TIF1A_HUMAN
ID TIF1A_HUMAN Reviewed; 1050 AA.
AC O15164; A4D1R7; A4D1R8; O95854;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Transcription intermediary factor 1-alpha;
DE Short=TIF1-alpha;
DE EC=2.3.2.27 {ECO:0000269|PubMed:24820418, ECO:0000269|PubMed:32324863};
DE AltName: Full=E3 ubiquitin-protein ligase TRIM24;
DE AltName: Full=RING finger protein 82;
DE AltName: Full=RING-type E3 ubiquitin transferase TIF1-alpha {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 24;
GN Name=TRIM24; Synonyms=RNF82, TIF1, TIF1A;
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 SHORT), AND SUBUNIT.
RC TISSUE=Mammary cancer;
RX PubMed=9115274; DOI=10.1074/jbc.272.18.12062;
RA Thenot S., Henriquet C., Rochefort H., Cavailles V.;
RT "Differential interaction of nuclear receptors with the putative human
RT transcriptional coactivator hTIF1.";
RL J. Biol. Chem. 272:12062-12068(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=10022127; DOI=10.1038/sj.onc.1202655;
RA Venturini L., You J., Stadler M., Galien R., Lallemand V., Koken M.H.M.,
RA Mattei M.-G., Ganser A., Chambon P., Losson R., De The H.;
RT "TIF1gamma, a novel member of the transcriptional intermediary factor 1
RT family.";
RL Oncogene 18:1209-1217(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Retinoblastoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Testis;
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 [7]
RP PROTEIN SEQUENCE OF 477-510 (ISOFORM LONG).
RC TISSUE=Mammary cancer;
RA Cavailles V.;
RL Submitted (JAN-1999) to UniProtKB.
RN [8]
RP INTERACTION WITH NR3C2.
RX PubMed=10935545; DOI=10.1210/mend.14.8.0502;
RA Hellal-Levy C., Fagart J., Souque A., Wurtz J.-M., Moras D.,
RA Rafestin-Oblin M.-E.;
RT "Crucial role of the H11-H12 loop in stabilizing the active conformation of
RT the human mineralocorticoid receptor.";
RL Mol. Endocrinol. 14:1210-1221(2000).
RN [9]
RP CHROMOSOMAL TRANSLOCATION WITH RET.
RC TISSUE=Thyroid;
RX PubMed=10439047; DOI=10.1038/sj.onc.1202824;
RA Klugbauer S., Rabes H.M.;
RT "The transcription coactivator HTIF1 and a related protein are fused to the
RT RET receptor tyrosine kinase in childhood papillary thyroid carcinomas.";
RL Oncogene 18:4388-4393(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811; SER-1025 AND SER-1028,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP FUNCTION.
RX PubMed=16322096; DOI=10.1210/me.2005-0393;
RA Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.;
RT "Transcriptional intermediary factor 1alpha mediates physical interaction
RT and functional synergy between the coactivator-associated arginine
RT methyltransferase 1 and glucocorticoid receptor-interacting protein 1
RT nuclear receptor coactivators.";
RL Mol. Endocrinol. 20:1276-1286(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-768; SER-808 AND
RP SER-811, AND 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 [13]
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 [14]
RP INTERACTION WITH AR.
RX PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
RA Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J.,
RA Imamura M., Hatakeyama S.;
RT "TRIM24 mediates ligand-dependent activation of androgen receptor and is
RT repressed by a bromodomain-containing protein, BRD7, in prostate cancer
RT cells.";
RL Biochim. Biophys. Acta 1793:1828-1836(2009).
RN [15]
RP FUNCTION AS E3 UBIQUITIN LIGASE, AND INTERACTION WITH TP53.
RX PubMed=19556538; DOI=10.1073/pnas.0813177106;
RA Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A.,
RA Johnson R.L., Barton M.C.;
RT "Trim24 targets endogenous p53 for degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025 AND SER-1028, AND
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-110; SER-768 AND
RP SER-811, AND 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744; SER-811; THR-818;
RP SER-1019; SER-1028 AND SER-1042, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [20]
RP INTERACTION WITH TRIM16.
