ID TIF1B_HUMAN Reviewed; 835 AA. AC Q13263; O00677; Q7Z632; Q93040; Q96IM1; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 11-NOV-2015, entry version 192. DE RecName: Full=Transcription intermediary factor 1-beta; DE Short=TIF1-beta; DE AltName: Full=E3 SUMO-protein ligase TRIM28; DE EC=6.3.2.-; DE AltName: Full=KRAB-associated protein 1; DE Short=KAP-1; DE AltName: Full=KRAB-interacting protein 1; DE Short=KRIP-1; DE AltName: Full=Nuclear corepressor KAP-1; DE AltName: Full=RING finger protein 96; DE AltName: Full=Tripartite motif-containing protein 28; GN Name=TRIM28; Synonyms=KAP1, RNF96, TIF1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=8769649; DOI=10.1101/gad.10.16.2067; RA Friedman J.R., Fredericks W.J., Jensen D.E., Speicher D.W., RA Huang X.-P., Neilson E.G., Rauscher F.J. III; RT "KAP-1, a novel corepressor for the highly conserved KRAB repression RT domain."; RL Genes Dev. 10:2067-2078(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ZNF10. RX PubMed=9016654; DOI=10.1093/nar/24.24.4859; RA Moosmann P.R., Georgiev O., le Douarin B., Bourquin J.-P., RA Schaffner W.; RT "Transcriptional repression by RING finger protein TIF1 beta that RT interacts with the KRAB repressor domain of KOX1."; RL Nucleic Acids Res. 24:4859-4867(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Spleen; RA Emison E.S., Lewis B.C., Shim H., Li Q., Dang C.V., Lee L.A.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin, and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [6] RP PROTEIN SEQUENCE OF 2-32; 408-427 AND 493-507, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V.; RL Submitted (JAN-2010) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 486-835. RA Lyle R., Hewitt J.E.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [8] RP PROTEIN SEQUENCE OF N-TERMINUS, OLIGOMERIZATION, INTERACTION WITH THE RP KRAB DOMAIN, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17512541; DOI=10.1016/j.jmb.2007.03.047; RA Peng H., Gibson L.C., Capili A.D., Borden K.L., Osborne M.J., RA Harper S.L., Speicher D.W., Zhao K., Marmorstein R., Rock T.A., RA Rauscher F.J. III; RT "The structurally disordered KRAB repression domain is incorporated RT into a protease resistant core upon binding to KAP-1-RBCC domain."; RL J. Mol. Biol. 370:269-289(2007). RN [9] RP INTERACTION WITH CBX1; CBX3 AND CBX5, AND SUBCELLULAR LOCATION. RX PubMed=10330177; RA Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R., RA Fredericks W.J., Rauscher F.J. III; RT "KAP-1 corepressor protein interacts and colocalizes with RT heterochromatic and euchromatic HP1 proteins: a potential role for RT Kruppel-associated box-zinc finger proteins in heterochromatin- RT mediated gene silencing."; RL Mol. Cell. Biol. 19:4366-4378(1999). RN [10] RP INTERACTION WITH ZFP53 AND ZFP68, AND FUNCTION. RX PubMed=10347202; DOI=10.1074/jbc.274.23.16412; RA Agata Y., Matsuda E., Shimizu A.; RT "Two novel Kruppel-associated box-containing zinc-finger proteins, RT KRAZ1 and KRAZ2, repress transcription through functional interaction RT with the corepressor KAP-1 (TIF1beta/KRIP-1)."; RL J. Biol. Chem. 274:16412-16422(1999). RN [11] RP INTERACTION WITH NCOR1. RX PubMed=11013263; DOI=10.1074/jbc.M007864200; RA Underhill C., Qutob M.S., Yee S.P., Torchia J.; RT "A novel nuclear receptor corepressor complex, N-CoR, contains RT components of the mammalian SWI/SNF complex and the corepressor KAP- RT 1."; RL J. Biol. Chem. 275:40463-40470(2000). RN [12] RP INTERACTION WITH CHD3. RX PubMed=11230151; DOI=10.1101/gad.869501; RA Schultz D.C., Friedman J.R., Rauscher F.J. III; RT "Targeting histone deacetylase complexes via KRAB-zinc finger RT proteins: the PHD and bromodomains of KAP-1 form a cooperative unit RT that recruits a novel isoform of the Mi-2alpha subunit of NuRD."; RL Genes Dev. 15:428-443(2001). RN [13] RP INTERACTION WITH SETDB1, AND FUNCTION. RX PubMed=11959841; DOI=10.1101/gad.973302; RA Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III; RT "SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific RT methyltransferase that contributes to HP1-mediated silencing of RT euchromatic genes by KRAB zinc-finger proteins."; RL Genes Dev. 16:919-932(2002). RN [14] RP INTERACTION WITH CBX5, AND FUNCTION. RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016; RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III; RT "The mammalian heterochromatin protein 1 binds diverse nuclear RT proteins through a common motif that targets the chromoshadow RT domain."; RL Biochem. Biophys. Res. Commun. 331:929-937(2005). RN [15] RP INTERACTION WITH MDM2, AND FUNCTION. RX PubMed=16107876; DOI=10.1038/sj.emboj.7600791; RA Wang C., Ivanov A., Chen L., Fredericks W.J., Seto E., RA Rauscher F.J. III, Chen J.; RT "MDM2 interaction with nuclear corepressor KAP1 contributes to p53 RT inactivation."; RL EMBO J. 24:3279-3290(2005). RN [16] RP INTERACTION WITH MDM2 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX. RX PubMed=17056014; DOI=10.1016/j.bbrc.2006.10.022; RA Okamoto K., Kitabayashi I., Taya Y.; RT "KAP1 dictates p53 response induced by chemotherapeutic agents via RT Mdm2 interaction."; RL Biochem. Biophys. Res. Commun. 