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Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)

 TIF1B_HUMAN             Reviewed;         835 AA.
Q13263; O00677; Q7Z632; Q93040; Q96IM1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
22-NOV-2017, entry version 215.
RecName: Full=Transcription intermediary factor 1-beta;
Short=TIF1-beta;
AltName: Full=E3 SUMO-protein ligase TRIM28;
EC=2.3.2.27;
AltName: Full=KRAB-associated protein 1;
Short=KAP-1;
AltName: Full=KRAB-interacting protein 1;
Short=KRIP-1;
AltName: Full=Nuclear corepressor KAP-1;
AltName: Full=RING finger protein 96;
AltName: Full=RING-type E3 ubiquitin transferase TIF1-beta {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 28;
Name=TRIM28; Synonyms=KAP1, RNF96, TIF1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=8769649; DOI=10.1101/gad.10.16.2067;
Friedman J.R., Fredericks W.J., Jensen D.E., Speicher D.W.,
Huang X.-P., Neilson E.G., Rauscher F.J. III;
"KAP-1, a novel corepressor for the highly conserved KRAB repression
domain.";
Genes Dev. 10:2067-2078(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ZNF10.
PubMed=9016654; DOI=10.1093/nar/24.24.4859;
Moosmann P.R., Georgiev O., le Douarin B., Bourquin J.-P.,
Schaffner W.;
"Transcriptional repression by RING finger protein TIF1 beta that
interacts with the KRAB repressor domain of KOX1.";
Nucleic Acids Res. 24:4859-4867(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Spleen;
Emison E.S., Lewis B.C., Shim H., Li Q., Dang C.V., Lee L.A.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 2-32; 408-427 AND 493-507, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V.;
Submitted (JAN-2010) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 486-835.
Lyle R., Hewitt J.E.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF N-TERMINUS, OLIGOMERIZATION, INTERACTION WITH THE
KRAB DOMAIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17512541; DOI=10.1016/j.jmb.2007.03.047;
Peng H., Gibson L.C., Capili A.D., Borden K.L., Osborne M.J.,
Harper S.L., Speicher D.W., Zhao K., Marmorstein R., Rock T.A.,
Rauscher F.J. III;
"The structurally disordered KRAB repression domain is incorporated
into a protease resistant core upon binding to KAP-1-RBCC domain.";
J. Mol. Biol. 370:269-289(2007).
[9]
INTERACTION WITH CBX1; CBX3 AND CBX5, AND SUBCELLULAR LOCATION.
PubMed=10330177; DOI=10.1128/MCB.19.6.4366;
Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R.,
Fredericks W.J., Rauscher F.J. III;
"KAP-1 corepressor protein interacts and colocalizes with
heterochromatic and euchromatic HP1 proteins: a potential role for
Kruppel-associated box-zinc finger proteins in heterochromatin-
mediated gene silencing.";
Mol. Cell. Biol. 19:4366-4378(1999).
[10]
INTERACTION WITH ZFP53 AND ZFP68, AND FUNCTION.
PubMed=10347202; DOI=10.1074/jbc.274.23.16412;
Agata Y., Matsuda E., Shimizu A.;
"Two novel Kruppel-associated box-containing zinc-finger proteins,
KRAZ1 and KRAZ2, repress transcription through functional interaction
with the corepressor KAP-1 (TIF1beta/KRIP-1).";
J. Biol. Chem. 274:16412-16422(1999).
[11]
INTERACTION WITH NCOR1.
PubMed=11013263; DOI=10.1074/jbc.M007864200;
Underhill C., Qutob M.S., Yee S.P., Torchia J.;
"A novel nuclear receptor corepressor complex, N-CoR, contains
components of the mammalian SWI/SNF complex and the corepressor KAP-
1.";
J. Biol. Chem. 275:40463-40470(2000).
[12]
INTERACTION WITH CHD3.
PubMed=11230151; DOI=10.1101/gad.869501;
Schultz D.C., Friedman J.R., Rauscher F.J. III;
"Targeting histone deacetylase complexes via KRAB-zinc finger
proteins: the PHD and bromodomains of KAP-1 form a cooperative unit
that recruits a novel isoform of the Mi-2alpha subunit of NuRD.";
Genes Dev. 15:428-443(2001).
[13]
INTERACTION WITH SETDB1, AND FUNCTION.
PubMed=11959841; DOI=10.1101/gad.973302;
Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III;
"SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific
methyltransferase that contributes to HP1-mediated silencing of
euchromatic genes by KRAB zinc-finger proteins.";
Genes Dev. 16:919-932(2002).
[14]
INTERACTION WITH CBX5, AND FUNCTION.
PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
"The mammalian heterochromatin protein 1 binds diverse nuclear
proteins through a common motif that targets the chromoshadow
domain.";
Biochem. Biophys. Res. Commun. 331:929-937(2005).
[15]
INTERACTION WITH MDM2, AND FUNCTION.
PubMed=16107876; DOI=10.1038/sj.emboj.7600791;
Wang C., Ivanov A., Chen L., Fredericks W.J., Seto E.,
Rauscher F.J. III, Chen J.;
"MDM2 interaction with nuclear corepressor KAP1 contributes to p53
inactivation.";
EMBO J. 24:3279-3290(2005).