RX PubMed=22629402; DOI=10.1371/journal.pone.0037470;
RA Bell J.L., Malyukova A., Holien J.K., Koach J., Parker M.W., Kavallaris M.,
RA Marshall G.M., Cheung B.B.;
RT "TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other
RT TRIM family members.";
RL PLoS ONE 7:E37470-E37470(2012).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654; SER-744; SER-811;
RP SER-1025 AND SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP IDENTIFICATION BY 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 [24]
RP FUNCTION, INDUCTION BY TP53, CATALYTIC ACTIVITY, PHOSPHORYLATION AT
RP SER-768, AND MUTAGENESIS OF SER-768.
RX PubMed=24820418; DOI=10.1128/mcb.01705-12;
RA Jain A.K., Allton K., Duncan A.D., Barton M.C.;
RT "TRIM24 is a p53-induced E3-ubiquitin ligase that undergoes ATM-mediated
RT phosphorylation and autodegradation during DNA damage.";
RL Mol. Cell. Biol. 34:2695-2709(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-711; LYS-723 AND LYS-949, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-723 AND LYS-741, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-702; LYS-723 AND LYS-1041, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-723, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-205; LYS-276; LYS-436;
RP LYS-458; LYS-552; LYS-641; LYS-702; LYS-711; LYS-723; LYS-741; LYS-801;
RP LYS-810; LYS-875 AND LYS-992, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=32324863; DOI=10.1084/jem.20192083;
RA Zhu Q., Yu T., Gan S., Wang Y., Pei Y., Zhao Q., Pei S., Hao S., Yuan J.,
RA Xu J., Hou F., Wu X., Peng C., Wu P., Qin J., Xiao Y.;
RT "TRIM24 facilitates antiviral immunity through mediating K63-linked TRAF3
RT ubiquitination.";
RL J. Exp. Med. 217:0-0(2020).
RN [31]
RP FUNCTION.
RX PubMed=33724611; DOI=10.1002/cbin.11592;
RA Hang Y., Tan L., Chen Q., Liu Q., Jin Y.;
RT "E3 ubiquitin ligase TRIM24 deficiency promotes NLRP3/caspase-1/IL-1beta-
RT mediated pyroptosis in endometriosis.";
RL Cell Biol. Int. 45:1561-1570(2021).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 891-1012.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of human bromodomain protein.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 824-1006 IN COMPLEXES WITH
RP METHYLATED HISTONE PEPTIDES AND ZINC IONS, FUNCTION, MUTAGENESIS OF
RP ASP-827; CYS-840 AND 979-PHE-ASN-980, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INDUCTION.
RX PubMed=21164480; DOI=10.1038/nature09542;
RA Tsai W.W., Wang Z., Yiu T.T., Akdemir K.C., Xia W., Winter S., Tsai C.Y.,
RA Shi X., Schwarzer D., Plunkett W., Aronow B., Gozani O., Fischle W.,
RA Hung M.C., Patel D.J., Barton M.C.;
RT "TRIM24 links a non-canonical histone signature to breast cancer.";
RL Nature 468:927-932(2010).
RN [34]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-320; ASN-403; ASN-762 AND SER-1009.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Transcriptional coactivator that interacts with numerous
CC nuclear receptors and coactivators and modulates the transcription of
CC target genes. Interacts with chromatin depending on histone H3
CC modifications, having the highest affinity for histone H3 that is both
CC unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac).
CC Has E3 protein-ubiquitin ligase activity. During the DNA damage
CC response, participates in an autoregulatory feedback loop with TP53.
