PDB:4KBQ}.
TURN 148 151 {ECO:0000244|PDB:4KBQ}.
SEQUENCE 303 AA; 34856 MW; 7E7D6568B17070BF CRC64;
MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA
VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA
YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC
QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM
REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV
EDY


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