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 27-MAR-2024, entry version 260.
DE RecName: Full=Transcription intermediary factor 1-beta {ECO:0000305};
DE Short=TIF1-beta;
DE AltName: Full=E3 SUMO-protein ligase TRIM28;
DE EC=2.3.2.27;
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=RING-type E3 ubiquitin transferase TIF1-beta {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 28;
GN Name=TRIM28 {ECO:0000312|HGNC:HGNC:16384}; Synonyms=KAP1, RNF96, TIF1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=8769649; DOI=10.1101/gad.10.16.2067;
RA Friedman J.R., Fredericks W.J., Jensen D.E., Speicher D.W., Huang X.-P.,
RA 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 LOCATION,
RP 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., Schaffner W.;
RT "Transcriptional repression by RING finger protein TIF1 beta that interacts
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP 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 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 KRAB
RP 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., Harper S.L.,
RA Speicher D.W., Zhao K., Marmorstein R., Rock T.A., Rauscher F.J. III;
RT "The structurally disordered KRAB repression domain is incorporated into a
RT 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; DOI=10.1128/mcb.19.6.4366;
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 heterochromatic
RT and euchromatic HP1 proteins: a potential role for Kruppel-associated box-
RT zinc finger proteins in heterochromatin-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, KRAZ1
RT and KRAZ2, repress transcription through functional interaction with the
RT 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 components
RT of the mammalian SWI/SNF complex and the corepressor KAP-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 proteins: the
RT PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel
RT 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 euchromatic
RT genes by KRAB zinc-finger proteins.";
RL Genes Dev. 16:919-932(2002).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [15]
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 proteins
RT through a common motif that targets the chromoshadow domain.";
RL Biochem. Biophys. Res. Commun. 331:929-937(2005).
RN [16]
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., Rauscher F.J. III,
RA Chen J.;
RT "MDM2 interaction with nuclear corepressor KAP1 contributes to p53
RT inactivation.";
RL EMBO J. 24:3279-3290(2005).
RN [17]
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 Mdm2
RT interaction.";
RL Biochem. Biophys. Res. Commun. 351:216-222(2006).
RN [18]
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 partner,
RT substrate and activator of the c-Fes protein tyrosine kinase.";
RL Biochem. J. 399:141-150(2006).
RN [19]
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., Rauscher F.J. III;
RT "KAP1, a novel substrate for PIKK family members, colocalizes with numerous
RT damage response factors at DNA lesions.";
RL Cancer Res. 66:11594-11599(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; THR-541 AND SER-757, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [22]
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 modulated
RT by a novel ATM- and KAP-1 dependent pathway.";
RL Nat. Cell Biol. 8:870-876(2006).
RN [23]
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., Ivanov A.V.,
RA Simpson A.J., Longley B.J.;
RT "MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress
RT p53-dependent apoptosis in MAGE-positive cell lines.";
RL Cancer Res. 67:9954-9962(2007).
RN [24]
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 [25]
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 [26]
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 sumoylation/desumoylation
RT switch in regulating KAP1-mediated transcriptional repression.";
RL J. Biol. Chem. 282:36177-36189(2007).
RN [27]
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 cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [28]
RP SUMOYLATION AT LYS-750, FUNCTION, DOMAIN PHD-TYPE, INTERACTION WITH CHD3
RP AND SETDB1, AND MUTAGENESIS OF LYS-554; LYS-575; CYS-651; LYS-676; LYS-750;
RP 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., Schultz D.C.,
RA Psulkowski E., Fredericks W.J., White D.E., Maul G.G., Sadofsky M.J.,
RA Zhou M.M., Rauscher F.J. III;
RT "PHD domain-mediated E3 ligase activity directs intramolecular sumoylation
RT of an adjacent bromodomain required for gene silencing.";
RL Mol. Cell 28:823-837(2007).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
RP 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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [30]
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 repressor
RT associated with KAP-1.";
RL Biochem. Biophys. Res. Commun. 366:226-232(2008).
RN [31]
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 vicinity of
RT TSS.";
RL J. Mol. Biol. 382:257-265(2008).
RN [32]
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [33]
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 sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [34]
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 [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [36]
RP INTERACTION WITH RRP1B.
RX PubMed=19710015; DOI=10.1074/jbc.m109.023457;
RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B
RT (RRP1B) is a chromatin-associated factor.";
RL J. Biol. Chem. 284:28660-28673(2009).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-501 AND SER-594, 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 [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304; LYS-340; LYS-377; LYS-770
RP AND LYS-774, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [39]
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 [40]
RP INTERACTION WITH ERBB4 AND MDM2 IN THE TRIM28/KAP1-ERBB4-MDM2 COMPLEX AND
RP WITH MDM2 AND P53/TP53 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX, FUNCTION,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS 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 damage
RT response pathways.";
RL Mol. Cancer Res. 8:1388-1398(2010).