CC Early in response to DNA damage, ATM kinase phosphorylates TRIM24
CC leading to its ubiquitination and degradation. After sufficient DNA
CC repair has occurred, TP53 activates TRIM24 transcription, ultimately
CC leading to TRIM24-mediated TP53 ubiquitination and degradation
CC (PubMed:24820418). Plays a role in the regulation of cell proliferation
CC and apoptosis, at least in part via its effects on p53/TP53 levels. Up-
CC regulates ligand-dependent transcription activation by AR, GCR/NR3C1,
CC thyroid hormone receptor (TR) and ESR1. Modulates transcription
CC activation by retinoic acid (RA) receptors, including RARA. Plays a
CC role in regulating retinoic acid-dependent proliferation of hepatocytes
CC (By similarity). Participates also in innate immunity by mediating the
CC specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation
CC of downstream signal transduction of the type I IFN pathway
CC (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-
CC 1beta-mediated pyroptosis and cell migration probably by ubiquitinating
CC NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269|PubMed:16322096,
CC ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:21164480,
CC ECO:0000269|PubMed:24820418, ECO:0000269|PubMed:32324863,
CC ECO:0000269|PubMed:33724611}.
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:24820418,
CC ECO:0000269|PubMed:32324863};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CARM1, NCOA2/GRIP1, PML, KAT5/TIP60, BRD7,
CC CBX1, CBX3 and CBX5. Part of a coactivator complex containing TRIM24,
CC NCOA2 and CARM1 (By similarity). Interacts with NR3C2/MCR. Interacts
CC with the ligand-binding domain of estrogen receptors (in vitro).
CC Interaction with DNA-bound estrogen receptors requires the presence of
CC estradiol. Interacts with AR and p53/TP53. Interacts (via bromo domain)
CC with histone H3 (via N-terminus), provided that it is not methylated at
CC 'Lys-4' (H3K4me0). Does not interact with histone H3 that is methylated
CC at 'Lys-4' (H3K4me1, H3K4me2 or H3K4me3). Interacts (via bromo domain)
CC with histone H3 (via N-terminus) that is acetylated at 'Lys-23'
CC (H3K23ac). Has the highest affinity for histone H3 that is both
CC unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac).
CC Has very low affinity for histone H3 that is methylated at 'Lys-9'
CC (H3K9me), or acetylated at both 'Lys-9' (H3K9ac) and 'Lys-14'
CC (H3K14ac), or acetylated at 'Lys-27' (H3K27ac) (in vitro). Interacts
CC with TRIM16. {ECO:0000250, ECO:0000269|PubMed:10935545,
CC ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775,
CC ECO:0000269|PubMed:21164480, ECO:0000269|PubMed:22629402,
CC ECO:0000269|PubMed:9115274}.
CC -!- INTERACTION:
CC O15164; P03372: ESR1; NbExp=3; IntAct=EBI-2130378, EBI-78473;
CC O15164; P04637: TP53; NbExp=3; IntAct=EBI-2130378, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21164480,
CC ECO:0000269|PubMed:32324863}. Cytoplasm {ECO:0000269|PubMed:21164480}.
CC Mitochondrion {ECO:0000269|PubMed:32324863}. Note=Colocalizes with
CC sites of active transcription. Detected both in nucleus and cytoplasm
CC in some breast cancer samples. Predominantly nuclear. Translocated from
CC nucleus to mitochondria to mediate antiviral immunity
CC (PubMed:32324863). {ECO:0000269|PubMed:32324863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O15164-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O15164-2; Sequence=VSP_005772;
CC -!- INDUCTION: Up-regulated in some cases of breast cancer
CC (PubMed:21164480). Expression is induced by damage-activated TP53
CC (PubMed:24820418). {ECO:0000269|PubMed:21164480,
CC ECO:0000269|PubMed:24820418}.
CC -!- PTM: Phosphorylated at Ser-768 by ATM kinase induces ubiquitination and
CC degradation during DNA damage. {ECO:0000269|PubMed:24820418}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:Q64127}.
CC -!- PTM: Undergoes ubiquitination-mediated degradation in response to DNA
CC damage. {ECO:0000269|PubMed:24820418}.
CC -!- DISEASE: Note=A chromosomal aberration involving TRIM24/TIF1 is found
CC in papillary thyroid carcinomas (PTCs). Translocation t(7;10)(q32;q11)
CC with RET. The translocation generates the TRIM24/RET (PTC6) oncogene.