[16]
INTERACTION WITH MDM2 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX.
PubMed=17056014; DOI=10.1016/j.bbrc.2006.10.022;
Okamoto K., Kitabayashi I., Taya Y.;
"KAP1 dictates p53 response induced by chemotherapeutic agents via
Mdm2 interaction.";
Biochem. Biophys. Res. Commun. 351:216-222(2006).
[17]
INTERACTION WITH FES/FPS, AND PHOSPHORYLATION.
PubMed=16792528; DOI=10.1042/BJ20060194;
Delfino F.J., Shaffer J.M., Smithgall T.E.;
"The KRAB-associated co-repressor KAP-1 is a coiled-coil binding
partner, substrate and activator of the c-Fes protein tyrosine
kinase.";
Biochem. J. 399:141-150(2006).
[18]
PHOSPHORYLATION AT SER-824, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17178852; DOI=10.1158/0008-5472.CAN-06-4138;
White D.E., Negorev D., Peng H., Ivanov A.V., Maul G.G.,
Rauscher F.J. III;
"KAP1, a novel substrate for PIKK family members, colocalizes with
numerous damage response factors at DNA lesions.";
Cancer Res. 66:11594-11599(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; THR-541 AND
SER-757, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[21]
PHOSPHORYLATION AT SER-824, AND FUNCTION.
PubMed=16862143; DOI=10.1038/ncb1446;
Ziv Y., Bielopolski D., Galanty Y., Lukas C., Taya Y., Schultz D.C.,
Lukas J., Bekker-Jensen S., Bartek J., Shiloh Y.;
"Chromatin relaxation in response to DNA double-strand breaks is
modulated by a novel ATM- and KAP-1 dependent pathway.";
Nat. Cell Biol. 8:870-876(2006).
[22]
INTERACTION WITH MAGEC2.
PubMed=17942928; DOI=10.1158/0008-5472.CAN-07-1478;
Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M.,
Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H.,
Ivanov A.V., Simpson A.J., Longley B.J.;
"MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and
suppress p53-dependent apoptosis in MAGE-positive cell lines.";
Cancer Res. 67:9954-9962(2007).
[23]
INTERACTION WITH ZNF350, SUMOYLATION AT LYS-554; LYS-779 AND LYS-804,
FUNCTION, AND MUTAGENESIS OF LYS-554; LYS-575; LYS-676; LYS-779 AND
LYS-804.
PubMed=17079232; DOI=10.1074/jbc.M606306200;
Lee Y.K., Thomas S.N., Yang A.J., Ann D.K.;
"Doxorubicin down-regulates Kruppel-associated box domain-associated
protein 1 sumoylation that relieves its transcription repression on
p21WAF1/CIP1 in breast cancer MCF-7 cells.";
J. Biol. Chem. 282:1595-1606(2007).
[24]
INTERACTION WITH E2F1, AND FUNCTION.
PubMed=17704056; DOI=10.1074/jbc.M704757200;
Wang C., Rauscher F.J. III, Cress W.D., Chen J.;
"Regulation of E2F1 function by the nuclear corepressor KAP1.";
J. Biol. Chem. 282:29902-29909(2007).
[25]
PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, AND MUTAGENESIS OF
LEU-306; LYS-554; LYS-779; LYS-804 AND SER-824.
PubMed=17942393; DOI=10.1074/jbc.M706912200;
Li X., Lee Y.K., Jeng J.C., Yen Y., Schultz D.C., Shih H.M., Ann D.K.;
"Role for KAP1 serine 824 phosphorylation and
sumoylation/desumoylation switch in regulating KAP1-mediated
transcriptional repression.";
J. Biol. Chem. 282:36177-36189(2007).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[27]
SUMOYLATION AT LYS-750, FUNCTION, DOMAIN PHD-TYPE, INTERACTION WITH
CHD3 AND SETDB1, AND MUTAGENESIS OF LYS-554; LYS-575; CYS-651;
LYS-676; LYS-750; LYS-779 AND LYS-804.
PubMed=18082607; DOI=10.1016/j.molcel.2007.11.012;
Ivanov A.V., Peng H., Yurchenko V., Yap K.L., Negorev D.G.,
Schultz D.C., Psulkowski E., Fredericks W.J., White D.E., Maul G.G.,
Sadofsky M.J., Zhou M.M., Rauscher F.J. III;
"PHD domain-mediated E3 ligase activity directs intramolecular
sumoylation of an adjacent bromodomain required for gene silencing.";
Mol. Cell 28:823-837(2007).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[29]
INTERACTION WITH ZNF256, AND FUNCTION.
PubMed=18060868; DOI=10.1016/j.bbrc.2007.11.118;
Suzuki C., Murakumo Y., Kawase Y., Sato T., Morinaga T., Fukuda N.,
Enomoto A., Ichihara M., Takahashi M.;
"A novel GDNF-inducible gene, BMZF3, encodes a transcriptional
repressor associated with KAP-1.";
Biochem. Biophys. Res. Commun. 366:226-232(2008).
[30]
INTERACTION WITH SMARCAD1.
