CHIP_HUMAN
ID CHIP_HUMAN Reviewed; 303 AA.
AC Q9UNE7; A2IDB9; O60526; Q969U2; Q9HBT1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=E3 ubiquitin-protein ligase CHIP {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472, ECO:0000269|PubMed:24043303};
DE AltName: Full=Antigen NY-CO-7 {ECO:0000303|PubMed:9610721};
DE AltName: Full=CLL-associated antigen KW-8 {ECO:0000303|PubMed:12200376};
DE AltName: Full=Carboxy terminus of Hsp70-interacting protein {ECO:0000303|PubMed:10330192};
DE AltName: Full=RING-type E3 ubiquitin transferase CHIP {ECO:0000305};
DE AltName: Full=STIP1 homology and U box-containing protein 1 {ECO:0000312|HGNC:HGNC:11427};
GN Name=STUB1 {ECO:0000303|PubMed:23973223, ECO:0000312|HGNC:HGNC:11427};
GN Synonyms=CHIP {ECO:0000303|PubMed:10330192};
GN ORFNames=PP1131 {ECO:0000312|EMBL:AAG17211.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION AS
RP TUMOR-ASSOCIATED ANTIGEN.
RC TISSUE=Colon carcinoma;
RX PubMed=9610721;
RX DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by autologous
RT antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HSPA8
RP AND HSPA1A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10330192; DOI=10.1128/mcb.19.6.4535;
RA Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y.,
RA Patterson C.;
RT "Identification of CHIP, a novel tetratricopeptide repeat-containing
RT protein that interacts with heat shock proteins and negatively regulates
RT chaperone functions.";
RL Mol. Cell. Biol. 19:4535-4545(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION AS
RP TUMOR-ASSOCIATED ANTIGEN.
RX PubMed=12200376; DOI=10.1182/blood-2002-02-0513;
RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M.,
RA Barrett P., Gribben J.G.;
RT "Identification of tumor-associated antigens in chronic lymphocytic
RT leukemia by SEREX.";
RL Blood 100:2123-2131(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 13-30; 56-66; 86-119; 129-140; 155-167; 235-241;
RP 256-263 AND 273-287, PHOSPHORYLATION AT SER-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11435423; DOI=10.1074/jbc.m102755200;
RA Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
RT "U box proteins as a new family of ubiquitin-protein ligases.";
RL J. Biol. Chem. 276:33111-33120(2001).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH HSPA8; UBE2D1;
RP UBE2D2 AND UBE2D3.
RX PubMed=11557750; DOI=10.1074/jbc.m101968200;
RA Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hoehfeld J.,
RA Patterson C.;
RT "CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as
RT a target for ubiquitylation.";
RL J. Biol. Chem. 276:42938-42944(2001).
RN [12]
RP FUNCTION, AND INTERACTION WITH HSP90.
RX PubMed=11146632; DOI=10.1038/35050618;
RA Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hoehfeld J.,
RA Patterson C.;
RT "The co-chaperone CHIP regulates protein triage decisions mediated by heat-
RT shock proteins.";
RL Nat. Cell Biol. 3:93-96(2001).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=15466472; DOI=10.1074/jbc.m406926200;
RA Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M., Patterson C.,
RA Pratt W.B., Osawa Y.;
RT "Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-
RT dependent E3 ligase.";
RL J. Biol. Chem. 279:52970-52977(2004).
RN [14]
RP INTERACTION WITH HSPA1A AND HSPBP1.
RX PubMed=15215316; DOI=10.1091/mbc.e04-04-0293;
RA Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
RT "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates
RT the maturation of the cystic fibrosis transmembrane conductance
RT regulator.";
RL Mol. Biol. Cell 15:4003-4010(2004).
RN [15]
RP INTERACTION WITH BAG2.
RX PubMed=16169850; DOI=10.1074/jbc.m507986200;
RA Dai Q., Qian S.B., Li H.-H., McDonough H., Borchers C., Huang D.,
RA Takayama S., Younger J.M., Ren H.Y., Cyr D.M., Patterson C.;
RT "Regulation of the cytoplasmic quality control protein degradation pathway
RT by BAG2.";
RL J. Biol. Chem. 280:38673-38681(2005).
RN [16]
RP INTERACTION WITH UBE2N AND UBE2V1.
RX PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
RA Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
RA Pearl L.H.;
RT "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
RT ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
RL Mol. Cell 20:525-538(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP FUNCTION, INTERACTION WITH UBE4B, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17369820; DOI=10.1038/ncb1554;
RA Janiesch P.C., Kim J., Mouysset J., Barikbin R., Lochmueller H.,
RA Cassata G., Krause S., Hoppe T.;
RT "The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to
RT human myopathy.";
RL Nat. Cell Biol. 9:379-390(2007).
RN [19]
RP POLYUBIQUITINATION AT LYS-22; LYS-221 AND LYS-255, AND DOMAIN TPR.
RX PubMed=18042044; DOI=10.1042/bj20071338;
RA Windheim M., Peggie M., Cohen P.;
RT "Two different classes of E2 ubiquitin-conjugating enzymes are required for
RT the mono-ubiquitination of proteins and elongation by polyubiquitin chains
RT with a specific topology.";
RL Biochem. J. 409:723-729(2008).
RN [20]
RP INTERACTION WITH MKKS.