351:216-222(2006). RN [17] RP INTERACTION WITH FES/FPS, AND PHOSPHORYLATION. RX PubMed=16792528; DOI=10.1042/BJ20060194; RA Delfino F.J., Shaffer J.M., Smithgall T.E.; RT "The KRAB-associated co-repressor KAP-1 is a coiled-coil binding RT partner, substrate and activator of the c-Fes protein tyrosine RT kinase."; RL Biochem. J. 399:141-150(2006). RN [18] RP PHOSPHORYLATION AT SER-824, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=17178852; DOI=10.1158/0008-5472.CAN-06-4138; RA White D.E., Negorev D., Peng H., Ivanov A.V., Maul G.G., RA Rauscher F.J. III; RT "KAP1, a novel substrate for PIKK family members, colocalizes with RT numerous damage response factors at DNA lesions."; RL Cancer Res. 66:11594-11599(2006). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION RP 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; THR-541 AND RP SER-757, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [21] RP PHOSPHORYLATION AT SER-824, AND FUNCTION. RX PubMed=16862143; DOI=10.1038/ncb1446; RA Ziv Y., Bielopolski D., Galanty Y., Lukas C., Taya Y., Schultz D.C., RA Lukas J., Bekker-Jensen S., Bartek J., Shiloh Y.; RT "Chromatin relaxation in response to DNA double-strand breaks is RT modulated by a novel ATM- and KAP-1 dependent pathway."; RL Nat. Cell Biol. 8:870-876(2006). RN [22] RP INTERACTION WITH MAGEC2. RX PubMed=17942928; DOI=10.1158/0008-5472.CAN-07-1478; RA Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M., RA Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H., RA Ivanov A.V., Simpson A.J., Longley B.J.; RT "MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and RT suppress p53-dependent apoptosis in MAGE-positive cell lines."; RL Cancer Res. 67:9954-9962(2007). RN [23] RP INTERACTION WITH ZNF350, SUMOYLATION AT LYS-554; LYS-779 AND LYS-804, RP FUNCTION, AND MUTAGENESIS OF LYS-554; LYS-575; LYS-676; LYS-779 AND RP LYS-804. RX PubMed=17079232; DOI=10.1074/jbc.M606306200; RA Lee Y.K., Thomas S.N., Yang A.J., Ann D.K.; RT "Doxorubicin down-regulates Kruppel-associated box domain-associated RT protein 1 sumoylation that relieves its transcription repression on RT p21WAF1/CIP1 in breast cancer MCF-7 cells."; RL J. Biol. Chem. 282:1595-1606(2007). RN [24] RP INTERACTION WITH E2F1, AND FUNCTION. RX PubMed=17704056; DOI=10.1074/jbc.M704757200; RA Wang C., Rauscher F.J. III, Cress W.D., Chen J.; RT "Regulation of E2F1 function by the nuclear corepressor KAP1."; RL J. Biol. Chem. 282:29902-29909(2007). RN [25] RP PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, AND MUTAGENESIS OF RP LEU-306; LYS-554; LYS-779; LYS-804 AND SER-824. RX PubMed=17942393; DOI=10.1074/jbc.M706912200; RA Li X., Lee Y.K., Jeng J.C., Yen Y., Schultz D.C., Shih H.M., Ann D.K.; RT "Role for KAP1 serine 824 phosphorylation and RT sumoylation/desumoylation switch in regulating KAP1-mediated RT transcriptional repression."; RL J. Biol. Chem. 282:36177-36189(2007). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [27] RP SUMOYLATION, FUNCTION, DOMAIN PHD-TYPE, INTERACTION WITH CHD3 AND RP SETDB1, AND MUTAGENESIS OF LYS-554; LYS-575; CYS-651; LYS-676; RP LYS-750; LYS-779 AND LYS-804. RX PubMed=18082607; DOI=10.1016/j.molcel.2007.11.012; RA Ivanov A.V., Peng H., Yurchenko V., Yap K.L., Negorev D.G., RA Schultz D.C., Psulkowski E., Fredericks W.J., White D.E., Maul G.G., RA Sadofsky M.J., Zhou M.M., Rauscher F.J. III; RT "PHD domain-mediated E3 ligase activity directs intramolecular RT sumoylation of an adjacent bromodomain required for gene silencing."; RL Mol. Cell 28:823-837(2007). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [29] RP INTERACTION WITH ZNF256, AND FUNCTION. RX PubMed=18060868; DOI=10.1016/j.bbrc.2007.11.118; RA Suzuki C., Murakumo Y., Kawase Y., Sato T., Morinaga T., Fukuda N., RA Enomoto A., Ichihara M., Takahashi M.; RT "A novel GDNF-inducible gene, BMZF3, encodes a transcriptional RT repressor associated with KAP-1."; RL Biochem. Biophys. Res. Commun. 366:226-232(2008). RN [30] RP INTERACTION WITH SMARCAD1. RX PubMed=18675275; DOI=10.1016/j.jmb.2008.07.031; RA Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T., RA Ohara O., Koga H.; RT "The novel protein complex with SMARCAD1/KIAA1122 binds to the RT vicinity of TSS."; RL J. Mol. Biol. 382:257-265(2008). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-439; SER-471; RP SER-473; SER-489; SER-752 AND SER-757, AND IDENTIFICATION BY MASS RP 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 [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-501 AND RP SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [36] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304; LYS-340; LYS-377; RP LYS-770 AND LYS-774, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [37] RP SUMOYLATION AT LYS-779. RC TISSUE=Cervix carcinoma; RX PubMed=20388717; DOI=10.1074/jbc.M110.106955; RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., RA Eriksson J.E., Sistonen L.; RT "In vivo identification of sumoylation sites by a signature tag and RT cysteine-targeted affinity purification."; RL J. Biol. Chem. 285:19324-19329(2010). RN [38] RP INTERACTION WITH ERBB4 AND MDM2 IN THE TRIM28/KAP1-ERBB4-MDM2 COMPLEX RP AND WITH MDM2 AND P53/TP53 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX, RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=20858735; DOI=10.1158/1541-7786.MCR-10-0042; RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.; RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA RT damage response pathways."; RL Mol. Cancer Res. 8:1388-1398(2010). RN [39] RP FUNCTION, UBIQUITINATION, AND INTERACTION WITH MAGEC2. RX PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029; RA Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.; RT "MAGE-RING protein complexes comprise a family of E3 ubiquitin RT ligases."; RL Mol. Cell 39:963-974(2010). RN [40] RP INTERACTION WITH CBX5 AND POGZ, AND MUTAGENESIS OF VAL-488 AND RP LEU-490. RX PubMed=20562864; DOI=10.1038/ncb2075; RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., RA Kimura H., Obuse C.; RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome RT arms through Aurora B activation."; RL Nat. Cell Biol. 12:719-727(2010). RN [41] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-19; SER-473; SER-489; THR-541; SER-697; SER-752 RP AND SER-757, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [42] RP PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, INTERACTION WITH RP PPP1CA AND PPP1CB, AND MUTAGENESIS OF PHE-370; SER-440; SER-501 AND RP SER-824. RX PubMed=20424263; DOI=10.1126/scisignal.2000781; RA Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.; RT "SUMOylation of the transcriptional co-repressor KAP1 is regulated by RT the serine and threonine phosphatase PP1."; RL Sci. Signal. 3:RA32-RA32(2010). RN [43] 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., RA Buerckstuemmer T., 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 [44] RP FUNCTION AS SUMO LIGASE, AND INTERACTION WITH IRF7. RX PubMed=21940674; DOI=10.4049/jimmunol.1101704; RA Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H., RA Rauscher F.J. III, Ozato K., Zhu F.; RT "Tripartite motif-containing protein 28 is a small ubiquitin-related RT modifier E3 ligase and negative regulator of IFN regulatory factor RT 7."; RL J. Immunol. 187:4754-4763(2011). RN [45] RP INTERACTION WITH SMARCAD1. RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036; RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., RA Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., RA Varga-Weisz P., Mermoud J.E.; RT "Maintenance of silent chromatin through replication requires SWI/SNF- RT like chromatin remodeler SMARCAD1."; RL Mol. Cell 42:285-296(2011). RN [46] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-19; SER-473; SER-479 AND SER-683, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [47] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [48] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP 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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [49] RP FUNCTION, INTERACTION WITH ZNF268; KOX1 AND ZNF300, SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF CYS-65 AND CYS-68. RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4; RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M., RA Huang Z.; RT "Novel activity of KRAB domain that functions to reinforce nuclear RT localization of KRAB-containing zinc finger proteins by interacting RT with KAP1."; RL Cell. Mol. Life Sci. 70:3947-3958(2013). RN [50] RP FUNCTION, AND INTERACTION WITH ZFP90. RX PubMed=23543754; DOI=10.4049/jimmunol.1203561; RA Huang C., Martin S., Pfleger C., Du J., Buckner J.H., Bluestone J.A., RA Riley J.L., Ziegler S.F.; RT "Cutting Edge: a novel, human-specific interacting protein couples RT FOXP3 to a chromatin-remodeling complex that contains KAP1/TRIM28."; RL J. Immunol. 190:4470-4473(2013). RN [51] RP INTERACTION WITH SETX. RX PubMed=23149945; DOI=10.1128/MCB.01195-12; RA Yuce O., West S.C.; RT "Senataxin, defective in the neurodegenerative disorder ataxia with RT oculomotor apraxia 2, lies at the interface of transcription and the RT DNA damage response."; RL Mol. Cell. Biol. 33:406-417(2013). RN [52] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-501; THR-541; RP SER-594; SER-683 AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [53] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-199; LYS-254; RP LYS-261; LYS-319; LYS-366; LYS-377; LYS-434; LYS-469; LYS-575; RP LYS-750; LYS-770; LYS-774 AND LYS-779, AND IDENTIFICATION BY MASS RP 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 [54] RP STRUCTURE BY NMR OF 619-688 IN COMPLEX WITH ZINC IONS. RX PubMed=11226167; DOI=10.1093/emboj/20.1.165; RA Capili A.D., Schultz D.C., Rauscher F.J. III, Borden K.L.; RT "Solution structure of the PHD domain from the KAP-1 corepressor: RT structural determinants for PHD, RING and LIM zinc-binding domains."; RL EMBO J. 20:165-177(2001). RN [55] RP STRUCTURE BY NMR OF 624-812 OF WILD TYPE AND IN COMPLEX WITH UBE2I, RP SUMOYLATION AT LYS-676; LYS-750; LYS-779 AND LYS-804, AND MUTAGENESIS RP OF CYS-651; LEU-653; LEU-668 AND LEU-709. RX PubMed=18488044; DOI=10.1038/nsmb.1416; RA Zeng L., Yap K.L., Ivanov A.V., Wang X., Mujtaba S., Plotnikova O., RA Rauscher F.J. III, Zhou M.M.; RT "Structural insights into human KAP1 PHD finger-bromodomain and its RT role in gene silencing."; RL Nat. Struct. Mol. Biol. 15:626-633(2008). RN [56] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 201-250. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of ms1043."; RL Submitted (FEB-2009) to the PDB data bank. RN [57] RP VARIANT [LARGE SCALE ANALYSIS] MET-794. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Nuclear corepressor for KRAB domain-containing zinc CC finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CC CHD3, a subunit of the nucleosome remodeling and deacetylation CC (NuRD) complex, and SETDB1 (which specifically methylates histone CC H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target CC genes. Enhances transcriptional repression by coordinating the CC increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' CC acetylation (H3K9ac and H3K14ac, respectively) and the disposition CC of HP1 proteins to silence gene expression. Recruitment of SETDB1 CC induces heterochromatinization. May play a role as a coactivator CC for CEBPB and NR3C1 in the transcriptional activation of ORM1. CC Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating CC E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May CC serve as a partial backup to prevent E2F1-mediated apoptosis in CC the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has CC E3 SUMO-protein ligase activity toward itself via its PHD-type CC zinc finger. Also specifically sumoylates IRF7, thereby inhibiting CC its transactivation activity. Ubiquitinates p53/TP53 leading to CC its proteosomal degradation; the function is enhanced by MAGEC2 CC and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear CC localization of KOX1, ZNF268 and ZNF300 transcription factors. In CC association with isoform 2 of ZFP90, is required for the CC transcriptional repressor activity of FOXP3 and the suppressive CC function of regulatory T-cells (Treg) (PubMed:23543754). CC {ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11959841, CC ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:16107876, CC ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17079232, CC ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17704056, CC ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18060868, CC ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:20424263, CC ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041, CC ECO:0000269|PubMed:21940674, ECO:0000269|PubMed:23543754, CC ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:8769649, CC ECO:0000269|PubMed:9016654}. CC -!- PATHWAY: Protein modification; protein sumoylation. CC -!- SUBUNIT: Interacts with SETX (PubMed:23149945). Oligomer; the RBCC CC domain homotrimerizes and interacts with one molecule of KRAB to CC form the KRAB-KAP1 corepressor complex. Binding to a KRAB domain CC is an absolute requirement for silencing gene expression. CC Interacts with CEBPB and NR3C1. Interacts with a number of KRAB- CC ZFP proteins including ZNF10, ZFP53, ZFP68, ZNF382 and ZNF256. CC Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via CC the RING-type and PHD-type zinc fingers). Component of a ternary CC complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5), CC a KRAB domain-containing protein, and DNA. Interacts with CBX5 CC (via the PxVxL motif); the interaction occurs in interphase nuclei CC and competes for binding POGZ. Interacts with POGZ; the CC interaction competes for interaction with CBX5. Interacts with CC SETDB1; the interaction is enhanced by KAP1 sumoylation, CC stimulates SETB1 histone methyltransferase activity and gene CC silencing. Interacts (via the PHD-type zinc finger) with UBE2I; CC the interaction is required for sumoylation and repressor CC activity. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved CC in connecting growth factor and DNA damage responses. Interacts CC directly with ERBB4; the interaction represses ERBB4-mediated CC transcription activity. Interacts with MDM2; the interaction CC contributes to p53/TP53 inactivation. Component of the CC TRIM28/KAP1-MDM2-p53/TP53; involved in regulating p53/TP53 CC stabilization and activity. Interacts (via the leucine zipper CC alpha helical coiled-coil) with E2F1 (central region); the CC interaction inhibits E2F1 acetylation and transcriptional CC activity. Interacts with PPP1CA; the interaction dephosphorylates CC TRIM28 at Ser-824 and forms a complex at the p21 promoter site. CC Interacts with PPP1CB; the interaction is weak but is increased on CC dephosphorylation at Ser-824. Interacts with FES/FPS. Interacts CC with SMARCAD1. Interacts with, and sumoylates IRF7. Interacts with CC MAGEC2. Part of a complex composed of TRIM28, HDAC1, HDAC2 and CC EHMT2. Interacts with AICDA (By similarity). Interacts (via the CC RBCC domain) with KOX1 (via the KRAB domain), ZNF268 (via the KRAB CC domain) and ZNF300 (via the KRAB domain); the interactions CC increase KOX1, ZNF268 and ZNF300 nuclear localization activities. CC The large PER complex involved in the histone methylation is CC composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CC CBX3 mediates the formation of the complex. Interacts with isoform CC 2 of ZFP90. Forms a complex with FOXP3 in the presence of isoform CC 2 of ZFP90. Interacts with NR4A3; the interactions potentiates CC NR4A3 activity on NurRE promoter (By similarity). CC {ECO:0000250|UniProtKB:Q62318, ECO:0000269|PubMed:10330177, CC ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11013263, CC ECO:0000269|PubMed:11226167, ECO:0000269|PubMed:11230151, CC ECO:0000269|PubMed:11959841, ECO:0000269|PubMed:15882967, CC ECO:0000269|PubMed:16107876, ECO:0000269|PubMed:16792528, CC ECO:0000269|PubMed:17056014, ECO:0000269|PubMed:17079232, CC ECO:0000269|PubMed:17512541, ECO:0000269|PubMed:17704056, CC ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:18060868, CC ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:18488044, CC ECO:0000269|PubMed:18675275, ECO:0000269|PubMed:20424263, CC ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:20858735, CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:21549307, CC ECO:0000269|PubMed:21940674, ECO:0000269|PubMed:23149945, CC ECO:0000269|PubMed:23543754, ECO:0000269|PubMed:23665872, CC ECO:0000269|PubMed:9016654}. CC -!- INTERACTION: CC Q13185:CBX3; NbExp=3; IntAct=EBI-78139, EBI-78176; CC P23198:Cbx3 (xeno); NbExp=2; IntAct=EBI-78139, EBI-78162; CC P45973:CBX5; NbExp=9; IntAct=EBI-78139, EBI-78219; CC P43356:MAGEA2B; NbExp=6; IntAct=EBI-78139, EBI-5650739; CC P43357:MAGEA3; NbExp=3; IntAct=EBI-78139, EBI-5651459; CC P43360:MAGEA6; NbExp=2; IntAct=EBI-78139, EBI-1045155; CC Q9UBF1:MAGEC2; NbExp=14; IntAct=EBI-78139, EBI-5651487; CC Q9HCI5:MAGEE1; NbExp=2; IntAct=EBI-78139, EBI-949966; CC O75376:NCOR1; NbExp=4; IntAct=EBI-78139, EBI-347233; CC Q9BQF6:SENP7; NbExp=2; IntAct=EBI-78139, EBI-766251; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330177, CC ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:20858735, CC ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:9016654}. CC Note=Associated with centromeric heterochromatin during cell CC differentiation through CBX1. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13263-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13263-2; Sequence=VSP_010898; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including CC spleen, thymus, prostate, testis, ovary, small intestine, colon CC and peripheral blood leukocytes. {ECO:0000269|PubMed:9016654}. CC -!- DOMAIN: The HP1 box is both necessary and sufficient for HP1 CC binding. {ECO:0000269|PubMed:18082607}. CC -!- DOMAIN: The PHD-type zinc finger enhances CEBPB transcriptional CC activity. The PHD-type zinc finger, the HP1 box and the bromo CC domain, function together to assemble the machinery required for CC repression of KRAB domain-containing proteins. Acts as an CC intramolecular SUMO E3 ligase for autosumoylation of bromodomain. CC {ECO:0000269|PubMed:18082607}. CC -!- DOMAIN: The RING-finger-B Box-coiled-coil/tripartite motif CC (RBCC/TRIM motif) is required for interaction with the KRAB domain CC of KRAB-zinc finger proteins. Binds four zinc ions per molecule. CC The RING finger and the N-terminal of the leucine zipper alpha CC helical coiled-coil region of RBCC are required for CC oligomerization. {ECO:0000269|PubMed:18082607}. CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is CC required for interaction with chromoshadow domains. This motif CC requires additional residues -7, -6, +4 and +5 of the central Val CC which contact the chromoshadow domain. CC {ECO:0000269|PubMed:18082607}. CC -!- PTM: ATM-induced phosphorylation on Ser-824 represses sumoylation CC leading to the de-repression of expression of a subset of genes CC involved in cell cycle control and apoptosis in response to CC genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA CC and PP1CB forms, allows sumoylation and expression of TRIM28 CC target genes. {ECO:0000269|PubMed:16862143, CC ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17942393, CC ECO:0000269|PubMed:20424263}. CC -!