RN [41]
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 ligases.";
RL Mol. Cell 39:963-974(2010).
RN [42]
RP INTERACTION WITH CBX5 AND POGZ, AND MUTAGENESIS OF VAL-488 AND 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 arms
RT through Aurora B activation.";
RL Nat. Cell Biol. 12:719-727(2010).
RN [43]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-19; SER-473; SER-489; THR-541; SER-697; SER-752 AND
RP SER-757, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [44]
RP PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, INTERACTION WITH PPP1CA
RP AND PPP1CB, AND MUTAGENESIS OF LYS-366; ILE-368; PHE-370; SER-440; SER-501
RP AND 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 the
RT serine and threonine phosphatase PP1.";
RL Sci. Signal. 3:RA32-RA32(2010).
RN [45]
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 [46]
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 7.";
RL J. Immunol. 187:4754-4763(2011).
RN [47]
RP IDENTIFICATION IN A COMPLEX WITH EHMT2; HDAC1 AND HDAC2.
RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N.,
RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P.,
RA Mermoud J.E.;
RT "Maintenance of silent chromatin through replication requires SWI/SNF-like
RT chromatin remodeler SMARCAD1.";
RL Mol. Cell 42:285-296(2011).
RN [48]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-19; SER-473; SER-479 AND SER-683, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], 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 [49]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA 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 [50]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PHF13.
RX PubMed=23034801; DOI=10.1093/nar/gks868;
RA Mund A., Schubert T., Staege H., Kinkley S., Reumann K., Kriegs M.,
RA Fritsch L., Battisti V., Ait-Si-Ali S., Hoffbeck A.S., Soutoglou E.,
RA Will H.;
RT "SPOC1 modulates DNA repair by regulating key determinants of chromatin
RT compaction and DNA damage response.";
RL Nucleic Acids Res. 40:11363-11379(2012).
RN [51]
RP ERRATUM OF PUBMED:23034801.
RX PubMed=32890405; DOI=10.1093/nar/gkaa754;
RA Mund A., Schubert T., Staege H., Kinkley S., Reumann K., Kriegs M.,
RA Fritsch L., Battisti V., Ait-Si-Ali S., Hoffbeck A.S., Soutoglou E.,
RA Will H.;
RT "SPOC1 modulates DNA repair by regulating key determinants of chromatin
RT compaction and DNA damage response.";
RL Nucleic Acids Res. 48:10013-10014(2020).
RN [52]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [53]
RP FUNCTION, INTERACTION WITH ZNF268; KOX1 AND ZNF300, SUBCELLULAR LOCATION,
RP 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 with
RT KAP1.";
RL Cell. Mol. Life Sci. 70:3947-3958(2013).
RN [54]
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 FOXP3 to
RT a chromatin-remodeling complex that contains KAP1/TRIM28.";
RL J. Immunol. 190:4470-4473(2013).
RN [55]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-26; SER-138; SER-417;
RP SER-453; SER-473; SER-479; SER-489; THR-498; SER-501; THR-541; SER-752;
RP SER-757 AND SER-784, 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 [56]
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 DNA
RT damage response.";
RL Mol. Cell. Biol. 33:406-417(2013).
RN [57]
RP FUNCTION, POSSIBLE IDENTIFICATION IN A COREPRESSOR COMPLEX, AND
RP CHROMATIN-BINDING.
RX PubMed=24623306; DOI=10.7554/elife.02313;
RA Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
RT "A KRAS-directed transcriptional silencing pathway that mediates the CpG
RT island methylator phenotype.";
RL Elife 3:E02313-E02313(2014).
RN [58]
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., 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 [59]
RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION),
RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=24741090; DOI=10.1128/jvi.00596-14;
RA Sun R., Liang D., Gao Y., Lan K.;
RT "Kaposi's sarcoma-associated herpesvirus-encoded LANA interacts with host
RT KAP1 to facilitate establishment of viral latency.";
RL J. Virol. 88:7331-7344(2014).
RN [60]
RP INTERACTION WITH ZBTB1.
RX PubMed=24657165; DOI=10.1016/j.molcel.2014.02.017;
RA Kim H., Dejsuphong D., Adelmant G., Ceccaldi R., Yang K., Marto J.A.,
RA D'Andrea A.D.;
RT "Transcriptional repressor ZBTB1 promotes chromatin remodeling and
RT translesion DNA synthesis.";
RL Mol. Cell 54:107-118(2014).
