TIF1B_MOUSE
ID TIF1B_MOUSE Reviewed; 834 AA.
AC Q62318; P70391; Q8C283; Q99PN4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 228.
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-A-interacting protein;
DE AltName: Full=KRIP-1;
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|MGI:MGI:109274}; Synonyms=Kap1, Krip1, Tif1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8978696;
RA le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA Losson R., Chambon P.;
RT "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT control of transcription by nuclear receptors.";
RL EMBO J. 15:6701-6715(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=8986806; DOI=10.1073/pnas.93.26.15299;
RA Kim S.-S., Chen Y.-M., O'Leary E., Witzgall R., Vidal M., Bonventre J.V.;
RT "A novel member of the RING finger family, KRIP-1, associates with the
RT KRAB-A transcriptional repressor domain of zinc finger proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15299-15304(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10940561; DOI=10.1016/s0378-1119(00)00263-8;
RA Cammas F., Garnier J.-M., Chambon P., Losson R.;
RT "Correlation of the exon/intron organization to the conserved domains of
RT the mouse transcriptional corepressor TIF1beta.";
RL Gene 253:231-235(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-834 (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP INTERACTION WITH CEBPB AND NR3C1, AND FUNCTION.
RX PubMed=9742105; DOI=10.1128/mcb.18.10.5880;
RA Chang C.J., Chen Y.L., Lee S.C.;
RT "Coactivator TIF1beta interacts with transcription factor C/EBPbeta and
RT glucocorticoid receptor to induce alpha1-acid glycoprotein gene
RT expression.";
RL Mol. Cell. Biol. 18:5880-5887(1998).
RN [8]
RP INTERACTION WITH CBX1; CBX3 AND CBX5.
RX PubMed=10562550; DOI=10.1093/emboj/18.22.6385;
RA Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R.,
RA Gansmuller A., Chambon P., Losson R.;
RT "Interaction with members of the heterochromatin protein 1 (HP1) family and
RT histone deacetylation are differentially involved in transcriptional
RT silencing by members of the TIF1 family.";
RL EMBO J. 18:6385-6395(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
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 ZNF382, AND SUBCELLULAR LOCATION.
RX PubMed=11154279; DOI=10.1128/mcb.21.3.928-939.2001;
RA Gebelein B., Urrutia R.;
RT "Sequence-specific transcriptional repression by KS1, a multiple-zinc-
RT finger-Kruppel-associated box protein.";
RL Mol. Cell. Biol. 21:928-939(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12154074; DOI=10.1242/jcs.115.17.3439;
RA Cammas F., Oulad-Abdelghani M., Vonesch J.-L., Huss-Garcia Y., Chambon P.,
RA Losson R.;
RT "Cell differentiation induces TIF1beta association with centromeric
RT heterochromatin via an HP1 interaction.";
RL J. Cell Sci. 115:3439-3448(2002).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-473, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [16]
RP INTERACTION WITH NR4A3.
RX PubMed=19321449; DOI=10.1074/jbc.m809023200;
RA Rambaud J., Desroches J., Balsalobre A., Drouin J.;
RT "TIF1beta/KAP-1 is a coactivator of the orphan nuclear receptor NGFI-
RT B/Nur77.";
RL J. Biol. Chem. 284:14147-14156(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-23; SER-473 AND SER-501, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-473; SER-489;
RP SER-594; SER-752 AND TYR-755, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP FUNCTION.
RX PubMed=20164836; DOI=10.1038/nature08858;
RA Matsui T., Leung D., Miyashita H., Maksakova I.A., Miyachi H., Kimura H.,
RA Tachibana M., Lorincz M.C., Shinkai Y.;
RT "Proviral silencing in embryonic stem cells requires the histone
RT methyltransferase ESET.";
RL Nature 464:927-931(2010).
RN [20]
RP FUNCTION, INTERACTION WITH ZFP568, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 713-CYS-HIS-714.
RX PubMed=22110054; DOI=10.1242/dev.072546;
RA Shibata M., Blauvelt K.E., Liem K.F. Jr., Garcia-Garcia M.J.;
RT "TRIM28 is required by the mouse KRAB domain protein ZFP568 to control
RT convergent extension and morphogenesis of extra-embryonic tissues.";
RL Development 138:5333-5343(2011).
RN [21]
RP FUNCTION, AND INTERACTION WITH AICDA.
RX PubMed=21518874; DOI=10.1073/pnas.1104423108;
RA Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S.,
RA Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T., Iemura S.,
RA Honjo T.;
RT "Histone chaperone Spt6 is required for class switch recombination but not
RT somatic hypermutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-779, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [23]
RP IDENTIFICATION IN A LARGE PER COMPLEX.