CC {ECO:0000269|PubMed:10439047}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRIM24ID504ch7q34.html";
CC ---------------------------------------------------------------------------
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DR EMBL; AF009353; AAB63585.1; -; mRNA.
DR EMBL; AF119042; AAD17258.1; -; mRNA.
DR EMBL; AK075306; BAG52105.1; -; mRNA.
DR EMBL; AC008265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24046.1; -; Genomic_DNA.
DR EMBL; CH236950; EAL24047.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83884.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83885.1; -; Genomic_DNA.
DR EMBL; BC028689; AAH28689.2; -; mRNA.
DR CCDS; CCDS47720.1; -. [O15164-2]
DR CCDS; CCDS5847.1; -. [O15164-1]
DR RefSeq; NP_003843.3; NM_003852.3. [O15164-2]
DR RefSeq; NP_056989.2; NM_015905.2. [O15164-1]
DR PDB; 2YYN; X-ray; 2.50 A; A/B/C/D=891-1012.
DR PDB; 3O33; X-ray; 2.00 A; A/B/C/D=824-1006.
DR PDB; 3O34; X-ray; 1.90 A; A=824-1006.
DR PDB; 3O35; X-ray; 1.76 A; A/B=824-1006.
DR PDB; 3O36; X-ray; 1.70 A; A/B=824-1006.
DR PDB; 3O37; X-ray; 2.00 A; A/B/C/D=824-1006.
DR PDB; 4YAB; X-ray; 1.90 A; A/B=824-1006.
DR PDB; 4YAD; X-ray; 1.73 A; A/B=824-1006.
DR PDB; 4YAT; X-ray; 2.18 A; A/B=824-1006.
DR PDB; 4YAX; X-ray; 2.25 A; A/B=824-1006.
DR PDB; 4YBM; X-ray; 1.46 A; A/B=824-1006.
DR PDB; 4YBS; X-ray; 1.83 A; A=824-1006.
DR PDB; 4YBT; X-ray; 1.82 A; A=824-1006.
DR PDB; 4YC9; X-ray; 1.82 A; A=824-1006.
DR PDB; 4ZQL; X-ray; 1.79 A; A/B=825-1006.
DR PDB; 5H1T; X-ray; 1.95 A; A/B/C/D=824-1006.
DR PDB; 5H1U; X-ray; 1.90 A; A/B/C/D=824-1006.
DR PDB; 5H1V; X-ray; 2.00 A; A/B=824-1006.
DR PDB; 7B9X; NMR; -; A=901-1006.
DR PDBsum; 2YYN; -.
DR PDBsum; 3O33; -.
DR PDBsum; 3O34; -.
DR PDBsum; 3O35; -.
DR PDBsum; 3O36; -.
DR PDBsum; 3O37; -.
DR PDBsum; 4YAB; -.
DR PDBsum; 4YAD; -.
DR PDBsum; 4YAT; -.
DR PDBsum; 4YAX; -.
DR PDBsum; 4YBM; -.
DR PDBsum; 4YBS; -.
DR PDBsum; 4YBT; -.
DR PDBsum; 4YC9; -.
DR PDBsum; 4ZQL; -.
DR PDBsum; 5H1T; -.
DR PDBsum; 5H1U; -.
DR PDBsum; 5H1V; -.
DR PDBsum; 7B9X; -.
DR AlphaFoldDB; O15164; -.
DR SMR; O15164; -.
DR BioGRID; 114333; 283.
DR DIP; DIP-52713N; -.
DR ELM; O15164; -.
DR IntAct; O15164; 144.
DR MINT; O15164; -.
DR STRING; 9606.ENSP00000340507; -.
DR BindingDB; O15164; -.
DR ChEMBL; CHEMBL3108638; -.
DR GuidetoPHARMACOLOGY; 2252; -.
DR GlyGen; O15164; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15164; -.
DR MetOSite; O15164; -.