RX PubMed=18094050; DOI=10.1091/mbc.e07-07-0631;
RA Hirayama S., Yamazaki Y., Kitamura A., Oda Y., Morito D., Okawa K.,
RA Kimura H., Cyr D.M., Kubota H., Nagata K.;
RT "MKKS is a centrosome-shuttling protein degraded by disease-causing
RT mutations via CHIP-mediated ubiquitination.";
RL Mol. Biol. Cell 19:899-911(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP FUNCTION.
RX PubMed=19103148; DOI=10.1016/j.abb.2008.12.001;
RA Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.;
RT "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor
RT receptor, AMFR) and CHIP E3 ligases.";
RL Arch. Biochem. Biophys. 483:66-74(2009).
RN [25]
RP FUNCTION, AND INTERACTION WITH POLB.
RX PubMed=19713937; DOI=10.1038/emboj.2009.243;
RA Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J.,
RA Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L.;
RT "Ubiquitin ligase ARF-BP1/Mule modulates base excision repair.";
RL EMBO J. 28:3207-3215(2009).
RN [26]
RP INTERACTION WITH DNAAF4.
RX PubMed=19423554; DOI=10.1093/hmg/ddp215;
RA Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
RA Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
RA Kere J.;
RT "Functional interaction of DYX1C1 with estrogen receptors suggests
RT involvement of hormonal pathways in dyslexia.";
RL Hum. Mol. Genet. 18:2802-2812(2009).
RN [27]
RP FUNCTION.
RX PubMed=19567782; DOI=10.1158/1541-7786.mcr-08-0582;
RA Annamalai B., Liu X., Gopal U., Isaacs J.S.;
RT "Hsp90 is an essential regulator of EphA2 receptor stability and signaling:
RT implications for cancer cell migration and metastasis.";
RL Mol. Cancer Res. 7:1021-1032(2009).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [33]
RP INTERACTION WITH DNAJB6.
RX PubMed=22366786; DOI=10.1038/ng.1103;
RA Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M.,
RA McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S.,
RA Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P.,
RA Hauser M., Katsanis N., Udd B.;
RT "Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6
RT cause limb-girdle muscular dystrophy.";
RL Nat. Genet. 44:450-455(2012).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [35]
RP UBIQUITINATION AT LYS-2.
RX PubMed=23560854; DOI=10.1042/bj20130244;
RA Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.;
RT "Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini.";
RL Biochem. J. 453:137-145(2013).
RN [36]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-30 AND
RP HIS-260.
RX PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
RA Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J.,
RA Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H.,
RA Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z.,
RA Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A.,
RA Greene M.I., Pardoll D.M., Pan F., Li B.;
RT "The ubiquitin ligase Stub1 negatively modulates regulatory T cell
RT suppressive activity by promoting degradation of the transcription factor
RT Foxp3.";
RL Immunity 39:272-285(2013).
RN [37]
RP FUNCTION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF PRO-269.
RX PubMed=23990462; DOI=10.1074/jbc.m113.479345;
RA Matsumura Y., Sakai J., Skach W.R.;
RT "Endoplasmic reticulum protein quality control is determined by cooperative
RT interactions between Hsp/c70 protein and the CHIP E3 ligase.";
RL J. Biol. Chem. 288:31069-31079(2013).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23; SER-25 AND
RP SER-149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [39]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-260.
RX PubMed=24043303; DOI=10.1128/mcb.00480-13;
RA Ronnebaum S.M., Wu Y., McDonough H., Patterson C.;
RT "The ubiquitin ligase CHIP prevents SirT6 degradation through noncanonical
RT ubiquitination.";
RL Mol. Cell. Biol. 33:4461-4472(2013).
RN [40]
RP FUNCTION, AND INTERACTION WITH SMAD3; HSPA1A; HSPA1B; HSP90AA1 AND
RP HSP90AB1.
RX PubMed=24613385; DOI=10.1016/j.bbrc.2014.02.124;
RA Shang Y., Xu X., Duan X., Guo J., Wang Y., Ren F., He D., Chang Z.;
RT "Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through
RT CHIP/Stub1.";
RL Biochem. Biophys. Res. Commun. 446:387-392(2014).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [42]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [43]
RP INTERACTION WITH FLCN AND HSP90AA1.
RX PubMed=27353360; DOI=10.1038/ncomms12037;
RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [44]
RP FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
RX PubMed=27708256; DOI=10.1038/ncomms12882;
RA Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K.,
RA Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J., Seok S.H.,
RA Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.;
RT "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding
RT and degradation.";
RL Nat. Commun. 7:12882-12882(2016).
RN [45]
RP FUNCTION.
RX PubMed=28813410; DOI=10.1038/nature23669;
RA Mezzadra R., Sun C., Jae L.T., Gomez-Eerland R., de Vries E., Wu W.,
RA Logtenberg M.E.W., Slagter M., Rozeman E.A., Hofland I., Broeks A.,
RA Horlings H.M., Wessels L.F.A., Blank C.U., Xiao Y., Heck A.J.R., Borst J.,
RA Brummelkamp T.R., Schumacher T.N.M.;
RT "Identification of CMTM6 and CMTM4 as PD-L1 protein regulators.";
RL Nature 549:106-110(2017).
RN [46]
RP FUNCTION.
RX PubMed=29883609; DOI=10.1016/j.molcel.2018.05.016;
RA Choi S.W., Park H.H., Kim S., Chung J.M., Noh H.J., Kim S.K., Song H.K.,
RA Lee C.W., Morgan M.J., Kang H.C., Kim Y.S.;
RT "PELI1 selectively targets kinase-active RIP3 for ubiquitylation-dependent
RT proteasomal degradation.";
RL Mol. Cell 70:920-935(2018).