RN [61]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-199; LYS-254; LYS-261;
RP LYS-319; LYS-366; LYS-377; LYS-434; LYS-469; LYS-575; LYS-750; LYS-770;
RP LYS-774 AND LYS-779, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [62]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-377; LYS-469; LYS-750 AND
RP LYS-779, AND 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 [63]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-377; LYS-469; LYS-750;
RP LYS-779 AND LYS-804, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [64]
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 [65]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-377; LYS-750 AND LYS-779, AND
RP IDENTIFICATION BY MASS 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 [66]
RP FUNCTION, INTERACTION WITH ATRX, AND FORMATION OF A COMPLEX WITH ATRX;
RP SETDB1 AND ZNF274.
RX PubMed=27029610; DOI=10.1080/15592294.2016.1169351;
RA Valle-Garcia D., Qadeer Z.A., McHugh D.S., Ghiraldini F.G., Chowdhury A.H.,
RA Hasson D., Dyer M.A., Recillas-Targa F., Bernstein E.;
RT "ATRX binds to atypical chromatin domains at the 3' exons of zinc finger
RT genes to preserve H3K9me3 enrichment.";
RL Epigenetics 11:398-414(2016).
RN [67]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-127; LYS-199; LYS-254;
RP LYS-261; LYS-272; LYS-304; LYS-319; LYS-377; LYS-407; LYS-434; LYS-469;
RP LYS-507; LYS-554; LYS-750; LYS-770; LYS-774; LYS-779 AND LYS-804, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [68]
RP INTERACTION WITH ZNF746.
RX PubMed=31856708; DOI=10.1186/s12860-019-0243-y;
RA Al Chiblak M., Steinbeck F., Thiesen H.J., Lorenz P.;
RT "DUF3669, a 'domain of unknown function' within ZNF746 and ZNF777,
RT oligomerizes and contributes to transcriptional repression.";
RL BMC Mol. Cell Biol. 20:60-60(2019).
RN [69]
RP INTERACTION WITH TRIM17.
RX PubMed=30042493; DOI=10.1038/s41418-018-0169-5;
RA Lionnard L., Duc P., Brennan M.S., Kueh A.J., Pal M., Guardia F., Mojsa B.,
RA Damiano M.A., Mora S., Lassot I., Ravichandran R., Cochet C.,
RA Aouacheria A., Potts P.R., Herold M.J., Desagher S., Kucharczak J.;
RT "TRIM17 and TRIM28 antagonistically regulate the ubiquitination and anti-
RT apoptotic activity of BCL2A1.";
RL Cell Death Differ. 26:902-917(2019).
RN [70]
RP INTERACTION WITH ZNF263.
RX PubMed=32051553; DOI=10.1038/s41388-020-1206-7;
RA Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C.,
RA Liu Q., Chen S., Wu M.;
RT "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma
RT epigenetically.";
RL Oncogene 39:3163-3178(2020).
RN [71]
RP INTERACTION WITH ZNF354C.
RX PubMed=33154469; DOI=10.1038/s41598-020-76193-0;
RA Oo J.A., Irmer B., Guenther S., Warwick T., Palfi K., Izquierdo Ponce J.,
RA Teichmann T., Pflueger-Mueller B., Gilsbach R., Brandes R.P.,
RA Leisegang M.S.;
RT "ZNF354C is a transcriptional repressor that inhibits endothelial
RT angiogenic sprouting.";
RL Sci. Rep. 10:19079-19079(2020).
RN [72]
RP INTERACTION WITH ZNF432.
RX PubMed=37823600; DOI=10.1093/nar/gkad791;
RA O'Sullivan J., Kothari C., Caron M.C., Gagne J.P., Jin Z., Nonfoux L.,
RA Beneyton A., Coulombe Y., Thomas M., Atalay N., Meng X.W., Milano L.,
RA Jean D., Boisvert F.M., Kaufmann S.H., Hendzel M.J., Masson J.Y.,
RA Poirier G.G.;
RT "ZNF432 stimulates PARylation and inhibits DNA resection to balance PARPi
RT sensitivity and resistance.";
RL Nucleic Acids Res. 0:0-0(2023).
RN [73]
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 [74]
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 OF
RP 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 role in
RT gene silencing.";
RL Nat. Struct. Mol. Biol. 15:626-633(2008).
RN [75]
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 [76]
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., 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: Nuclear corepressor for KRAB domain-containing zinc finger
CC proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a
CC subunit of the nucleosome remodeling and deacetylation (NuRD) complex,
CC and SETDB1 (which specifically methylates histone H3 at 'Lys-9'
CC (H3K9me)) to the promoter regions of KRAB target genes. Enhances
CC transcriptional repression by coordinating the increase in H3K9me, the
CC decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and
CC H3K14ac, respectively) and the disposition of HP1 proteins to silence
CC gene expression. Recruitment of SETDB1 induces heterochromatinization.
CC May play a role as a coactivator for CEBPB and NR3C1 in the
CC transcriptional activation of ORM1. Also a corepressor for ERBB4.