RX PubMed=24413057; DOI=10.1038/nsmb.2746;
RA Duong H.A., Weitz C.J.;
RT "Temporal orchestration of repressive chromatin modifiers by circadian
RT clock Period complexes.";
RL Nat. Struct. Mol. Biol. 21:126-132(2014).
RN [24]
RP CITRULLINATION AT ARG-470 AND ARG-472.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [25]
RP FUNCTION, ADP-RIBOSYLATION, AND INTERACTION WITH CBX5.
RX PubMed=25247314; DOI=10.1038/ncomms6011;
RA Van Meter M., Kashyap M., Rezazadeh S., Geneva A.J., Morello T.D.,
RA Seluanov A., Gorbunova V.;
RT "SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this
RT repression fails with stress and age.";
RL Nat. Commun. 5:5011-5011(2014).
RN [26]
RP INTERACTION WITH CRY1.
RX PubMed=27123980; DOI=10.1371/journal.pone.0154263;
RA Hirano A., Nakagawa T., Yoshitane H., Oyama M., Kozuka-Hata H.,
RA Lanjakornsiripan D., Fukada Y.;
RT "USP7 and TDP-43: pleiotropic regulation of cryptochrome protein stability
RT paces the oscillation of the mammalian circadian clock.";
RL PLoS ONE 11:E0154263-E0154263(2016).
RN [27]
RP INTERACTION WITH ZNF568, AND FUNCTION.
RX PubMed=27658112; DOI=10.1371/journal.pone.0163555;
RA Murphy K.E., Shylo N.A., Alexander K.A., Churchill A.J., Copperman C.,
RA Garcia-Garcia M.J.;
RT "The Transcriptional Repressive Activity of KRAB Zinc Finger Proteins Does
RT Not Correlate with Their Ability to Recruit TRIM28.";
RL PLoS ONE 11:E0163555-E0163555(2016).
RN [28]
RP INTERACTION WITH CYREN.
RX PubMed=30017584; DOI=10.1016/j.molcel.2018.06.018;
RA Hung P.J., Johnson B., Chen B.R., Byrum A.K., Bredemeyer A.L.,
RA Yewdell W.T., Johnson T.E., Lee B.J., Deivasigamani S., Hindi I.,
RA Amatya P., Gross M.L., Paull T.T., Pisapia D.J., Chaudhuri J.,
RA Petrini J.J.H., Mosammaparast N., Amarasinghe G.K., Zha S., Tyler J.K.,
RA Sleckman B.P.;
RT "MRI is a DNA damage response adaptor during classical non-homologous end
RT joining.";
RL Mol. Cell 71:332-342(2018).
CC -!- FUNCTION: Nuclear corepressor for KRAB domain-containing zinc finger
CC proteins (KRAB-ZFPs) (PubMed:20164836, PubMed:22110054,
CC PubMed:25247314, PubMed:27658112). Mediates gene silencing by
CC recruiting CHD3, a subunit of the nucleosome remodeling and
CC deacetylation (NuRD) complex, and SETDB1 (which specifically methylates
CC histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target
CC genes. Enhances transcriptional repression by coordinating the increase
CC in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation
CC (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins
CC to silence gene expression. Recruitment of SETDB1 induces
CC heterochromatinization. May play a role as a coactivator for CEBPB and
CC NR3C1 in the transcriptional activation of ORM1. Also a corepressor for
CC ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex
CC formation and inhibiting E2F1 acetylation. May serve as a partial
CC backup to prevent E2F1-mediated apoptosis in the absence of RB1.
CC Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase
CC activity toward itself via its PHD-type zinc finger. Specifically
CC sumoylates IRF7, thereby inhibiting its transactivation activity.
CC Ubiquitinates p53/TP53 leading to its proteosomal degradation; the
CC function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and
CC MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300
CC transcription factors. Probably forms a corepressor complex required
CC for activated KRAS-mediated promoter hypermethylation and
CC transcriptional silencing of tumor suppressor genes (TSGs) or other
CC tumor-related genes in colorectal cancer (CRC) cells. Required to
CC maintain a transcriptionally repressive state of genes in
CC undifferentiated embryonic stem cells (ESCs) (PubMed:20164836). In
CC ESCs, in collaboration with SETDB1, is also required for H3K9me3 and
CC silencing of endogenous and introduced retroviruses in a DNA-
CC methylation independent-pathway (PubMed:20164836). Associates at
CC promoter regions of tumor suppressor genes (TSGs) leading to their gene
CC silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in
CC recruiting ATRX to the 3'-exons of zinc-finger coding genes with
CC atypical chromatin signatures to establish or maintain/protect H3K9me3
CC at these transcriptionally active regions (By similarity). Acts as a
CC corepressor for ZFP568 (PubMed:22110054, PubMed:27658112).