RN [47]
RP INVOLVEMENT IN SCA48.
RX PubMed=30381368; DOI=10.1212/wnl.0000000000006550;
RA Genis D., Ortega-Cubero S., San Nicolas H., Corral J., Gardenyes J.,
RA de Jorge L., Lopez E., Campos B., Lorenzo E., Tonda R., Beltran S.,
RA Negre M., Obon M., Beltran B., Fabregas L., Alemany B., Marquez F.,
RA Ramio-Torrenta L., Gich J., Volpini V., Pastor P.;
RT "Heterozygous STUB1 mutation causes familial ataxia with cognitive
RT affective syndrome (SCA48).";
RL Neurology 91:E1988-E1998(2018).
RN [48]
RP INTERACTION WITH PRMT5.
RX PubMed=33376131; DOI=10.26508/lsa.202000699;
RA Chakrapani B., Khan M.I.K., Kadumuri R.V., Gupta S., Verma M., Awasthi S.,
RA Govindaraju G., Mahesh A., Rajavelu A., Chavali S., Dhayalan A.;
RT "The uncharacterized protein FAM47E interacts with PRMT5 and regulates its
RT functions.";
RL Life. Sci Alliance 4:e202000699-e202000699(2021).
RN [49]
RP VARIANTS SCAR16 ILE-130; CYS-147; PHE-165 AND THR-236, AND INVOLVEMENT IN
RP SCAR16.
RX PubMed=24312598; DOI=10.1371/journal.pone.0081884;
RA Shi Y., Wang J., Li J.D., Ren H., Guan W., He M., Yan W., Zhou Y., Hu Z.,
RA Zhang J., Xiao J., Su Z., Dai M., Wang J., Jiang H., Guo J., Zhou Y.,
RA Zhang F., Li N., Du J., Xu Q., Hu Y., Pan Q., Shen L., Wang G., Xia K.,
RA Zhang Z., Tang B.;
RT "Identification of CHIP as a novel causative gene for autosomal recessive
RT cerebellar ataxia.";
RL PLoS ONE 8:E81884-E81884(2013).
RN [50]
RP VARIANT SCAR16 MET-246.
RX PubMed=24113144; DOI=10.1093/hmg/ddt497;
RA Shi C.H., Schisler J.C., Rubel C.E., Tan S., Song B., McDonough H., Xu L.,
RA Portbury A.L., Mao C.Y., True C., Wang R.H., Wang Q.Z., Sun S.L.,
RA Seminara S.B., Patterson C., Xu Y.M.;
RT "Ataxia and hypogonadism caused by the loss of ubiquitin ligase activity of
RT the U box protein CHIP.";
RL Hum. Mol. Genet. 23:1013-1024(2014).
RN [51]
RP VARIANTS SCAR16 ASP-79; THR-79; VAL-123 AND THR-240.
RX PubMed=24742043; DOI=10.1186/1750-1172-9-57;
RA Synofzik M., Schuele R., Schulze M., Gburek-Augustat J., Schweizer R.,
RA Schirmacher A., Kraegeloh-Mann I., Gonzalez M., Young P., Zuechner S.,
RA Schoels L., Bauer P.;
RT "Phenotype and frequency of STUB1 mutations: next-generation screenings in
RT Caucasian ataxia and spastic paraplegia cohorts.";
RL Orphanet J. Rare Dis. 9:57-64(2014).
RN [52]
RP VARIANT SCAR16 GLN-145.
RX PubMed=24719489; DOI=10.1212/wnl.0000000000000416;
RA Depondt C., Donatello S., Simonis N., Rai M., van Heurck R., Abramowicz M.,
RA D'Hooghe M., Pandolfo M.;
RT "Autosomal recessive cerebellar ataxia of adult onset due to STUB1
RT mutations.";
RL Neurology 82:1749-1750(2014).
RN [53]
RP VARIANTS SCAR16 LYS-28; SER-65 AND MET-246, AND CHARACTERIZATION OF
RP VARIANTS SCAR16 LYS-28; SER-65 AND MET-246.
RX PubMed=25258038; DOI=10.1186/s13023-014-0146-0;
RA Heimdal K., Sanchez-Guixe M., Aukrust I., Bollerslev J., Bruland O.,
RA Jablonski G.E., Erichsen A.K., Gude E., Koht J.A., Erdal S.,
RA Fiskerstrand T., Haukanes B.I., Boman H., Bjoerkhaug L., Tallaksen C.M.,
RA Knappskog P.M., Johansson S.;
RT "STUB1 mutations in autosomal recessive ataxias - evidence for mutation-
RT specific clinical heterogeneity.";
RL Orphanet J. Rare Dis. 9:146-146(2014).
RN [54]
RP VARIANT SER-57.