- PTM: Sumoylation/desumoylation events regulate TRIM28-mediated CC transcriptional repression. Sumoylation is required for CC interaction with CHD3 and SETDB1 and the corepressor activity. CC Represses and is repressed by Ser-824 phosphorylation. Enhances CC the TRIM28 corepressor activity, inhibiting transcriptional CC activity of a number of genes including GADD45A and CDKN1A/p21. CC Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation. CC In response to Dox-induced DNA damage, enhanced phosphorylation on CC Ser-824 prevents sumoylation and allows de-repression of CC CDKN1A/p21. {ECO:0000269|PubMed:16862143, CC ECO:0000269|PubMed:17079232, ECO:0000269|PubMed:17178852, CC ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18488044, CC ECO:0000269|PubMed:20388717, ECO:0000269|PubMed:20424263}. CC -!- PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2. CC {ECO:0000269|PubMed:20864041}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 B box-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00024}. CC -!- SIMILARITY: Contains 1 bromo domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. {ECO:0000255|PROSITE- CC ProRule:PRU00146}. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00175}. 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; U78773; AAB37341.1; -; mRNA. DR EMBL; X97548; CAA66150.1; -; mRNA. DR EMBL; U95040; AAB51517.1; -; mRNA. DR EMBL; BC004978; AAH04978.1; -; mRNA. DR EMBL; BC007390; AAH07390.2; -; mRNA. DR EMBL; BC052986; AAH52986.1; -; mRNA. DR EMBL; U31657; AAA74954.1; -; mRNA. DR CCDS; CCDS12985.1; -. [Q13263-1] DR PIR; G01950; G01950. DR RefSeq; NP_005753.1; NM_005762.2. [Q13263-1] DR UniGene; Hs.467408; -. DR PDB; 1FP0; NMR; -; A=619-679. DR PDB; 2RO1; NMR; -; A=624-812. DR PDB; 2YVR; X-ray; 1.80 A; A/B=201-250. DR PDBsum; 1FP0; -. DR PDBsum; 2RO1; -. DR PDBsum; 2YVR; -. DR ProteinModelPortal; Q13263; -. DR SMR; Q13263; 203-247, 624-812. DR BioGrid; 115457; 255. DR DIP; DIP-30891N; -. DR IntAct; Q13263; 57. DR MINT; MINT-5001244; -. DR STRING; 9606.ENSP00000253024; -. DR PhosphoSite; Q13263; -. DR BioMuta; TRIM28; -. DR DMDM; 3183179; -. DR MaxQB; Q13263; -. DR PaxDb; Q13263; -. DR PeptideAtlas; Q13263; -. DR PRIDE; Q13263; -. DR DNASU; 10155; -. DR Ensembl; ENST00000253024; ENSP00000253024; ENSG00000130726. [Q13263-1] DR Ensembl; ENST00000341753; ENSP00000342232; ENSG00000130726. [Q13263-2] DR GeneID; 10155; -. DR KEGG; hsa:10155; -. DR UCSC; uc002qtg.1; human. [Q13263-1] DR UCSC; uc010eut.1; human. [Q13263-2] DR CTD; 10155; -. DR GeneCards; TRIM28; -. DR HGNC; HGNC:16384; TRIM28. DR HPA; CAB010066; -. DR HPA; HPA064033; -. DR MIM; 601742; gene. DR neXtProt; NX_Q13263; -. DR PharmGKB; PA38131; -. DR eggNOG; ENOG410ITES; Eukaryota. DR eggNOG; ENOG41102KI; LUCA. DR GeneTree; ENSGT00530000062982; -. DR HOGENOM; HOG000137674; -. DR HOVERGEN; HBG055353; -. DR InParanoid; Q13263; -. DR KO; K08882; -. DR OMA; ANQQKCE; -. DR OrthoDB; EOG790FZZ; -. DR PhylomeDB; Q13263; -. DR TreeFam; TF106455; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q13263; -. DR UniPathway; UPA00886; -. DR ChiTaRS; TRIM28; human. DR EvolutionaryTrace; Q13263; -. DR GeneWiki; TRIM28; -. DR GenomeRNAi; 10155; -. DR NextBio; 38440; -. DR PMAP-CutDB; Q13263; -. DR PRO; PR:Q13263; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; Q13263; -. DR CleanEx; HS_TRIM28; -. DR ExpressionAtlas; Q13263; baseline and differential. DR Genevisible; Q13263; HS. DR GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl. DR GO; GO:0005720; C:nuclear heterochromatin; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL. DR GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0035851; F:Krueppel-associated box domain binding; IDA:UniProtKB. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IEA:Ensembl. DR GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl. DR GO; GO:0043045; P:DNA methylation involved in embryo development; IEA:Ensembl. DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0060669; P:embryonic placenta morphogenesis; IEA:Ensembl. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:1901536; P:negative regulation of DNA demethylation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB. DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB. DR GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:GOC. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC. DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl. DR GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB. DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:GOC. DR GO; GO:2000653; P:regulation of genetic imprinting; IEA:Ensembl. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR Gene3D; 1.20.920.10; -; 1. DR Gene3D; 3.30.40.10; -; 2. DR InterPro; IPR003649; Bbox_C. DR InterPro; IPR001487; Bromodomain. 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 Pfam; PF00628; PHD; 1. DR Pfam; PF00643; zf-B_box; 2. DR Pfam; PF14634; zf-RING_5; 1. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 2. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00184; RING; 2. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS50119; ZF_BBOX; 2. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Citrullination; KW Complete proteome; Direct protein sequencing; Isopeptide bond; Ligase; KW Metal-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Ubl conjugation pathway; KW Zinc; Zinc-finger. