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 27-MAR-2024, entry version 226. 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 SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] 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:25593309, ECO:0000269|PubMed:32324863}. Cytoplasm CC {ECO:0000269|PubMed:21164480}. Mitochondrion CC {ECO:0000269|PubMed:32324863}. Note=Colocalizes with sites of active CC transcription. Predominantly nuclear. Translocated from nucleus to CC mitochondria to mediate antiviral immunity (PubMed:32324863). Localizes CC to sites of DNA damage (PubMed:25593309). {ECO:0000269|PubMed:25593309, CC 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="https://atlasgeneticsoncology.org/gene/504/trim24"; 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; 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; 375. DR DIP; DIP-52713N; -. DR ELM; O15164; -. DR IntAct; O15164; 145. 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 SwissPalm; O15164; -. DR BioMuta; TRIM24; -. DR EPD; O15164; -. DR jPOST; O15164; -. DR MassIVE; O15164; -. DR MaxQB; O15164; -. DR PaxDb; 9606-ENSP00000340507; -. DR PeptideAtlas; O15164; -. DR ProteomicsDB; 48484; -. [O15164-1] DR ProteomicsDB; 48485; -. [O15164-2] DR Pumba; O15164; -. DR ABCD; O15164; 1 sequenced antibody. DR Antibodypedia; 32326; 649 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 AGR; HGNC:11812; -. 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; AIKQWQV; -. DR OrthoDB; 56754at2759; -. 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; 33 hits in 1220 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 213 other cell types or tissues. DR ExpressionAtlas; O15164; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; 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:0043434; P:response to peptide hormone; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd19845; Bbox1_TIF1a_C-VI; 1. DR CDD; cd19828; Bbox2_TIF1a_C-VI; 1. DR CDD; cd05502; Bromo_tif1_like; 1. DR CDD; cd15622; PHD_TIF1alpha; 1. DR CDD; cd16764; RING-HC_TIF1alpha; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1. DR PANTHER; PTHR45915:SF4; TRANSCRIPTION INTERMEDIARY FACTOR 1-ALPHA; 1. 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; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF57850; RING/U-box; 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. DR Genevisible; O15164; HS. 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 //