RX PubMed=33798445; DOI=10.1016/j.ajhg.2021.03.013;
RA Courage C., Oliver K.L., Park E.J., Cameron J.M., Grabinska K.A., Muona M.,
RA Canafoglia L., Gambardella A., Said E., Afawi Z., Baykan B., Brandt C.,
RA di Bonaventura C., Chew H.B., Criscuolo C., Dibbens L.M., Castellotti B.,
RA Riguzzi P., Labate A., Filla A., Giallonardo A.T., Berecki G.,
RA Jackson C.B., Joensuu T., Damiano J.A., Kivity S., Korczyn A., Palotie A.,
RA Striano P., Uccellini D., Giuliano L., Andermann E., Scheffer I.E.,
RA Michelucci R., Bahlo M., Franceschetti S., Sessa W.C., Berkovic S.F.,
RA Lehesjoki A.E.;
RT "Progressive myoclonus epilepsies-Residual unsolved cases have marked
RT genetic heterogeneity including dolichol-dependent protein glycosylation
RT pathway genes.";
RL Am. J. Hum. Genet. 108:722-738(2021).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone
CC substrates towards proteasomal degradation (PubMed:10330192,
CC PubMed:11146632, PubMed:11557750, PubMed:23990462). Collaborates with
CC ATXN3 in the degradation of misfolded chaperone substrates: ATXN3
CC restricting the length of ubiquitin chain attached to STUB1/CHIP
CC substrates and preventing further chain extension (PubMed:10330192,
CC PubMed:11146632, PubMed:11557750, PubMed:23990462). Ubiquitinates NOS1
CC in concert with Hsp70 and Hsp40 (PubMed:15466472). Modulates the
CC activity of several chaperone complexes, including Hsp70, Hsc70 and
CC Hsp90 (PubMed:10330192, PubMed:11146632, PubMed:15466472). Mediates
CC transfer of non-canonical short ubiquitin chains to HSPA8 that have no
CC effect on HSPA8 degradation (PubMed:11557750, PubMed:23990462).
CC Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41',
CC 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair:
CC catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent
CC monoubiquitination and leading to POLB-degradation by the proteasome
CC (PubMed:19713937). Mediates polyubiquitination of CYP3A4
CC (PubMed:19103148). Ubiquitinates EPHA2 and may regulate the receptor
CC stability and activity through proteasomal degradation
CC (PubMed:19567782). Acts as a co-chaperone for HSPA1A and HSPA1B
CC chaperone proteins and promotes ubiquitin-mediated protein degradation
CC (PubMed:27708256). Negatively regulates the suppressive function of
CC regulatory T-cells (Treg) during inflammation by mediating the
CC ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner
CC (PubMed:23973223). Catalyzes monoubiquitination of SIRT6, preventing
CC its degradation by the proteasome (PubMed:24043303). Likely mediates
CC polyubiquitination and down-regulates plasma membrane expression of PD-
CC L1/CD274, an immune inhibitory ligand critical for immune tolerance to
CC self and antitumor immunity (PubMed:28813410). Negatively regulates
CC TGF-beta signaling by modulating the basal level of SMAD3 via
CC ubiquitin-mediated degradation (PubMed:24613385). May regulate myosin
CC assembly in striated muscles together with UBE4B and VCP/p97 by
CC targeting myosin chaperone UNC45B for proteasomal degradation
CC (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its
CC subsequent proteasome-dependent degradation (PubMed:29883609).
CC {ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11146632,
CC ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472,
CC ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:19103148,
CC ECO:0000269|PubMed:19567782, ECO:0000269|PubMed:19713937,
CC ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:23990462,
CC ECO:0000269|PubMed:24043303, ECO:0000269|PubMed:24613385,
CC ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:28813410,
CC ECO:0000269|PubMed:29883609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11557750,
CC ECO:0000269|PubMed:15466472, ECO:0000269|PubMed:24043303};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BAG2
CC (PubMed:16169850). Interacts with E2 ubiquitin conjugating enzymes
CC UBE2D1, UBE2D2 and UBE2D3 (PubMed:11557750). Detected in a ternary
CC complex containing STUB1, HSPA1A and HSPBP1 (PubMed:15215316).
CC Interacts with MKKS (PubMed:18094050). Interacts with DNAAF4
CC (PubMed:19423554). Interacts (when monoubiquitinated) with ATXN3.
CC Interacts with UBE2W. Interacts (via the U-box domain) with the UBE2V2-
CC UBE2N heterodimer; the complex has a specific 'Lys-63'-linked
CC polyubiquitination activity (By similarity). Interacts with DNAJB6
CC (PubMed:22366786). Interacts with FLCN (PubMed:27353360). Interacts
CC with HSP90AA1 (PubMed:27353360, PubMed:24613385). Interacts with HSP90
CC (PubMed:11146632). Interacts with UBE2N and UBE2V1 (PubMed:16307917).
CC Interacts (via TPR repeats) with the C-terminal domain of HSPA1A
CC (PubMed:10330192). Interacts with the non-acetylated form of HSPA1A and
CC HSPA1B (PubMed:27708256). Interacts (via TPR repeats) with the C-
CC terminal domain of HSPA8 (PubMed:10330192, PubMed:11557750,
CC PubMed:23990462, PubMed:27708256). Interacts with SMAD3 and HSP90AB1
CC (PubMed:24613385). Interacts with UBE4B (PubMed:17369820). Interacts
CC with PRMT5 (PubMed:33376131). {ECO:0000250|UniProtKB:Q9WUD1,
CC ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11146632,
CC ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15215316,
CC ECO:0000269|PubMed:16169850, ECO:0000269|PubMed:16307917,
CC ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:18094050,
CC ECO:0000269|PubMed:19423554, ECO:0000269|PubMed:19713937,
CC ECO:0000269|PubMed:22366786, ECO:0000269|PubMed:23990462,
CC ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27353360,
CC ECO:0000269|PubMed:27708256}.