CC Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and
CC inhibiting E2F1 acetylation. May serve as a partial backup to prevent
CC E2F1-mediated apoptosis in the absence of RB1. Important regulator of
CC CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via
CC its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby
CC inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading
CC to its proteasomal degradation; the function is enhanced by MAGEC2 and
CC 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). Probably forms
CC a corepressor complex required for activated KRAS-mediated promoter
CC hypermethylation and transcriptional silencing of tumor suppressor
CC genes (TSGs) or other tumor-related genes in colorectal cancer (CRC)
CC cells (PubMed:24623306). Required to maintain a transcriptionally
CC repressive state of genes in undifferentiated embryonic stem cells
CC (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is
CC also required for H3K9me3 and silencing of endogenous and introduced
CC retroviruses in a DNA-methylation independent-pathway (By similarity).
CC Associates at promoter regions of tumor suppressor genes (TSGs) leading
CC to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274
CC complex may play a role in recruiting ATRX to the 3'-exons of zinc-
CC finger coding genes with atypical chromatin signatures to establish or
CC maintain/protect H3K9me3 at these transcriptionally active regions
CC (PubMed:27029610). {ECO:0000250|UniProtKB:Q62318,
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:24623306,
CC ECO:0000269|PubMed:27029610, ECO:0000269|PubMed:8769649,
CC ECO:0000269|PubMed:9016654}.
CC -!- FUNCTION: (Microbial infection) Plays a critical role in the shutdown
CC of lytic gene expression during the early stage of herpes virus 8
CC primary infection. This inhibition is mediated through interaction with
CC herpes virus 8 protein LANA1. {ECO:0000269|PubMed:24741090}.
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;
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 form
CC the KRAB-KAP1 corepressor complex. Binding to a KRAB domain is an
CC absolute requirement for silencing gene expression. Interacts with
CC CEBPB and NR3C1. Interacts with a number of KRAB-ZFP proteins including
CC ZNF10, ZFP53, ZFP68, ZNF382 and ZNF256. Interacts with NCOR1, NR3C1 and
CC CHD3. Interacts with CEBPB (via the RING-type and PHD-type zinc
CC fingers). Component of a ternary complex that includes TRIM28, a HP1
CC protein (CBX1, CBX3 OR CBX5), a KRAB domain-containing protein, and
CC DNA. Interacts with CBX5 (via the PxVxL motif); the interaction occurs
CC in interphase nuclei and competes for binding POGZ. Interacts with
CC POGZ; the interaction competes for interaction with CBX5. Interacts
CC with SETDB1; the interaction is enhanced by KAP1 sumoylation,
CC stimulates SETDB1 histone methyltransferase activity and gene
CC silencing. Interacts (via the PHD-type zinc finger) with UBE2I; the
CC interaction is required for sumoylation and repressor activity.
CC Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting
CC growth factor and DNA damage responses. Interacts directly with ERBB4;
CC the interaction represses ERBB4-mediated transcription activity.
CC Interacts with MDM2; the interaction contributes to p53/TP53
CC inactivation. Component of the TRIM28/KAP1-MDM2-p53/TP53; involved in
CC regulating p53/TP53 stabilization and activity. Interacts (via the
CC leucine zipper alpha helical coiled-coil) with E2F1 (central region);
CC the interaction inhibits E2F1 acetylation and transcriptional activity.
CC Interacts with PPP1CA; the interaction dephosphorylates TRIM28 at Ser-
CC 824 and forms a complex at the p21 promoter site. Interacts with
CC PPP1CB; the interaction is weak but is increased on dephosphorylation
CC at Ser-824. Interacts with FES/FPS. Interacts with SMARCAD1. Interacts
CC with, and sumoylates IRF7. Interacts with MAGEC2. Part of a complex
CC composed of TRIM28, HDAC1, HDAC2 and EHMT2 (PubMed:21549307). Interacts
CC with AICDA (By similarity). Interacts (via the RBCC domain) with KOX1
CC (via the KRAB domain), ZNF268 (via the KRAB domain) and ZNF300 (via the
CC KRAB domain); the interactions increase KOX1, ZNF268 and ZNF300 nuclear
CC localization activities. The large PER complex involved in the histone
CC methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or
CC SUV39H2; CBX3 mediates the formation of the complex. Interacts with
CC isoform 2 of ZFP90. Forms a complex with FOXP3 in the presence of
CC isoform 2 of ZFP90. Interacts with NR4A3; the interactions potentiates
CC NR4A3 activity on NurRE promoter (By similarity). Interacts
CC (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain)
CC (PubMed:24657165). Probably part of a corepressor complex containing
CC ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306). Interacts with
CC ATRX. Forms a complex with ATRX, SETDB1 and ZNF274 (PubMed:27029610).