DR PhosphoSitePlus; O15164; -.
DR BioMuta; TRIM24; -.
DR EPD; O15164; -.
DR jPOST; O15164; -.
DR MassIVE; O15164; -.
DR MaxQB; O15164; -.
DR PaxDb; O15164; -.
DR PeptideAtlas; O15164; -.
DR PRIDE; O15164; -.
DR ProteomicsDB; 48484; -. [O15164-1]
DR ProteomicsDB; 48485; -. [O15164-2]
DR ABCD; O15164; 1 sequenced antibody.
DR Antibodypedia; 32326; 563 antibodies from 39 providers.
DR DNASU; 8805; -.
DR Ensembl; ENST00000343526.9; ENSP00000340507.4; ENSG00000122779.18. [O15164-1]
DR Ensembl; ENST00000415680.6; ENSP00000390829.2; ENSG00000122779.18. [O15164-2]
DR GeneID; 8805; -.
DR KEGG; hsa:8805; -.
DR MANE-Select; ENST00000343526.9; ENSP00000340507.4; NM_015905.3; NP_056989.2.
DR UCSC; uc003vub.4; human. [O15164-1]
DR CTD; 8805; -.
DR DisGeNET; 8805; -.
DR GeneCards; TRIM24; -.
DR HGNC; HGNC:11812; TRIM24.
DR HPA; ENSG00000122779; Low tissue specificity.
DR MalaCards; TRIM24; -.
DR MIM; 603406; gene.
DR neXtProt; NX_O15164; -.
DR OpenTargets; ENSG00000122779; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA36519; -.
DR VEuPathDB; HostDB:ENSG00000122779; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159863; -.
DR HOGENOM; CLU_005817_0_1_1; -.
DR InParanoid; O15164; -.
DR OMA; WIGPSHT; -.
DR OrthoDB; 756911at2759; -.
DR PhylomeDB; O15164; -.
DR TreeFam; TF106455; -.
DR PathwayCommons; O15164; -.
DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR SignaLink; O15164; -.
DR SIGNOR; O15164; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8805; 30 hits in 1139 CRISPR screens.
DR ChiTaRS; TRIM24; human.
DR EvolutionaryTrace; O15164; -.
DR GeneWiki; TRIM24; -.
DR GenomeRNAi; 8805; -.
DR Pharos; O15164; Tchem.
DR PRO; PR:O15164; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15164; protein.
DR Bgee; ENSG00000122779; Expressed in sperm and 212 other tissues.
DR ExpressionAtlas; O15164; baseline and differential.
DR Genevisible; O15164; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0034056; F:estrogen response element binding; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR IDEAL; IID00289; -.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Bromodomain; Chromosomal rearrangement;
KW Coiled coil; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Tumor suppressor; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1050
FT /note="Transcription intermediary factor 1-alpha"
FT /id="PRO_0000056390"
FT DOMAIN 932..987
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 56..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 158..211
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 218..259
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 826..873
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 15..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..779
FT /note="Nuclear receptor binding site (NRBS)"
FT REGION 766..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..840
FT /note="Interaction with histone H3 that is not methylated
FT at 'Lys-4' (H3K4me0)"
FT REGION 979..980
FT /note="Interaction with histone H3 that is acetylated at
FT 'Lys-23' (H3K23ac)"
FT REGION 1011..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..359
FT /evidence="ECO:0000255"
FT MOTIF 891..907
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 431..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT SITE 476..477
FT /note="Breakpoint for translocation to form TRIM24-RET
FT oncogene"
FT SITE 827
FT /note="Interaction with histone H3 that is not methylated
FT at 'Lys-4' (H3K4me0)"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 469
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q64127"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64127"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 768
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:24820418,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 552
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 641
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 702
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 711
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 801
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 810
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 875
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 949
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 992
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1041
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT VAR_SEQ 477..510
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10022127,
FT ECO:0000303|PubMed:9115274"
FT /id="VSP_005772"
FT VARIANT 320
FT /note="I -> T (in an ovarian serous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042382"
FT VARIANT 403
FT /note="T -> N (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042383"
FT VARIANT 762
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042384"
FT VARIANT 796
FT /note="N -> S (in dbSNP:rs35356723)"
FT /id="VAR_052148"
FT VARIANT 1009
FT /note="R -> S (in dbSNP:rs34585297)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042385"
FT MUTAGEN 768
FT /note="S->A: Ubiquitination is significantly lower than
FT wild-type."