CC -!- INTERACTION:
CC Q9UNE7; P01023: A2M; NbExp=3; IntAct=EBI-357085, EBI-640741;
CC Q9UNE7; Q96AP0: ACD; NbExp=2; IntAct=EBI-357085, EBI-717666;
CC Q9UNE7; P61158: ACTR3; NbExp=3; IntAct=EBI-357085, EBI-351428;
CC Q9UNE7; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-357085, EBI-25928834;
CC Q9UNE7; Q86WG3: ATCAY; NbExp=4; IntAct=EBI-357085, EBI-1783328;
CC Q9UNE7; Q99933: BAG1; NbExp=2; IntAct=EBI-357085, EBI-1030678;
CC Q9UNE7; O95816: BAG2; NbExp=4; IntAct=EBI-357085, EBI-355275;
CC Q9UNE7; O95817: BAG3; NbExp=3; IntAct=EBI-357085, EBI-747185;
CC Q9UNE7; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-357085, EBI-11532900;
CC Q9UNE7; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-357085, EBI-1383687;
CC Q9UNE7; Q9NRJ3: CCL28; NbExp=3; IntAct=EBI-357085, EBI-7783254;
CC Q9UNE7; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-357085, EBI-1045797;
CC Q9UNE7; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-357085, EBI-25836642;
CC Q9UNE7; P21964-2: COMT; NbExp=3; IntAct=EBI-357085, EBI-10200977;
CC Q9UNE7; Q15438: CYTH1; NbExp=3; IntAct=EBI-357085, EBI-997830;
CC Q9UNE7; P53355: DAPK1; NbExp=2; IntAct=EBI-357085, EBI-358616;
CC Q9UNE7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-357085, EBI-10976677;
CC Q9UNE7; Q8WXU2-2: DNAAF4; NbExp=3; IntAct=EBI-357085, EBI-9381887;
CC Q9UNE7; A0AVK6: E2F8; NbExp=3; IntAct=EBI-357085, EBI-7779316;
CC Q9UNE7; P00533: EGFR; NbExp=4; IntAct=EBI-357085, EBI-297353;
CC Q9UNE7; O00471: EXOC5; NbExp=3; IntAct=EBI-357085, EBI-949824;
CC Q9UNE7; O75344: FKBP6; NbExp=3; IntAct=EBI-357085, EBI-744771;
CC Q9UNE7; Q9BZS1: FOXP3; NbExp=7; IntAct=EBI-357085, EBI-983719;
CC Q9UNE7; P06241: FYN; NbExp=3; IntAct=EBI-357085, EBI-515315;
CC Q9UNE7; P22466: GAL; NbExp=3; IntAct=EBI-357085, EBI-6624768;
CC Q9UNE7; Q53GS7: GLE1; NbExp=3; IntAct=EBI-357085, EBI-1955541;
CC Q9UNE7; P28799: GRN; NbExp=3; IntAct=EBI-357085, EBI-747754;
CC Q9UNE7; P07900: HSP90AA1; NbExp=9; IntAct=EBI-357085, EBI-296047;
CC Q9UNE7; P08238: HSP90AB1; NbExp=5; IntAct=EBI-357085, EBI-352572;
CC Q9UNE7; P08107: HSPA1B; NbExp=5; IntAct=EBI-357085, EBI-629985;
CC Q9UNE7; P11142: HSPA8; NbExp=8; IntAct=EBI-357085, EBI-351896;
CC Q9UNE7; P04792: HSPB1; NbExp=4; IntAct=EBI-357085, EBI-352682;
CC Q9UNE7; P42858: HTT; NbExp=12; IntAct=EBI-357085, EBI-466029;
CC Q9UNE7; P02545: LMNA; NbExp=3; IntAct=EBI-357085, EBI-351935;
CC Q9UNE7; Q07954-2: LRP1; NbExp=3; IntAct=EBI-357085, EBI-25833471;
CC Q9UNE7; Q5S007: LRRK2; NbExp=4; IntAct=EBI-357085, EBI-5323863;
CC Q9UNE7; Q9Y2U5: MAP3K2; NbExp=9; IntAct=EBI-357085, EBI-357393;
CC Q9UNE7; P10636: MAPT; NbExp=2; IntAct=EBI-357085, EBI-366182;
CC Q9UNE7; Q15773: MLF2; NbExp=3; IntAct=EBI-357085, EBI-1051875;
CC Q9UNE7; P00540: MOS; NbExp=2; IntAct=EBI-357085, EBI-1757866;
CC Q9UNE7; P05164: MPO; NbExp=3; IntAct=EBI-357085, EBI-2556173;
CC Q9UNE7; P13591: NCAM1; NbExp=3; IntAct=EBI-357085, EBI-2846607;
CC Q9UNE7; P35240: NF2; NbExp=3; IntAct=EBI-357085, EBI-1014472;
CC Q9UNE7; P08138: NGFR; NbExp=3; IntAct=EBI-357085, EBI-1387782;
CC Q9UNE7; Q96PB7: OLFM3; NbExp=4; IntAct=EBI-357085, EBI-10292253;
CC Q9UNE7; Q96PB7-3: OLFM3; NbExp=3; IntAct=EBI-357085, EBI-12005356;
CC Q9UNE7; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-357085, EBI-25929070;
CC Q9UNE7; O00628-2: PEX7; NbExp=3; IntAct=EBI-357085, EBI-25882083;
CC Q9UNE7; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-357085, EBI-9090282;
CC Q9UNE7; P17612: PRKACA; NbExp=3; IntAct=EBI-357085, EBI-476586;
CC Q9UNE7; O60260-5: PRKN; NbExp=6; IntAct=EBI-357085, EBI-21251460;
CC Q9UNE7; P51149: RAB7A; NbExp=3; IntAct=EBI-357085, EBI-1056089;
CC Q9UNE7; Q14257: RCN2; NbExp=3; IntAct=EBI-357085, EBI-356710;
CC Q9UNE7; O95072: REC8; NbExp=2; IntAct=EBI-357085, EBI-9361206;
CC Q9UNE7; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-357085, EBI-3918154;
CC Q9UNE7; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-357085, EBI-6257312;