PubMed=18675275; DOI=10.1016/j.jmb.2008.07.031;
Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T.,
Ohara O., Koga H.;
"The novel protein complex with SMARCAD1/KIAA1122 binds to the
vicinity of TSS.";
J. Mol. Biol. 382:257-265(2008).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-439; SER-471;
SER-473; SER-489; SER-752 AND SER-757, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
INTERACTION WITH RRP1B.
PubMed=19710015; DOI=10.1074/jbc.M109.023457;
Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
"The metastasis efficiency modifier ribosomal RNA processing 1 homolog
B (RRP1B) is a chromatin-associated factor.";
J. Biol. Chem. 284:28660-28673(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-501 AND
SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304; LYS-340; LYS-377;
LYS-770 AND LYS-774, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[38]
SUMOYLATION AT LYS-779.
TISSUE=Cervix carcinoma;
PubMed=20388717; DOI=10.1074/jbc.M110.106955;
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
Eriksson J.E., Sistonen L.;
"In vivo identification of sumoylation sites by a signature tag and
cysteine-targeted affinity purification.";
J. Biol. Chem. 285:19324-19329(2010).
[39]
INTERACTION WITH ERBB4 AND MDM2 IN THE TRIM28/KAP1-ERBB4-MDM2 COMPLEX
AND WITH MDM2 AND P53/TP53 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX,
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20858735; DOI=10.1158/1541-7786.MCR-10-0042;
Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
"Interactions of ErbB4 and Kap1 connect the growth factor and DNA
damage response pathways.";
Mol. Cancer Res. 8:1388-1398(2010).
[40]
FUNCTION, UBIQUITINATION, AND INTERACTION WITH MAGEC2.
PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
"MAGE-RING protein complexes comprise a family of E3 ubiquitin
ligases.";
Mol. Cell 39:963-974(2010).
[41]
INTERACTION WITH CBX5 AND POGZ, AND MUTAGENESIS OF VAL-488 AND
LEU-490.
PubMed=20562864; DOI=10.1038/ncb2075;
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
Kimura H., Obuse C.;
"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome
arms through Aurora B activation.";
Nat. Cell Biol. 12:719-727(2010).
[42]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-19; SER-473; SER-489; THR-541; SER-697; SER-752
AND SER-757, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS],
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[43]
PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, INTERACTION WITH
PPP1CA AND PPP1CB, AND MUTAGENESIS OF PHE-370; SER-440; SER-501 AND
SER-824.
PubMed=20424263; DOI=10.1126/scisignal.2000781;
Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.;
"SUMOylation of the transcriptional co-repressor KAP1 is regulated by
the serine and threonine phosphatase PP1.";
Sci. Signal. 3:RA32-RA32(2010).
[44]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[45]
FUNCTION AS SUMO LIGASE, AND INTERACTION WITH IRF7.
PubMed=21940674; DOI=10.4049/jimmunol.1101704;
Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H.,
Rauscher F.J. III, Ozato K., Zhu F.;
"Tripartite motif-containing protein 28 is a small ubiquitin-related
modifier E3 ligase and negative regulator of IFN regulatory factor
7.";
J. Immunol. 187:4754-4763(2011).
[46]
INTERACTION WITH SMARCAD1.
PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
Varga-Weisz P., Mermoud J.E.;
"Maintenance of silent chromatin through replication requires SWI/SNF-
like chromatin remodeler SMARCAD1.";
Mol. Cell 42:285-296(2011).
[47]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-19; SER-473; SER-479 AND SER-683, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[48]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[50]
FUNCTION, INTERACTION WITH ZNF268; KOX1 AND ZNF300, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF CYS-65 AND CYS-68.
PubMed=23665872; DOI=10.1007/s00018-013-1359-4;
Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M.,
Huang Z.;
"Novel activity of KRAB domain that functions to reinforce nuclear
localization of KRAB-containing zinc finger proteins by interacting
with KAP1.";
Cell. Mol. Life Sci. 70:3947-3958(2013).
[51]
FUNCTION, AND INTERACTION WITH ZFP90.
PubMed=23543754; DOI=10.4049/jimmunol.1203561;
Huang C., Martin S., Pfleger C., Du J., Buckner J.H., Bluestone J.A.,
Riley J.L., Ziegler S.F.;
"Cutting Edge: a novel, human-specific interacting protein couples
FOXP3 to a chromatin-remodeling complex that contains KAP1/TRIM28.";
J. Immunol. 190:4470-4473(2013).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-26; SER-138;
SER-417; SER-453; SER-473; SER-479; SER-489; THR-498; SER-501;
THR-541; SER-752; SER-757 AND SER-784, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[53]
INTERACTION WITH SETX.
PubMed=23149945; DOI=10.1128/MCB.01195-12;
Yuce O., West S.C.;
"Senataxin, defective in the neurodegenerative disorder ataxia with
oculomotor apraxia 2, lies at the interface of transcription and the
DNA damage response.";
Mol. Cell. Biol. 33:406-417(2013).
[54]
FUNCTION, POSSIBLE IDENTIFICATION IN A COREPRESSOR COMPLEX, AND
CHROMATIN-BINDING.