CC Interacts with ZFP568; the interaction mediates ZFP568 transcriptional
CC repression activity (By similarity). Interacts with RRP1B
CC (PubMed:19710015). Interacts with CRY1 (By similarity). Interacts with
CC ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (PubMed:32051553).
CC Interacts with CYREN (via XLF motif) (By similarity). Interacts with
CC TRIM17; this interaction prevents TRIM28 activity (PubMed:30042493).
CC Interacts with ZNF746 (PubMed:31856708). Interacts with PHF13
CC (PubMed:23034801). Interacts with ZNF354C (PubMed:33154469). Interacts
CC with ZNF432; the interaction is independent of PARP1 (PubMed:37823600).
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:19710015,
CC ECO:0000269|PubMed:20424263, ECO:0000269|PubMed:20562864,
CC ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041,
CC ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21940674,
CC ECO:0000269|PubMed:23034801, ECO:0000269|PubMed:23149945,
CC ECO:0000269|PubMed:23543754, ECO:0000269|PubMed:23665872,
CC ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:24657165,
CC ECO:0000269|PubMed:27029610, ECO:0000269|PubMed:30042493,
CC ECO:0000269|PubMed:31856708, ECO:0000269|PubMed:32051553,
CC ECO:0000269|PubMed:33154469, ECO:0000269|PubMed:37823600,
CC ECO:0000269|PubMed:9016654}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein
CC LANA1; this interaction facilitates establishment of viral latency.
CC {ECO:0000269|PubMed:24741090}.
CC -!- INTERACTION:
CC Q13263; Q13185: CBX3; NbExp=4; IntAct=EBI-78139, EBI-78176;
CC Q13263; P45973: CBX5; NbExp=11; IntAct=EBI-78139, EBI-78219;
CC Q13263; Q12873: CHD3; NbExp=4; IntAct=EBI-78139, EBI-523590;
CC Q13263; P43356: MAGEA2B; NbExp=6; IntAct=EBI-78139, EBI-5650739;
CC Q13263; P43357: MAGEA3; NbExp=3; IntAct=EBI-78139, EBI-5651459;
CC Q13263; P43360: MAGEA6; NbExp=2; IntAct=EBI-78139, EBI-1045155;
CC Q13263; Q9UBF1: MAGEC2; NbExp=14; IntAct=EBI-78139, EBI-5651487;
CC Q13263; Q9HCI5: MAGEE1; NbExp=2; IntAct=EBI-78139, EBI-949966;
CC Q13263; O75376: NCOR1; NbExp=4; IntAct=EBI-78139, EBI-347233;
CC Q13263; Q9BQF6: SENP7; NbExp=3; IntAct=EBI-78139, EBI-766251;
CC Q13263; Q8TF47-3: ZFP90; NbExp=2; IntAct=EBI-78139, EBI-11419904;
CC Q13263; P83917: Cbx1; Xeno; NbExp=2; IntAct=EBI-78139, EBI-78119;
CC Q13263; P23198: Cbx3; Xeno; NbExp=2; IntAct=EBI-78139, EBI-78162;
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:24741090,
CC ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:9016654}.
CC Note=Associated with centromeric heterochromatin during cell
CC differentiation through CBX1 (By similarity). Localizes to sites of DNA
CC damage (PubMed:25593309). {ECO:0000250|UniProtKB:Q62318,
CC ECO:0000269|PubMed:25593309}.
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 -!- TISSUE SPECIFICITY: Expressed in all tissues tested including spleen,
CC thymus, prostate, testis, ovary, small intestine, colon and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:9016654}.
CC -!- DOMAIN: The HP1 box is both necessary and sufficient for HP1 binding.
CC {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 domain,
CC function together to assemble the machinery required for repression of
CC KRAB domain-containing proteins. Acts as an intramolecular SUMO E3
CC ligase for autosumoylation of bromodomain.
CC {ECO:0000269|PubMed:18082607}.
CC -!- DOMAIN: The RING-finger-B Box-coiled-coil/tripartite motif (RBCC/TRIM
CC motif) is required for interaction with the KRAB domain of KRAB-zinc
CC finger proteins. Binds four zinc ions per molecule. The RING finger and
CC the N-terminal of the leucine zipper alpha helical coiled-coil region
CC of RBCC are required for oligomerization.
CC {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 requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain. {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 genotoxic
CC stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms,
CC allows sumoylation and expression of TRIM28 target genes.
CC {ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17178852,
CC ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:20424263}.