CC Q9UNE7; Q15019-2: SEPTIN2; NbExp=3; IntAct=EBI-357085, EBI-10983222;
CC Q9UNE7; P01011: SERPINA3; NbExp=3; IntAct=EBI-357085, EBI-296557;
CC Q9UNE7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-357085, EBI-5235340;
CC Q9UNE7; O15269-2: SPTLC1; NbExp=3; IntAct=EBI-357085, EBI-25912901;
CC Q9UNE7; Q13501: SQSTM1; NbExp=3; IntAct=EBI-357085, EBI-307104;
CC Q9UNE7; Q86WV8: TSC1; NbExp=3; IntAct=EBI-357085, EBI-12806590;
CC Q9UNE7; Q99757: TXN2; NbExp=3; IntAct=EBI-357085, EBI-2932492;
CC Q9UNE7; P68036: UBE2L3; NbExp=3; IntAct=EBI-357085, EBI-711173;
CC Q9UNE7; P61088: UBE2N; NbExp=5; IntAct=EBI-357085, EBI-1052908;
CC Q9UNE7; Q7Z7E8: UBE2Q1; NbExp=3; IntAct=EBI-357085, EBI-1783287;
CC Q9UNE7; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-357085, EBI-11141397;
CC Q9UNE7; O76024: WFS1; NbExp=3; IntAct=EBI-357085, EBI-720609;
CC Q9UNE7; P12504: vif; Xeno; NbExp=2; IntAct=EBI-357085, EBI-779991;
CC Q9UNE7-1; P31749: AKT1; NbExp=5; IntAct=EBI-15687717, EBI-296087;
CC Q9UNE7-1; P11142-1: HSPA8; NbExp=4; IntAct=EBI-15687717, EBI-351908;
CC Q9UNE7-1; Q5S007: LRRK2; NbExp=2; IntAct=EBI-15687717, EBI-5323863;
CC Q9UNE7-1; P10636: MAPT; NbExp=5; IntAct=EBI-15687717, EBI-366182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10330192,
CC ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:23973223}. Nucleus
CC {ECO:0000269|PubMed:23973223}. Note=Translocates to the nucleus in
CC response to inflammatory signals in regulatory T-cells (Treg).
CC {ECO:0000269|PubMed:23973223}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNE7-2; Sequence=VSP_015947;
CC -!- TISSUE SPECIFICITY: Expressed in differentiated myotubes (at protein
CC level) (PubMed:17369820). Highly expressed in skeletal muscle, heart,
CC pancreas, brain and placenta (PubMed:10330192, PubMed:11435423).
CC Detected in kidney, liver and lung (PubMed:10330192, PubMed:11435423).
CC {ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11435423,
CC ECO:0000269|PubMed:17369820}.
CC -!- INDUCTION: Up-regulated by inflammatory signals in regulatory T-cells
CC (Treg). {ECO:0000269|PubMed:23973223}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000250|UniProtKB:Q9WUD1}.
CC -!- DOMAIN: The TPR domain is essential for ubiquitination mediated by
CC UBE2D1. {ECO:0000269|PubMed:18042044}.
CC -!- PTM: Monoubiquitinated at Lys-2 following cell stress by UBE2W,
CC promoting the interaction with ATXN3 (By similarity). Auto-
CC ubiquitinated; mediated by UBE2D1 and UBE2D2. {ECO:0000250,
CC ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:23560854}.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16)
CC [MIM:615768]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders. Patients show
CC progressive incoordination of gait and often poor coordination of
CC hands, speech and eye movements, due to degeneration of the cerebellum
CC with variable involvement of the brainstem and spinal cord. SCAR16 is
CC characterized by truncal and limb ataxia resulting in gait instability.
CC Additionally, patients may show dysarthria, nystagmus, spasticity of
CC the lower limbs, and mild peripheral sensory neuropathy.
CC {ECO:0000269|PubMed:24113144, ECO:0000269|PubMed:24312598,
CC ECO:0000269|PubMed:24719489, ECO:0000269|PubMed:24742043,
CC ECO:0000269|PubMed:25258038}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinocerebellar ataxia 48 (SCA48) [MIM:618093]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA48 is an autosomal dominant
CC neurodegenerative disease characterized by onset in mid-adulthood of
CC progressive cognitive decline and gait ataxia, and vermian and
CC hemispheric cerebellar atrophy. {ECO:0000269|PubMed:30381368}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Antibodies against STUB1 are found in patients with
CC chronic lymphocytic leukemia (CLL) and in colorectal cancer patients.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF039689; AAC18038.1; -; mRNA.