PubMed=24623306; DOI=10.7554/eLife.02313;
Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
"A KRAS-directed transcriptional silencing pathway that mediates the
CpG island methylator phenotype.";
Elife 3:E02313-E02313(2014).
[55]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-501; THR-541;
SER-594; SER-683 AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[56]
INTERACTION WITH ZBTB1.
PubMed=24657165; DOI=10.1016/j.molcel.2014.02.017;
Kim H., Dejsuphong D., Adelmant G., Ceccaldi R., Yang K., Marto J.A.,
D'Andrea A.D.;
"Transcriptional repressor ZBTB1 promotes chromatin remodeling and
translesion DNA synthesis.";
Mol. Cell 54:107-118(2014).
[57]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-199; LYS-254;
LYS-261; LYS-319; LYS-366; LYS-377; LYS-434; LYS-469; LYS-575;
LYS-750; LYS-770; LYS-774 AND LYS-779, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[58]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-377; LYS-469; LYS-750 AND
LYS-779, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[59]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-377; LYS-469;
LYS-750; LYS-779 AND LYS-804, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[60]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-377; LYS-750 AND LYS-779,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[61]
FUNCTION, INTERACTION WITH ATRX, AND FORMATION OF A COMPLEX WITH ATRX;
SETDB1 AND ZNF274.
PubMed=27029610; DOI=10.1080/15592294.2016.1169351;
Valle-Garcia D., Qadeer Z.A., McHugh D.S., Ghiraldini F.G.,
Chowdhury A.H., Hasson D., Dyer M.A., Recillas-Targa F., Bernstein E.;
"ATRX binds to atypical chromatin domains at the 3' exons of zinc
finger genes to preserve H3K9me3 enrichment.";
Epigenetics 11:398-414(2016).
[62]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-127; LYS-199;
LYS-254; LYS-261; LYS-272; LYS-304; LYS-319; LYS-377; LYS-407;
LYS-434; LYS-469; LYS-507; LYS-554; LYS-750; LYS-770; LYS-774; LYS-779
AND LYS-804, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[63]
STRUCTURE BY NMR OF 619-688 IN COMPLEX WITH ZINC IONS.
PubMed=11226167; DOI=10.1093/emboj/20.1.165;
Capili A.D., Schultz D.C., Rauscher F.J. III, Borden K.L.;
"Solution structure of the PHD domain from the KAP-1 corepressor:
structural determinants for PHD, RING and LIM zinc-binding domains.";
EMBO J. 20:165-177(2001).
[64]
STRUCTURE BY NMR OF 624-812 OF WILD TYPE AND IN COMPLEX WITH UBE2I,
SUMOYLATION AT LYS-676; LYS-750; LYS-779 AND LYS-804, AND MUTAGENESIS
OF CYS-651; LEU-653; LEU-668 AND LEU-709.
PubMed=18488044; DOI=10.1038/nsmb.1416;
Zeng L., Yap K.L., Ivanov A.V., Wang X., Mujtaba S., Plotnikova O.,
Rauscher F.J. III, Zhou M.M.;
"Structural insights into human KAP1 PHD finger-bromodomain and its
role in gene silencing.";
Nat. Struct. Mol. Biol. 15:626-633(2008).
[65]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 201-250.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of ms1043.";
Submitted (FEB-2009) to the PDB data bank.
[66]
VARIANT [LARGE SCALE ANALYSIS] MET-794.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Nuclear corepressor for KRAB domain-containing zinc
finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting
CHD3, a subunit of the nucleosome remodeling and deacetylation
(NuRD) complex, and SETDB1 (which specifically methylates histone
H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target
genes. Enhances transcriptional repression by coordinating the
increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14'
acetylation (H3K9ac and H3K14ac, respectively) and the disposition
of HP1 proteins to silence gene expression. Recruitment of SETDB1
induces heterochromatinization. May play a role as a coactivator
for CEBPB and NR3C1 in the transcriptional activation of ORM1.
Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating
E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May
serve as a partial backup to prevent E2F1-mediated apoptosis in
the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has
E3 SUMO-protein ligase activity toward itself via its PHD-type
zinc finger. Also specifically sumoylates IRF7, thereby inhibiting
its transactivation activity. Ubiquitinates p53/TP53 leading to
its proteosomal degradation; the function is enhanced by MAGEC2
and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear
localization of KOX1, ZNF268 and ZNF300 transcription factors. In
association with isoform 2 of ZFP90, is required for the
transcriptional repressor activity of FOXP3 and the suppressive
function of regulatory T-cells (Treg) (PubMed:23543754). Probably
forms a corepressor complex required for activated KRAS-mediated
promoter hypermethylation and transcriptional silencing of tumor
suppressor genes (TSGs) or other tumor-related genes in colorectal
cancer (CRC) cells (PubMed:24623306). Also required to maintain a
transcriptionally repressive state of genes in undifferentiated
embryonic stem cells (ESCs) (PubMed:24623306). Associates at
promoter regions of tumor suppressor genes (TSGs) leading to their
gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex
may play a role in recruiting ATRX to the 3'-exons of zinc-finger
coding genes with atypical chromatin signatures to establish or
maintain/protect H3K9me3 at these transcriptionally active regions
(PubMed:27029610). Acts as a corepressor for ZFP568 (By
similarity). {ECO:0000250|UniProtKB:Q62318,
ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11959841,
ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:16107876,
ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17704056,
ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18060868,
ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:20424263,
ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041,
ECO:0000269|PubMed:21940674, ECO:0000269|PubMed:23543754,
ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:24623306,
ECO:0000269|PubMed:27029610, ECO:0000269|PubMed:8769649,
ECO:0000269|PubMed:9016654}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with SETX (PubMed:23149945). Oligomer; the RBCC
domain homotrimerizes and interacts with one molecule of KRAB to
form the KRAB-KAP1 corepressor complex. Binding to a KRAB domain
is an absolute requirement for silencing gene expression.