CC -!- PTM: Sumoylation/desumoylation events regulate TRIM28-mediated
CC transcriptional repression. Sumoylation is required for interaction
CC with CHD3 and SETDB1 and the corepressor activity. Represses and is
CC repressed by Ser-824 phosphorylation. Enhances the TRIM28 corepressor
CC activity, inhibiting transcriptional activity of a number of genes
CC including GADD45A and CDKN1A/p21. Lys-554, Lys-779 and Lys-804 are the
CC major sites of sumoylation. In response to Dox-induced DNA damage,
CC enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-
CC repression of 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|UniProtKB:Q62318}.
CC -!- PTM: ADP-ribosylated by SIRT6, promoting TRIM28/KAP1 interaction with
CC CBX5, thereby contributing to the packaging of LINE-1 retrotransposon
CC elements into transcriptionally repressive heterochromatin.
CC {ECO:0000250|UniProtKB:Q62318}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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 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 PDB; 6H3A; X-ray; 5.50 A; A/F=53-434.
DR PDB; 6I9H; NMR; -; A=54-145.
DR PDB; 6QAJ; X-ray; 2.90 A; A/B=56-413.
DR PDB; 6QU1; X-ray; 3.70 A; A=53-434.
DR PDB; 7Z36; X-ray; 2.80 A; A/B=114-413.
DR PDBsum; 1FP0; -.
DR PDBsum; 2RO1; -.
DR PDBsum; 2YVR; -.
DR PDBsum; 6H3A; -.
DR PDBsum; 6I9H; -.
DR PDBsum; 6QAJ; -.
DR PDBsum; 6QU1; -.
DR PDBsum; 7Z36; -.
DR AlphaFoldDB; Q13263; -.
DR BMRB; Q13263; -.
DR SASBDB; Q13263; -.
DR SMR; Q13263; -.
DR BioGRID; 115457; 1408.
DR CORUM; Q13263; -.
DR DIP; DIP-30891N; -.
DR ELM; Q13263; -.
DR IntAct; Q13263; 196.
DR MINT; Q13263; -.
DR STRING; 9606.ENSP00000253024; -.
DR ChEMBL; CHEMBL3769297; -.
DR GlyGen; Q13263; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q13263; -.
DR MetOSite; Q13263; -.
DR PhosphoSitePlus; Q13263; -.
DR SwissPalm; Q13263; -.
DR BioMuta; TRIM28; -.
DR DMDM; 3183179; -.
DR CPTAC; CPTAC-446; -.
DR CPTAC; CPTAC-447; -.
DR EPD; Q13263; -.
DR jPOST; Q13263; -.
DR MassIVE; Q13263; -.
DR MaxQB; Q13263; -.
DR PaxDb; 9606-ENSP00000253024; -.
DR PeptideAtlas; Q13263; -.
DR ProteomicsDB; 59266; -. [Q13263-1]
DR ProteomicsDB; 59267; -. [Q13263-2]
DR Pumba; Q13263; -.
DR ABCD; Q13263; 2 sequenced antibodies.
DR Antibodypedia; 4109; 981 antibodies from 49 providers.
DR DNASU; 10155; -.
DR Ensembl; ENST00000253024.10; ENSP00000253024.4; ENSG00000130726.12. [Q13263-1]
DR Ensembl; ENST00000341753.10; ENSP00000342232.5; ENSG00000130726.12. [Q13263-2]
DR GeneID; 10155; -.
DR KEGG; hsa:10155; -.
DR MANE-Select; ENST00000253024.10; ENSP00000253024.4; NM_005762.3; NP_005753.1.
DR UCSC; uc002qtg.2; human. [Q13263-1]
DR AGR; HGNC:16384; -.
DR CTD; 10155; -.
DR DisGeNET; 10155; -.
DR GeneCards; TRIM28; -.
DR HGNC; HGNC:16384; TRIM28.
DR HPA; ENSG00000130726; Low tissue specificity.
DR MalaCards; TRIM28; -.
DR MIM; 601742; gene.
DR neXtProt; NX_Q13263; -.
DR OpenTargets; ENSG00000130726; -.
DR Orphanet; 654; Nephroblastoma.
DR PharmGKB; PA38131; -.
DR VEuPathDB; HostDB:ENSG00000130726; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160527; -.
DR HOGENOM; CLU_005817_2_0_1; -.
DR InParanoid; Q13263; -.
DR OMA; DCKDEVP; -.
DR OrthoDB; 56754at2759; -.
DR PhylomeDB; Q13263; -.
DR TreeFam; TF106455; -.
DR PathwayCommons; Q13263; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR SignaLink; Q13263; -.
DR SIGNOR; Q13263; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 10155; 174 hits in 1238 CRISPR screens.
DR ChiTaRS; TRIM28; human.
DR EvolutionaryTrace; Q13263; -.
DR GeneWiki; TRIM28; -.
DR GenomeRNAi; 10155; -.
DR Pharos; Q13263; Tbio.
DR PRO; PR:Q13263; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q13263; Protein.