DR EMBL; AF129085; AAD33400.1; -; mRNA.
DR EMBL; AF432221; AAL99927.1; -; mRNA.
DR EMBL; AF217968; AAG17211.1; -; mRNA.
DR EMBL; AE006464; AAK61242.1; -; Genomic_DNA.
DR EMBL; Z92544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85758.1; -; Genomic_DNA.
DR EMBL; BC007545; AAH07545.1; -; mRNA.
DR EMBL; BC017178; AAH17178.1; -; mRNA.
DR EMBL; BC022788; AAH22788.1; -; mRNA.
DR EMBL; BC063617; AAH63617.1; -; mRNA.
DR CCDS; CCDS10419.1; -. [Q9UNE7-1]
DR CCDS; CCDS76797.1; -. [Q9UNE7-2]
DR RefSeq; NP_001280126.1; NM_001293197.1. [Q9UNE7-2]
DR RefSeq; NP_005852.2; NM_005861.3. [Q9UNE7-1]
DR PDB; 4KBQ; X-ray; 2.91 A; A/B=21-154.
DR PDB; 6EFK; X-ray; 1.50 A; A/B=23-154.
DR PDB; 6NSV; X-ray; 1.30 A; A/B=23-152.
DR PDBsum; 4KBQ; -.
DR PDBsum; 6EFK; -.
DR PDBsum; 6NSV; -.
DR AlphaFoldDB; Q9UNE7; -.
DR BMRB; Q9UNE7; -.
DR SMR; Q9UNE7; -.
DR BioGRID; 115563; 605.
DR CORUM; Q9UNE7; -.
DR DIP; DIP-29752N; -.
DR IntAct; Q9UNE7; 242.
DR MINT; Q9UNE7; -.
DR STRING; 9606.ENSP00000219548; -.
DR MoonDB; Q9UNE7; Predicted.
DR GlyGen; Q9UNE7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UNE7; -.
DR PhosphoSitePlus; Q9UNE7; -.
DR SwissPalm; Q9UNE7; -.
DR BioMuta; STUB1; -.
DR DMDM; 78099173; -.
DR EPD; Q9UNE7; -.
DR jPOST; Q9UNE7; -.
DR MassIVE; Q9UNE7; -.
DR MaxQB; Q9UNE7; -.
DR PaxDb; Q9UNE7; -.
DR PeptideAtlas; Q9UNE7; -.
DR PRIDE; Q9UNE7; -.
DR ProteomicsDB; 85282; -. [Q9UNE7-1]
DR ProteomicsDB; 85283; -. [Q9UNE7-2]
DR Antibodypedia; 22808; 487 antibodies from 46 providers.
DR DNASU; 10273; -.
DR Ensembl; ENST00000219548.9; ENSP00000219548.4; ENSG00000103266.11. [Q9UNE7-1]
DR Ensembl; ENST00000564370.5; ENSP00000456875.1; ENSG00000103266.11. [Q9UNE7-2]
DR Ensembl; ENST00000565677.5; ENSP00000457228.1; ENSG00000103266.11. [Q9UNE7-2]
DR GeneID; 10273; -.
DR KEGG; hsa:10273; -.
DR MANE-Select; ENST00000219548.9; ENSP00000219548.4; NM_005861.4; NP_005852.2.
DR UCSC; uc002cit.4; human. [Q9UNE7-1]
DR CTD; 10273; -.
DR DisGeNET; 10273; -.
DR GeneCards; STUB1; -.
DR HGNC; HGNC:11427; STUB1.
DR HPA; ENSG00000103266; Low tissue specificity.
DR MalaCards; STUB1; -.
DR MIM; 607207; gene.
DR MIM; 615768; phenotype.
DR MIM; 618093; phenotype.
DR neXtProt; NX_Q9UNE7; -.
DR OpenTargets; ENSG00000103266; -.
DR Orphanet; 412057; Autosomal recessive cerebellar ataxia due to STUB1 deficiency.
DR PharmGKB; PA36227; -.
DR VEuPathDB; HostDB:ENSG00000103266; -.
DR eggNOG; KOG4642; Eukaryota.
DR GeneTree; ENSGT00930000151045; -.
DR HOGENOM; CLU_056455_1_0_1; -.
DR InParanoid; Q9UNE7; -.
DR OMA; FLEKNGW; -.
DR OrthoDB; 1422450at2759; -.
DR PhylomeDB; Q9UNE7; -.
DR TreeFam; TF313937; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q9UNE7; -.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UNE7; -.
DR SIGNOR; Q9UNE7; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10273; 106 hits in 1130 CRISPR screens.
DR ChiTaRS; STUB1; human.
DR GeneWiki; STUB1; -.
DR GenomeRNAi; 10273; -.
DR Pharos; Q9UNE7; Tbio.
DR PRO; PR:Q9UNE7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UNE7; protein.
DR Bgee; ENSG00000103266; Expressed in lateral nuclear group of thalamus and 200 other tissues.
DR ExpressionAtlas; Q9UNE7; baseline and differential.
DR Genevisible; Q9UNE7; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:ARUK-UCL.
DR GO; GO:0031371; C:ubiquitin conjugating enzyme complex; TAS:HGNC-UCL.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:ARUK-UCL.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:HGNC-UCL.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
DR GO; GO:0051787; F:misfolded protein binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:HGNC-UCL.