Interacts with CEBPB and NR3C1. Interacts with a number of KRAB-
ZFP proteins including ZNF10, ZFP53, ZFP68, ZNF382 and ZNF256.
Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via
the RING-type and PHD-type zinc fingers). Component of a ternary
complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5),
a KRAB domain-containing protein, and DNA. Interacts with CBX5
(via the PxVxL motif); the interaction occurs in interphase nuclei
and competes for binding POGZ. Interacts with POGZ; the
interaction competes for interaction with CBX5. Interacts with
SETDB1; the interaction is enhanced by KAP1 sumoylation,
stimulates SETB1 histone methyltransferase activity and gene
silencing. Interacts (via the PHD-type zinc finger) with UBE2I;
the interaction is required for sumoylation and repressor
activity. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved
in connecting growth factor and DNA damage responses. Interacts
directly with ERBB4; the interaction represses ERBB4-mediated
transcription activity. Interacts with MDM2; the interaction
contributes to p53/TP53 inactivation. Component of the
TRIM28/KAP1-MDM2-p53/TP53; involved in regulating p53/TP53
stabilization and activity. Interacts (via the leucine zipper
alpha helical coiled-coil) with E2F1 (central region); the
interaction inhibits E2F1 acetylation and transcriptional
activity. Interacts with PPP1CA; the interaction dephosphorylates
TRIM28 at Ser-824 and forms a complex at the p21 promoter site.
Interacts with PPP1CB; the interaction is weak but is increased on
dephosphorylation at Ser-824. Interacts with FES/FPS. Interacts
with SMARCAD1. Interacts with, and sumoylates IRF7. Interacts with
MAGEC2. Part of a complex composed of TRIM28, HDAC1, HDAC2 and
EHMT2. Interacts with AICDA (By similarity). Interacts (via the
RBCC domain) with KOX1 (via the KRAB domain), ZNF268 (via the KRAB
domain) and ZNF300 (via the KRAB domain); the interactions
increase KOX1, ZNF268 and ZNF300 nuclear localization activities.
The large PER complex involved in the histone methylation is
composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2;
CBX3 mediates the formation of the complex. Interacts with isoform
2 of ZFP90. Forms a complex with FOXP3 in the presence of isoform
2 of ZFP90. Interacts with NR4A3; the interactions potentiates
NR4A3 activity on NurRE promoter (By similarity). Interacts
(unphosphorylated or phosphorylated form) with ZBTB1 (via BTB
domain) (PubMed:24657165). Probably part of a corepressor complex
containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306).
Interacts with ATRX. Forms a complex with ATRX, SETDB1 and ZNF274
(PubMed:27029610). Interacts with ZFP568; the interaction mediates
ZFP568 transcriptional repression activity (By similarity).
Interacts with RRP1B (PubMed:19710015).
{ECO:0000250|UniProtKB:Q62318, ECO:0000269|PubMed:10330177,
ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11013263,
ECO:0000269|PubMed:11226167, ECO:0000269|PubMed:11230151,
ECO:0000269|PubMed:11959841, ECO:0000269|PubMed:15882967,
ECO:0000269|PubMed:16107876, ECO:0000269|PubMed:16792528,
ECO:0000269|PubMed:17056014, ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:17512541, ECO:0000269|PubMed:17704056,
ECO:0000269|PubMed:17942928, ECO:0000269|PubMed:18060868,
ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:18488044,
ECO:0000269|PubMed:18675275, ECO:0000269|PubMed:19710015,
ECO:0000269|PubMed:20424263, ECO:0000269|PubMed:20562864,
ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041,
ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21940674,
ECO:0000269|PubMed:23149945, ECO:0000269|PubMed:23543754,
ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:24623306,
ECO:0000269|PubMed:24657165, ECO:0000269|PubMed:27029610,
ECO:0000269|PubMed:9016654}.