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000269|Ref.5, ECO:0000269|Ref.6}. FT CHAIN 2 835 Transcription intermediary factor 1-beta. FT /FTId=PRO_0000056392. FT DOMAIN 697 801 Bromo. FT ZN_FING 65 121 RING-type. {ECO:0000255|PROSITE- FT ProRule:PRU00175}. FT ZN_FING 148 195 B box-type 1; atypical. FT {ECO:0000255|PROSITE-ProRule:PRU00024}. FT ZN_FING 204 245 B box-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00024}. FT ZN_FING 625 672 PHD-type. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT REGION 65 376 RBCC domain. FT REGION 246 376 Leucine zipper alpha helical coiled-coil FT region. FT REGION 247 376 Interaction with MAGEC2. FT REGION 366 370 Involved in binding PPP1CA. FT REGION 476 513 HP1 box. FT MOTIF 481 494 PxVxL motif. FT COMPBIAS 2 58 Ala-rich. FT COMPBIAS 526 530 Poly-Ala. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000269|Ref.5, ECO:0000269|Ref.6}. FT MOD_RES 19 19 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 50 50 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 266 266 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q62318}. FT MOD_RES 304 304 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 340 340 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 377 377 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 437 437 Phosphoserine. FT {ECO:0000250|UniProtKB:Q62318}. FT MOD_RES 439 439 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 470 470 Citrulline. {ECO:0000250}. FT MOD_RES 471 471 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 472 472 Citrulline. {ECO:0000250}. FT MOD_RES 473 473 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 479 479 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 489 489 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 501 501 Phosphoserine. FT {ECO:0000244|PubMed:17525332, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 541 541 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 594 594 Phosphoserine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 683 683 Phosphoserine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 689 689 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 697 697 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 752 752 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 755 755 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q62318}. FT MOD_RES 757 757 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 770 770 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 774 774 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 779 779 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q62318}. FT MOD_RES 824 824 Phosphoserine; by ATM and ATR and dsDNA FT kinase. {ECO:0000269|PubMed:16862143, FT ECO:0000269|PubMed:17178852, FT ECO:0000269|PubMed:17942393, FT ECO:0000269|PubMed:20424263}. FT CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 199 199 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 319 319 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 377 377 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 434 434 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 554 554 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT CROSSLNK 575 575 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO); FT alternate. FT CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 770 770 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 774 774 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO1); FT alternate. FT CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 804 804 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT VAR_SEQ 114 195 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_010898. FT VARIANT 794 794 T -> M (in dbSNP:rs56229738). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_042386. FT MUTAGEN 65 65 C->A: Reduces nuclear localization FT activity of ZNF268; when associated with FT A-68. {ECO:0000269|PubMed:23665872}. FT MUTAGEN 68 68 C->A: Reduces nuclear localization FT activity of ZNF268; when associated with FT A-65. {ECO:0000269|PubMed:23665872}. FT MUTAGEN 306 306 L->P: Disrupts the interaction with FT ZNF350 and amost competely relieves the FT transcription repressive effect of FT sumoylated TRIM28. FT {ECO:0000269|PubMed:17942393}. FT MUTAGEN 366 366 K->G: Greatly reduced interaction with FT PPP1CA. FT MUTAGEN 368 368 I->G: Increased interaction with PPP1CA. FT Greatly decreased phosphorylation on S- FT 824. FT MUTAGEN 370 370 F->A: Some reduction in interaction with FT PPP1CA. {ECO:0000269|PubMed:20424263}. FT MUTAGEN 370 370 F->G: Some reduction in interaction with FT PPP1CA. {ECO:0000269|PubMed:20424263}. FT MUTAGEN 440 440 S->A: No effect on interaction with FT PPP1CA nor on sumoylation levels. FT Decreased sumoylation levels; when FT associated with D-501 and D-824. FT {ECO:0000269|PubMed:20424263}. FT MUTAGEN 488 488 V->E: Abolishes interaction with CBX5; FT when associated with E-490. FT {ECO:0000269|PubMed:20562864}. FT MUTAGEN 490 490 L->E: Abolishes interaction with CBX5; FT when