DR GO; GO:0046332; F:SMAD binding; IDA:HGNC-UCL.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0030911; F:TPR domain binding; IDA:HGNC-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:ARUK-UCL.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:ARUK-UCL.
DR GO; GO:0071218; P:cellular response to misfolded protein; IDA:BHF-UCL.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; IDA:BHF-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:HGNC-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:HGNC-UCL.
DR GO; GO:0045862; P:positive regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0051604; P:protein maturation; TAS:HGNC-UCL.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:HGNC-UCL.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:BHF-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0031943; P:regulation of glucocorticoid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR GO; GO:0002931; P:response to ischemia; ISS:ARUK-UCL.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IDA:HGNC-UCL.
DR CDD; cd16654; RING-Ubox_CHIP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045200; CHIP/LubX.
DR InterPro; IPR045202; CHIP/LubX_RING-Ubox.
DR InterPro; IPR041312; CHIP_TPR_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46803; PTHR46803; 1.
DR Pfam; PF18391; CHIP_TPR_N; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00028; TPR; 3.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disease variant; DNA damage; DNA repair; Isopeptide bond;
KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Spinocerebellar ataxia; TPR repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..303
FT /note="E3 ubiquitin-protein ligase CHIP"
FT /id="PRO_0000106329"
FT REPEAT 26..59
FT /note="TPR 1"
FT REPEAT 60..93
FT /note="TPR 2"
FT REPEAT 95..127
FT /note="TPR 3"
FT DOMAIN 226..300
FT /note="U-box"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23560854"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18042044"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18042044"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18042044"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_015947"
FT VARIANT 28
FT /note="E -> K (in SCAR16; reduces protein level; does not
FT reduce ubiquitin ligase activity and autoubiquitination)"
FT /evidence="ECO:0000269|PubMed:25258038"
FT /id="VAR_072348"
FT VARIANT 57
FT /note="P -> S (found in a patient with progressive
FT myoclonus epilepsy; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33798445"
FT /id="VAR_085041"
FT VARIANT 65
FT /note="N -> S (in SCAR16; reduces protein level; reduces
FT ubiquitin ligase activity; does not change
FT autoubiquitination; dbSNP:rs690016544)"
FT /evidence="ECO:0000269|PubMed:25258038"
FT /id="VAR_072349"
FT VARIANT 79
FT /note="A -> D (in SCAR16; dbSNP:rs587777347)"
FT /evidence="ECO:0000269|PubMed:24742043"
FT /id="VAR_071293"
FT VARIANT 79
FT /note="A -> T (in SCAR16; dbSNP:rs587777346)"
FT /evidence="ECO:0000269|PubMed:24742043"
FT /id="VAR_071294"
FT VARIANT 123
FT /note="L -> V (in SCAR16; dbSNP:rs587777344)"
FT /evidence="ECO:0000269|PubMed:24742043"
FT /id="VAR_071295"
FT VARIANT 130
FT /note="N -> I (in SCAR16; dbSNP:rs587777341)"
FT /evidence="ECO:0000269|PubMed:24312598"
FT /id="VAR_071296"
FT VARIANT 145
FT /note="K -> Q (in SCAR16; dbSNP:rs146251364)"
FT /evidence="ECO:0000269|PubMed:24719489"
FT /id="VAR_072350"
FT VARIANT 147
FT /note="W -> C (in SCAR16; dbSNP:rs587777342)"
FT /evidence="ECO:0000269|PubMed:24312598"
FT /id="VAR_071297"
FT VARIANT 165
FT /note="L -> F (in SCAR16; dbSNP:rs587777340)"
FT /evidence="ECO:0000269|PubMed:24312598"
FT /id="VAR_071298"
FT VARIANT 236
FT /note="S -> T (in SCAR16)"
FT /evidence="ECO:0000269|PubMed:24312598"
FT /id="VAR_071299"
FT VARIANT 240
FT /note="M -> T (in SCAR16; dbSNP:rs587777345)"
FT /evidence="ECO:0000269|PubMed:24742043"
FT /id="VAR_071300"
FT VARIANT 246
FT /note="T -> M (in SCAR16; inhibits ubiquitin ligase
FT activity and autoubiquitination; dbSNP:rs587777343)"
FT /evidence="ECO:0000269|PubMed:24113144,
FT ECO:0000269|PubMed:25258038"
FT /id="VAR_071301"
FT MUTAGEN 30
FT /note="K->A: Loss of interaction with FOXP3 and its ability
FT to ubiquitinate FOXP3. Loss of interaction with SMAD3,
FT HSPA8, HSP90AA1 and HSP90AB1."
FT /evidence="ECO:0000269|PubMed:23973223,
FT ECO:0000269|PubMed:24613385"
FT MUTAGEN 260
FT /note="H->Q: Loss of ability to ubiquitinate FOXP3 and
FT SIRT6."
FT /evidence="ECO:0000269|PubMed:23973223,
FT ECO:0000269|PubMed:24043303"
FT MUTAGEN 269
FT /note="P->A: Abolishes E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:23990462"
FT CONFLICT 52
FT /note="A -> V (in Ref. 2; AAD33400)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="R -> G (in Ref. 1; AAC18038)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> F (in Ref. 1; AAC18038)"
FT /evidence="ECO:0000305"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:6NSV"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:6NSV"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:6NSV"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:6NSV"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:6NSV"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:6NSV"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:6NSV"
SQ 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