DR Bgee; ENSG00000130726; Expressed in left testis and 102 other cell types or tissues.
DR ExpressionAtlas; Q13263; baseline and differential.
DR Genevisible; Q13263; HS.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
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:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; 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-UCL.
DR GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
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 DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:HGNC-UCL.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0043045; P:post-fertilization epigenetic regulation of gene expression; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR CDD; cd19846; Bbox1_TIF1b_C-VI; 1.
DR CDD; cd19829; Bbox2_TIF1b_C-VI; 1.
DR CDD; cd05502; Bromo_tif1_like; 1.
DR CDD; cd15623; PHD_TIF1beta; 1.
DR CDD; cd16765; RING-HC_TIF1beta; 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 InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037373; KAP1.
DR InterPro; IPR047059; TIF1b_Bbox1_Znf.
DR InterPro; IPR047058; TIF1b_Bbox2_Znf.
DR InterPro; IPR042713; TIF1beta_RING-HC.
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 PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR PANTHER; PTHR45915:SF9; TRIPARTITE MOTIF CONTAINING 28; 1.
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; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 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; ADP-ribosylation; Alternative splicing;
KW Chromatin regulator; Citrullination; Coiled coil;
KW Direct protein sequencing; Host-virus interaction; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..835
FT /note="Transcription intermediary factor 1-beta"
FT /id="PRO_0000056392"
FT DOMAIN 697..801
FT /note="Bromo"
FT ZN_FING 65..121
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 148..195
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 204..245
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 625..672
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..376
FT /note="RBCC domain"
FT REGION 246..376
FT /note="Leucine zipper alpha helical coiled-coil region"
FT REGION 247..376
FT /note="Interaction with MAGEC2"
FT REGION 366..370
FT /note="Involved in binding PPP1CA"
FT REGION 411..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..513
FT /note="HP1 box"
FT REGION 584..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 481..494
FT /note="PxVxL motif"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 304
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 377
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 472
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 755
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 770
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 774
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 779
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 824
FT /note="Phosphoserine; by ATM and ATR and dsDNA kinase"
FT /evidence="ECO:0000269|PubMed:16862143,
FT ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17942393,
FT ECO:0000269|PubMed:20424263"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 199
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 254
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 261
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 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 319
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 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 434
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 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:17079232"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 575
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:18488044"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:18082607"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 750
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 770
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 779
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 804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:17079232"
FT CROSSLNK 804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 114..195
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010898"
FT VARIANT 794
FT /note="T -> M (in dbSNP:rs56229738)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042386"
FT MUTAGEN 65
FT /note="C->A: Reduces nuclear localization activity of
FT ZNF268; when associated with A-68."
FT /evidence="ECO:0000269|PubMed:23665872"
FT MUTAGEN 68
FT /note="C->A: Reduces nuclear localization activity of
FT ZNF268; when associated with A-65."
FT /evidence="ECO:0000269|PubMed:23665872"
FT MUTAGEN 306
FT /note="L->P: Disrupts the interaction with ZNF350 and amost
FT completely relieves the transcription repressive effect of
FT sumoylated TRIM28."
FT /evidence="ECO:0000269|PubMed:17942393"
FT MUTAGEN 366
FT /note="K->G: Greatly reduced interaction with PPP1CA."
FT /evidence="ECO:0000269|PubMed:20424263"
FT MUTAGEN 368
FT /note="I->G: Increased interaction with PPP1CA. Greatly
FT decreased phosphorylation on S-824."
FT /evidence="ECO:0000269|PubMed:20424263"
FT MUTAGEN 370
FT /note="F->A: Some reduction in interaction with PPP1CA."
FT /evidence="ECO:0000269|PubMed:20424263"
FT MUTAGEN 370
FT /note="F->G: Some reduction in interaction with PPP1CA."
FT /evidence="ECO:0000269|PubMed:20424263"
FT MUTAGEN 440
FT /note="S->A: No effect on interaction with PPP1CA nor on
FT sumoylation levels. Decreased sumoylation levels; when
FT associated with D-501 and D-824."
FT /evidence="ECO:0000269|PubMed:20424263"
FT MUTAGEN 488
FT /note="V->E: Abolishes interaction with CBX5; when
FT associated with E-490."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 490
FT /note="L->E: Abolishes interaction with CBX5; when
FT associated with E-488."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 501
FT /note="S->A: No effect on interaction with PPP1CA nor on
FT sumoylation levels. Decreased sumoylation levels; when
FT associated with D-440 and D-824."
FT /evidence="ECO:0000269|PubMed:20424263"
FT MUTAGEN 554
FT /note="K->R: Moderately reduces sumoylation and repression.