associated with E-488. FT {ECO:0000269|PubMed:20562864}. FT MUTAGEN 501 501 S->A: No effect on interaction with FT PPP1CA nor on sumoylation levels. FT Decreased sumoylation levels; when FT associated with D-440 and D-824. FT {ECO:0000269|PubMed:20424263}. FT MUTAGEN 554 554 K->R: Moderately reduces sumoylation and FT repression. Abolishes both sumoylation FT and repression; when associated with R- FT 575. Relieves the repressor activity on FT Dox-induced GADD45A transcription and 2- FT fold increase in phosphorylation at Ser- FT 824; when associated with R-779 and R- FT 804. {ECO:0000269|PubMed:17079232, FT ECO:0000269|PubMed:17942393, FT ECO:0000269|PubMed:18082607}. FT MUTAGEN 575 575 K->R: Modestly reduced sumoylation and FT repression. Abolishes both sumoylation FT and repression; when associated with R- FT 554. {ECO:0000269|PubMed:17079232, FT ECO:0000269|PubMed:18082607}. FT MUTAGEN 651 651 C->A: Complete loss of the PHD finger- FT mediated stimulatory effect on FT sumoylation. Loss of binding UBE2I. FT {ECO:0000269|PubMed:18082607, FT ECO:0000269|PubMed:18488044}. FT MUTAGEN 653 653 L->A: Greatly reduced sumoylation. Little FT further effect on sumoylation; when FT associated with A-668 and/or A-709. FT {ECO:0000269|PubMed:18488044}. FT MUTAGEN 668 668 L->A: Little effect on sumoylation. FT Little further effect on sumoylation; FT when associated with A-653 and/or A-709. FT {ECO:0000269|PubMed:18488044}. FT MUTAGEN 676 676 K->R: Modestly reduces sumoylation and FT repression. {ECO:0000269|PubMed:17079232, FT ECO:0000269|PubMed:18082607}. FT MUTAGEN 709 709 L->A: Greatly reduced sumoylation. Little FT further effect on sumoylation; when FT associated with A-653 and/or A-668. FT {ECO:0000269|PubMed:18488044}. FT MUTAGEN 750 750 K->R: Some reduced sumoylation and FT repression. FT {ECO:0000269|PubMed:18082607}. FT MUTAGEN 779 779 K->R: Abolishes both sumoylation and FT repression; when associated with R-804. FT Relieves the repressor activity on Dox- FT induced GADD45A transcription and 2-fold FT increase in phosphorylation at Ser-824; FT when associated with R-554 and R-804. FT {ECO:0000269|PubMed:17079232, FT ECO:0000269|PubMed:17942393, FT ECO:0000269|PubMed:18082607}. FT MUTAGEN 804 804 K->R: Abolishes both sumoylation and FT repression; when associated with R-779. FT Relieves the repressor activity on Dox- FT induced GADD45A transcription and 2-fold FT increase in phosphorylation at Ser-824; FT when associated with R-554 and R-779. FT {ECO:0000269|PubMed:17079232, FT ECO:0000269|PubMed:17942393, FT ECO:0000269|PubMed:18082607}. FT MUTAGEN 824 824 S->A: Suppresses Dox-induced CDKN1A/p21 FT promoter activation. No effect on FT sumoylation levels. Decreased sumoylation FT levels; when associated with D-440 and D- FT 501. {ECO:0000269|PubMed:17942393, FT ECO:0000269|PubMed:20424263}. FT MUTAGEN 824 824 S->D: Enhances Dox-induced CDKN1A/p21 FT promoter activation. Decreased FT sumoylation with or without Dox- FT treatment. {ECO:0000269|PubMed:17942393, FT ECO:0000269|PubMed:20424263}. FT CONFLICT 162 162 A -> G (in Ref. 1; AAB37341). FT {ECO:0000305}. FT STRAND 210 212 {ECO:0000244|PDB:2YVR}. FT STRAND 219 221 {ECO:0000244|PDB:2YVR}. FT TURN 222 225 {ECO:0000244|PDB:2YVR}. FT STRAND 226 228 {ECO:0000244|PDB:2YVR}. FT HELIX 230 234 {ECO:0000244|PDB:2YVR}. FT TURN 235 239 {ECO:0000244|PDB:2YVR}. FT STRAND 242 244 {ECO:0000244|PDB:2YVR}. FT STRAND 620 626 {ECO:0000244|PDB:1FP0}. FT STRAND 629 631 {ECO:0000244|PDB:1FP0}. FT STRAND 633 635 {ECO:0000244|PDB:1FP0}. FT TURN 641 643 {ECO:0000244|PDB:2RO1}. FT STRAND 651 653 {ECO:0000244|PDB:1FP0}. FT STRAND 661 663 {ECO:0000244|PDB:1FP0}. FT TURN 666 669 {ECO:0000244|PDB:2RO1}. FT STRAND 684 690 {ECO:0000244|PDB:2RO1}. FT HELIX 698 713 {ECO:0000244|PDB:2RO1}. FT HELIX 717 721 {ECO:0000244|PDB:2RO1}. FT STRAND 730 732 {ECO:0000244|PDB:2RO1}. FT HELIX 740 748 {ECO:0000244|PDB:2RO1}. FT STRAND 750 753 {ECO:0000244|PDB:2RO1}. FT HELIX 758 775 {ECO:0000244|PDB:2RO1}. FT HELIX 783 799 {ECO:0000244|PDB:2RO1}. FT TURN 800 802 {ECO:0000244|PDB:2RO1}. SQ SEQUENCE 835 AA; 88550 MW; 2027BABB7C94FE20 CRC64; MAASAAAASA AAASAASGSP GPGEGSAGGE KRSTAPSAAA SASASAAASS PAGGGAEALE LLEHCGVCRE RLRPEREPRL LPCLHSACSA CLGPAAPAAA NSSGDGGAAG DGTVVDCPVC KQQCFSKDIV ENYFMRDSGS KAATDAQDAN QCCTSCEDNA PATSYCVECS EPLCETCVEA HQRVKYTKDH TVRSTGPAKS RDGERTVYCN VHKHEPLVLF CESCDTLTCR DCQLNAHKDH QYQFLEDAVR NQRKLLASLV KRLGDKHATL QKSTKEVRSS IRQVSDVQKR VQVDVKMAIL QIMKELNKRG RVLVNDAQKV TEGQQERLER QHWTMTKIQK HQEHILRFAS WALESDNNTA LLLSKKLIYF QLHRALKMIV DPVEPHGEMK FQWDLNAWTK SAEAFGKIVA ERPGTNSTGP APMAPPRAPG PLSKQGSGSS QPMEVQEGYG FGSGDDPYSS AEPHVSGVKR SRSGEGEVSG LMRKVPRVSL ERLDLDLTAD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA TGQPGTAPAG TPGAPPLAGM AIVKEEETEA AIGAPPTATE GPETKPVLMA LAEGPGAEGP RLASPSGSTS SGLEVVAPEG TSAPGGGPGT LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL HQLATDSTFS LDQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA DVQSIIGLQR FFETRMNEAF GDTKFSAVLV EPPPMSLPGA GLSSQELSGG PGDGP //