FT /evidence="ECO:0000269|PubMed:24820418"
FT MUTAGEN 827
FT /note="D->A: Strongly reduced affinity for histone H3 that
FT is not methylated at 'Lys-4' (H3K4me0)."
FT /evidence="ECO:0000269|PubMed:21164480"
FT MUTAGEN 840
FT /note="C->W: Abolishes interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:21164480"
FT MUTAGEN 979..980
FT /note="FN->AA: Strongly reduced affinity for histone H3
FT that is acetylated at 'Lys-23' (H3K23ac)."
FT /evidence="ECO:0000269|PubMed:21164480"
FT CONFLICT 14..20
FT /note="AASAAAS -> RLGCAP (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..28
FT /note="SAAPS -> RGG (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..114
FT /note="GSPVSG -> ARRSA (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="A -> T (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="D -> N (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="M -> I (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="A -> R (in Ref. 1; AAB63585)"
FT /evidence="ECO:0000305"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:3O33"
FT TURN 830..832
FT /evidence="ECO:0007829|PDB:4YBM"
FT STRAND 836..840
FT /evidence="ECO:0007829|PDB:3O37"
FT STRAND 842..845
FT /evidence="ECO:0007829|PDB:4YBM"
FT TURN 850..852
FT /evidence="ECO:0007829|PDB:4YBM"
FT STRAND 853..855
FT /evidence="ECO:0007829|PDB:4YBM"
FT TURN 868..870
FT /evidence="ECO:0007829|PDB:4YBM"
FT STRAND 873..875
FT /evidence="ECO:0007829|PDB:4YBM"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:4YBM"
FT TURN 889..891
FT /evidence="ECO:0007829|PDB:3O36"
FT HELIX 902..917
FT /evidence="ECO:0007829|PDB:4YBM"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:3O37"
FT HELIX 922..924
FT /evidence="ECO:0007829|PDB:4YBM"
FT HELIX 935..938
FT /evidence="ECO:0007829|PDB:4YBM"
FT HELIX 945..953
FT /evidence="ECO:0007829|PDB:4YBM"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:4YC9"
FT HELIX 962..979
FT /evidence="ECO:0007829|PDB:4YBM"
FT HELIX 985..1004
FT /evidence="ECO:0007829|PDB:4YBM"
FT STRAND 1005..1007
FT /evidence="ECO:0007829|PDB:2YYN"
SQ SEQUENCE 1050 AA; 116831 MW; D341E8022AACC67E CRC64;
MEVAVEKAVA AAAAASAAAS GGPSAAPSGE NEAESRQGPD SERGGEAARL NLLDTCAVCH
QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE TPPPVPAPGS PVSGSSPFAT
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NNTIQFHCDP SFWAQNIINL
GSLVIEDKES QPQMPKQNPV VEQNSQPPSG LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY
PPNQNIPRQA IKPNPLQMAF LAQQAIKQWQ ISSGQGTPST TNSTSSTPSS PTITSAAGYD
GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTNIDHGQP RPPSNRTVQS
PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS SKPAGADSTH KVPVVMLEPI
RIKQENSGPP ENYDFPVVIV KQESDEESRP QNANYPRSIL TSLLLNSSQS STSEETVLRS
DAPDSTGDQP GLHQDNSSNG KSEWLDPSQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC
CEKCPKVFHL SCHVPTLTNF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL
TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK RLQEDYSMYS
KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL LKNLYPEKRF PKPEFRNESE
DNKFSDDSDD DFVQPRKKRL KSIEERQLLK