-!- INTERACTION:
P83917:Cbx1 (xeno); NbExp=2; IntAct=EBI-78139, EBI-78119;
Q13185:CBX3; NbExp=4; IntAct=EBI-78139, EBI-78176;
P23198:Cbx3 (xeno); NbExp=2; IntAct=EBI-78139, EBI-78162;
P45973:CBX5; NbExp=10; IntAct=EBI-78139, EBI-78219;
Q12873:CHD3; NbExp=4; IntAct=EBI-78139, EBI-523590;
P43356:MAGEA2B; NbExp=6; IntAct=EBI-78139, EBI-5650739;
P43357:MAGEA3; NbExp=3; IntAct=EBI-78139, EBI-5651459;
P43360:MAGEA6; NbExp=2; IntAct=EBI-78139, EBI-1045155;
Q9UBF1:MAGEC2; NbExp=14; IntAct=EBI-78139, EBI-5651487;
Q9HCI5:MAGEE1; NbExp=2; IntAct=EBI-78139, EBI-949966;
O75376:NCOR1; NbExp=4; IntAct=EBI-78139, EBI-347233;
Q9BQF6:SENP7; NbExp=3; IntAct=EBI-78139, EBI-766251;
Q8TF47-3:ZFP90; NbExp=2; IntAct=EBI-78139, EBI-11419904;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330177,
ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:20858735,
ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:9016654}.
Note=Associated with centromeric heterochromatin during cell
differentiation through CBX1. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13263-1; Sequence=Displayed;
Name=2;
IsoId=Q13263-2; Sequence=VSP_010898;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested including
spleen, thymus, prostate, testis, ovary, small intestine, colon
and peripheral blood leukocytes. {ECO:0000269|PubMed:9016654}.
-!- DOMAIN: The HP1 box is both necessary and sufficient for HP1
binding. {ECO:0000269|PubMed:18082607}.
-!- DOMAIN: The PHD-type zinc finger enhances CEBPB transcriptional
activity. The PHD-type zinc finger, the HP1 box and the bromo
domain, function together to assemble the machinery required for
repression of KRAB domain-containing proteins. Acts as an
intramolecular SUMO E3 ligase for autosumoylation of bromodomain.
{ECO:0000269|PubMed:18082607}.
-!- DOMAIN: The RING-finger-B Box-coiled-coil/tripartite motif
(RBCC/TRIM motif) is required for interaction with the KRAB domain
of KRAB-zinc finger proteins. Binds four zinc ions per molecule.
The RING finger and the N-terminal of the leucine zipper alpha
helical coiled-coil region of RBCC are required for
oligomerization. {ECO:0000269|PubMed:18082607}.
-!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
required for interaction with chromoshadow domains. This motif
requires additional residues -7, -6, +4 and +5 of the central Val
which contact the chromoshadow domain.
{ECO:0000269|PubMed:18082607}.
-!- PTM: ATM-induced phosphorylation on Ser-824 represses sumoylation
leading to the de-repression of expression of a subset of genes
involved in cell cycle control and apoptosis in response to
genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA
and PP1CB forms, allows sumoylation and expression of TRIM28
target genes. {ECO:0000269|PubMed:16862143,
ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:20424263}.
-!- PTM: Sumoylation/desumoylation events regulate TRIM28-mediated
transcriptional repression. Sumoylation is required for
interaction with CHD3 and SETDB1 and the corepressor activity.
Represses and is repressed by Ser-824 phosphorylation. Enhances
the TRIM28 corepressor activity, inhibiting transcriptional
activity of a number of genes including GADD45A and CDKN1A/p21.
Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.
In response to Dox-induced DNA damage, enhanced phosphorylation on
Ser-824 prevents sumoylation and allows de-repression of
CDKN1A/p21. {ECO:0000269|PubMed:16862143,
ECO:0000269|PubMed:17079232, ECO:0000269|PubMed:17178852,
ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18488044,
ECO:0000269|PubMed:20388717, ECO:0000269|PubMed:20424263}.
-!- PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
{ECO:0000269|PubMed:20864041}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U78773; AAB37341.1; -; mRNA.
EMBL; X97548; CAA66150.1; -; mRNA.
EMBL; U95040; AAB51517.1; -; mRNA.
EMBL; BC004978; AAH04978.1; -; mRNA.
EMBL; BC007390; AAH07390.2; -; mRNA.
EMBL; BC052986; AAH52986.1; -; mRNA.
EMBL; U31657; AAA74954.1; -; mRNA.
CCDS; CCDS12985.1; -. [Q13263-1]
PIR; G01950; G01950.
RefSeq; NP_005753.1; NM_005762.2. [Q13263-1]
UniGene; Hs.467408; -.
PDB; 1FP0; NMR; -; A=619-679.
PDB; 2RO1; NMR; -; A=624-812.
PDB; 2YVR; X-ray; 1.80 A; A/B=201-250.
PDBsum; 1FP0; -.
PDBsum; 2RO1; -.
PDBsum; 2YVR; -.
ProteinModelPortal; Q13263; -.
SMR; Q13263; -.
BioGrid; 115457; 312.
CORUM; Q13263; -.
DIP; DIP-30891N; -.
ELM; Q13263; -.
IntAct; Q13263; 87.
MINT; MINT-5001244; -.
STRING; 9606.ENSP00000253024; -.
ChEMBL; CHEMBL3769297; -.
iPTMnet; Q13263; -.
PhosphoSitePlus; Q13263; -.
SwissPalm; Q13263; -.
BioMuta; TRIM28; -.
DMDM; 3183179; -.
EPD; Q13263; -.
MaxQB; Q13263; -.
PaxDb; Q13263; -.
PeptideAtlas; Q13263; -.
PRIDE; Q13263; -.