FT Abolishes both sumoylation and repression; when associated
FT with R-575. Relieves the repressor activity on Dox-induced
FT GADD45A transcription and 2-fold increase in
FT phosphorylation at Ser-824; when associated with R-779 and
FT R-804."
FT /evidence="ECO:0000269|PubMed:17079232,
FT ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18082607"
FT MUTAGEN 575
FT /note="K->R: Modestly reduced sumoylation and repression.
FT Abolishes both sumoylation and repression; when associated
FT with R-554."
FT /evidence="ECO:0000269|PubMed:17079232,
FT ECO:0000269|PubMed:18082607"
FT MUTAGEN 651
FT /note="C->A: Complete loss of the PHD finger-mediated
FT stimulatory effect on sumoylation. Loss of binding UBE2I."
FT /evidence="ECO:0000269|PubMed:18082607,
FT ECO:0000269|PubMed:18488044"
FT MUTAGEN 653
FT /note="L->A: Greatly reduced sumoylation. Little further
FT effect on sumoylation; when associated with A-668 and/or A-
FT 709."
FT /evidence="ECO:0000269|PubMed:18488044"
FT MUTAGEN 668
FT /note="L->A: Little effect on sumoylation. Little further
FT effect on sumoylation; when associated with A-653 and/or A-
FT 709."
FT /evidence="ECO:0000269|PubMed:18488044"
FT MUTAGEN 676
FT /note="K->R: Modestly reduces sumoylation and repression."
FT /evidence="ECO:0000269|PubMed:17079232,
FT ECO:0000269|PubMed:18082607"
FT MUTAGEN 709
FT /note="L->A: Greatly reduced sumoylation. Little further
FT effect on sumoylation; when associated with A-653 and/or A-
FT 668."
FT /evidence="ECO:0000269|PubMed:18488044"
FT MUTAGEN 750
FT /note="K->R: Some reduced sumoylation and repression."
FT /evidence="ECO:0000269|PubMed:18082607"
FT MUTAGEN 779
FT /note="K->R: Abolishes both sumoylation and repression;
FT when associated with R-804. Relieves the repressor activity
FT on Dox-induced GADD45A transcription and 2-fold increase in
FT phosphorylation at Ser-824; when associated with R-554 and
FT R-804."
FT /evidence="ECO:0000269|PubMed:17079232,
FT ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18082607"
FT MUTAGEN 804
FT /note="K->R: Abolishes both sumoylation and repression;
FT when associated with R-779. Relieves the repressor activity
FT on Dox-induced GADD45A transcription and 2-fold increase in
FT phosphorylation at Ser-824; when associated with R-554 and
FT R-779."
FT /evidence="ECO:0000269|PubMed:17079232,
FT ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18082607"
FT MUTAGEN 824
FT /note="S->A: Suppresses Dox-induced CDKN1A/p21 promoter
FT activation. No effect on sumoylation levels. Decreased
FT sumoylation levels; when associated with D-440 and D-501."
FT /evidence="ECO:0000269|PubMed:17942393,
FT ECO:0000269|PubMed:20424263"
FT MUTAGEN 824
FT /note="S->D: Enhances Dox-induced CDKN1A/p21 promoter
FT activation. Decreased sumoylation with or without Dox-
FT treatment."
FT /evidence="ECO:0000269|PubMed:17942393,
FT ECO:0000269|PubMed:20424263"
FT CONFLICT 162
FT /note="A -> G (in Ref. 1; AAB37341)"
FT /evidence="ECO:0000305"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:7Z36"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:7Z36"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7Z36"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7Z36"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6I9H"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6I9H"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7Z36"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7Z36"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7Z36"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2YVR"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2YVR"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:2YVR"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2YVR"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:2YVR"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:2YVR"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2YVR"
FT HELIX 245..354
FT /evidence="ECO:0007829|PDB:7Z36"
FT HELIX 358..377
FT /evidence="ECO:0007829|PDB:7Z36"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:7Z36"
FT STRAND 620..626
FT /evidence="ECO:0007829|PDB:1FP0"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:1FP0"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:1FP0"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:2RO1"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:1FP0"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:1FP0"
FT TURN 666..669
FT /evidence="ECO:0007829|PDB:2RO1"
FT STRAND 684..690
FT /evidence="ECO:0007829|PDB:2RO1"
FT HELIX 698..713
FT /evidence="ECO:0007829|PDB:2RO1"
FT HELIX 717..721
FT /evidence="ECO:0007829|PDB:2RO1"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:2RO1"
FT HELIX 740..748
FT /evidence="ECO:0007829|PDB:2RO1"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:2RO1"
FT HELIX 758..775
FT /evidence="ECO:0007829|PDB:2RO1"
FT HELIX 783..799
FT /evidence="ECO:0007829|PDB:2RO1"
FT TURN 800..802
FT /evidence="ECO:0007829|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
//