DNASU; 10155; -.
Ensembl; ENST00000253024; ENSP00000253024; ENSG00000130726. [Q13263-1]
Ensembl; ENST00000341753; ENSP00000342232; ENSG00000130726. [Q13263-2]
GeneID; 10155; -.
KEGG; hsa:10155; -.
UCSC; uc002qtg.2; human. [Q13263-1]
CTD; 10155; -.
DisGeNET; 10155; -.
EuPathDB; HostDB:ENSG00000130726.11; -.
GeneCards; TRIM28; -.
HGNC; HGNC:16384; TRIM28.
HPA; CAB010066; -.
HPA; HPA064033; -.
MIM; 601742; gene.
neXtProt; NX_Q13263; -.
OpenTargets; ENSG00000130726; -.
PharmGKB; PA38131; -.
eggNOG; ENOG410ITES; Eukaryota.
eggNOG; ENOG41102KI; LUCA.
GeneTree; ENSGT00890000139374; -.
HOGENOM; HOG000137674; -.
HOVERGEN; HBG055353; -.
InParanoid; Q13263; -.
KO; K08882; -.
OMA; NQRKCER; -.
OrthoDB; EOG091G01KK; -.
PhylomeDB; Q13263; -.
TreeFam; TF106455; -.
Reactome; R-HSA-212436; Generic Transcription Pathway.
SignaLink; Q13263; -.
SIGNOR; Q13263; -.
UniPathway; UPA00886; -.
ChiTaRS; TRIM28; human.
EvolutionaryTrace; Q13263; -.
GeneWiki; TRIM28; -.
GenomeRNAi; 10155; -.
PMAP-CutDB; Q13263; -.
PRO; PR:Q13263; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130726; -.
CleanEx; HS_TRIM28; -.
ExpressionAtlas; Q13263; baseline and differential.
Genevisible; Q13263; HS.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005720; C:nuclear heterochromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0035851; F:Krueppel-associated box domain binding; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0043045; P:DNA methylation involved in embryo development; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0060669; P:embryonic placenta morphogenesis; IEA:Ensembl.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:1901536; P:negative regulation of DNA demethylation; IEA:Ensembl.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
GO; GO:2000653; P:regulation of genetic imprinting; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
CDD; cd00021; BBOX; 2.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR003649; Bbox_C.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00628; PHD; 1.
Pfam; PF00643; zf-B_box; 2.
Pfam; PF14634; zf-RING_5; 1.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 2.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Citrullination; Coiled coil; Complete proteome;
Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
CHAIN 2 835 Transcription intermediary factor 1-beta.
/FTId=PRO_0000056392.
DOMAIN 697 801 Bromo.
ZN_FING 65 121 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 148 195 B box-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
ZN_FING 204 245 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 625 672 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 65 376 RBCC domain.
REGION 246 376 Leucine zipper alpha helical coiled-coil
region.
REGION 247 376 Interaction with MAGEC2.
REGION 366 370 Involved in binding PPP1CA.
REGION 476 513 HP1 box.
MOTIF 481 494 PxVxL motif.
COMPBIAS 2 58 Ala-rich.
COMPBIAS 526 530 Poly-Ala.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 266 266 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 304 304 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 340 340 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 377 377 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 470 470 Citrulline. {ECO:0000250}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 472 472 Citrulline. {ECO:0000250}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 498 498 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 541 541 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 689 689 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 755 755 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 770 770 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 774 774 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 779 779 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 824 824 Phosphoserine; by ATM and ATR and dsDNA
kinase. {ECO:0000269|PubMed:16862143,
ECO:0000269|PubMed:17178852,
ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:20424263}.
CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 127 127 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 199 199 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 272 272 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 319 319 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 377 377 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 377 377 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 407 407 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 434 434 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 507 507 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 554 554 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:17079232}.
CROSSLNK 554 554 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 575 575 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:18488044}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:18082607}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 770 770 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 774 774 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 804 804 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:17079232}.
CROSSLNK 804 804 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 114 195 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010898.
VARIANT 794 794 T -> M (in dbSNP:rs56229738).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042386.
MUTAGEN 65 65 C->A: Reduces nuclear localization
activity of ZNF268; when associated with
A-68. {ECO:0000269|PubMed:23665872}.
MUTAGEN 68 68 C->A: Reduces nuclear localization
activity of ZNF268; when associated with
A-65. {ECO:0000269|PubMed:23665872}.
MUTAGEN 306 306 L->P: Disrupts the interaction with
ZNF350 and amost completely relieves the
transcription repressive effect of
sumoylated TRIM28.
{ECO:0000269|PubMed:17942393}.
MUTAGEN 366 366 K->G: Greatly reduced interaction with
PPP1CA.
MUTAGEN 368 368 I->G: Increased interaction with PPP1CA.
Greatly decreased phosphorylation on S-
824.
MUTAGEN 370 370 F->A: Some reduction in interaction with
PPP1CA. {ECO:0000269|PubMed:20424263}.
MUTAGEN 370 370 F->G: Some reduction in interaction with
PPP1CA. {ECO:0000269|PubMed:20424263}.
MUTAGEN 440 440 S->A: No effect on interaction with
PPP1CA nor on sumoylation levels.
Decreased sumoylation levels; when
associated with D-501 and D-824.
{ECO:0000269|PubMed:20424263}.
MUTAGEN 488 488 V->E: Abolishes interaction with CBX5;
when associated with E-490.
{ECO:0000269|PubMed:20562864}.
MUTAGEN 490 490 L->E: Abolishes interaction with CBX5;
when associated with E-488.
{ECO:0000269|PubMed:20562864}.
MUTAGEN 501 501 S->A: No effect on interaction with
PPP1CA nor on sumoylation levels.
Decreased sumoylation levels; when
associated with D-440 and D-824.
{ECO:0000269|PubMed:20424263}.
MUTAGEN 554 554 K->R: Moderately reduces sumoylation and
repression. Abolishes both sumoylation
and repression; when associated with R-
575. Relieves the repressor activity on
Dox-induced GADD45A transcription and 2-
fold increase in phosphorylation at Ser-
824; when associated with R-779 and R-
804. {ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:18082607}.
MUTAGEN 575 575 K->R: Modestly reduced sumoylation and
repression. Abolishes both sumoylation
and repression; when associated with R-
554. {ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:18082607}.
MUTAGEN 651 651 C->A: Complete loss of the PHD finger-
mediated stimulatory effect on
sumoylation. Loss of binding UBE2I.
{ECO:0000269|PubMed:18082607,
ECO:0000269|PubMed:18488044}.
MUTAGEN 653 653 L->A: Greatly reduced sumoylation. Little
further effect on sumoylation; when
associated with A-668 and/or A-709.
{ECO:0000269|PubMed:18488044}.
MUTAGEN 668 668 L->A: Little effect on sumoylation.
Little further effect on sumoylation;
when associated with A-653 and/or A-709.
{ECO:0000269|PubMed:18488044}.
MUTAGEN 676 676 K->R: Modestly reduces sumoylation and
repression. {ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:18082607}.
MUTAGEN 709 709 L->A: Greatly reduced sumoylation. Little
further effect on sumoylation; when
associated with A-653 and/or A-668.
{ECO:0000269|PubMed:18488044}.
MUTAGEN 750 750 K->R: Some reduced sumoylation and
repression.
{ECO:0000269|PubMed:18082607}.
MUTAGEN 779 779 K->R: Abolishes both sumoylation and
repression; when associated with R-804.
Relieves the repressor activity on Dox-
induced GADD45A transcription and 2-fold
increase in phosphorylation at Ser-824;
when associated with R-554 and R-804.
{ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:18082607}.
MUTAGEN 804 804 K->R: Abolishes both sumoylation and
repression; when associated with R-779.
Relieves the repressor activity on Dox-
induced GADD45A transcription and 2-fold
increase in phosphorylation at Ser-824;
when associated with R-554 and R-779.
{ECO:0000269|PubMed:17079232,
ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:18082607}.
MUTAGEN 824 824 S->A: Suppresses Dox-induced CDKN1A/p21
promoter activation. No effect on
sumoylation levels. Decreased sumoylation
levels; when associated with D-440 and D-
501. {ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:20424263}.
MUTAGEN 824 824 S->D: Enhances Dox-induced CDKN1A/p21
promoter activation. Decreased
sumoylation with or without Dox-
treatment. {ECO:0000269|PubMed:17942393,
ECO:0000269|PubMed:20424263}.
CONFLICT 162 162 A -> G (in Ref. 1; AAB37341).
{ECO:0000305}.
STRAND 210 212 {ECO:0000244|PDB:2YVR}.
STRAND 219 221 {ECO:0000244|PDB:2YVR}.
TURN 222 225 {ECO:0000244|PDB:2YVR}.
STRAND 226 228 {ECO:0000244|PDB:2YVR}.
HELIX 230 234 {ECO:0000244|PDB:2YVR}.
TURN 235 239 {ECO:0000244|PDB:2YVR}.
STRAND 242 244 {ECO:0000244|PDB:2YVR}.
STRAND 620 626 {ECO:0000244|PDB:1FP0}.
STRAND 629 631 {ECO:0000244|PDB:1FP0}.
STRAND 633 635 {ECO:0000244|PDB:1FP0}.
TURN 641 643 {ECO:0000244|PDB:2RO1}.
STRAND 651 653 {ECO:0000244|PDB:1FP0}.
STRAND 661 663 {ECO:0000244|PDB:1FP0}.
TURN 666 669 {ECO:0000244|PDB:2RO1}.
STRAND 684 690 {ECO:0000244|PDB:2RO1}.
HELIX 698 713 {ECO:0000244|PDB:2RO1}.
HELIX 717 721 {ECO:0000244|PDB:2RO1}.
STRAND 730 732 {ECO:0000244|PDB:2RO1}.
HELIX 740 748 {ECO:0000244|PDB:2RO1}.
STRAND 750 753 {ECO:0000244|PDB:2RO1}.
HELIX 758 775 {ECO:0000244|PDB:2RO1}.
HELIX 783 799 {ECO:0000244|PDB:2RO1}.
TURN 800 802 {ECO:0000244|PDB:2RO1}.
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


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