CC {ECO:0000250|UniProtKB:Q13263, ECO:0000269|PubMed:20164836,
CC ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22110054,
CC ECO:0000269|PubMed:25247314, ECO:0000269|PubMed:27658112,
CC ECO:0000269|PubMed:9742105}.
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: Oligomer; the RBCC domain homotrimerizes and interacts with
CC one molecule of KRAB to form the KRAB-KAP1 corepressor complex.
CC Interacts with SETX (By similarity). Binding to a KRAB domain is an
CC absolute requirement for silencing gene expression. Interacts with a
CC number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68, ZNF382 and
CC ZNF256. Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via
CC the RING-type and PHD-type zinc fingers). Interacts with CBX5 (via the
CC PxVxL motif); the interaction occurs in interphase nuclei and competes
CC for binding POGZ (PubMed:10562550, PubMed:10330177, PubMed:25247314).
CC Interacts with POGZ; the interaction competes for interaction with
CC CBX5. Interacts with SETDB1; the interaction is enhanced by KAP1
CC sumoylation, stimulates SETDB1 histone methyltransferase activity and
CC gene silencing. Interacts (via the PHD-type zinc finger) with UBE2I;
CC the 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 CEBPB and NR3C1. Interacts with CBX5 (via
CC the PxVxL motif); the interaction occurs in interphase nuclei and
CC competes for binding POGZ. Component of a ternary complex that includes
CC TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5), a KRAB domain-containing
CC protein, and DNA. Interacts with SMARCAD1. Interacts with, and
CC sumoylates IRF7. Interacts with MAGEC2. Part of a complex composed of
CC TRIM28, HDAC1, HDAC2 and EHMT2. Interacts (via the RBCC domain) with
CC KOX1 (via the KRAB domain), ZNF268 (via the KRAB domain) and ZNF300
CC (via the KRAB domain); the interactions increase KOX1, ZNF268 and
CC ZNF300 nuclear localization activities. Interacts with AICDA. The large
CC PER complex involved in the histone methylation is composed of at least
CC PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation
CC of the complex. Interacts with NR4A3; the interactions potentiates
CC NR4A3 activity on NurRE promoter (PubMed:19321449). Interacts
CC (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain)
CC (By similarity). Probably part of a corepressor complex containing
CC ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with ATRX. Forms a complex
CC with ATRX, SETDB1 and ZNF274 (By similarity). Interacts with ZFP568;
CC the interaction mediates ZFP568 transcriptional repression activity
CC (PubMed:22110054, PubMed:27658112). Interacts with RRP1B (By
CC similarity). Interacts with CRY1 (PubMed:27123980). 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 (By similarity).
CC Interacts with CYREN (via XLF motif) (PubMed:30017584). Interacts with
CC TRIM17; this interaction prevents TRIM28 activity (By similarity).
CC Interacts with ZNF746 (By similarity). {ECO:0000250|UniProtKB:O08629,
CC ECO:0000250|UniProtKB:Q13263, ECO:0000269|PubMed:10330177,
CC ECO:0000269|PubMed:10562550, ECO:0000269|PubMed:11154279,
CC ECO:0000269|PubMed:19321449, ECO:0000269|PubMed:21518874,
CC ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:25247314,
CC ECO:0000269|PubMed:27123980, ECO:0000269|PubMed:27658112,
CC ECO:0000269|PubMed:30017584, ECO:0000269|PubMed:9742105}.
CC -!- INTERACTION:
CC Q62318; O35613: Daxx; NbExp=2; IntAct=EBI-346909, EBI-77304;
CC Q62318; P12813: Nr4a1; NbExp=3; IntAct=EBI-346909, EBI-10896863;
CC Q62318-1; P45481: Crebbp; NbExp=2; IntAct=EBI-6876996, EBI-296306;
CC Q62318-1; P20263: Pou5f1; NbExp=3; IntAct=EBI-6876996, EBI-1606219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330177,
CC ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:12154074,
CC ECO:0000269|PubMed:22110054}. Note=Associated with centromeric
CC heterochromatin during cell differentiation through CBX1.
CC {ECO:0000269|PubMed:10330177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62318-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62318-2; Sequence=VSP_010899, VSP_010900;
CC -!- DOMAIN: The HP1 box is both necessary and sufficient for HP1 binding.
CC {ECO:0000250|UniProtKB:Q13263}.
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:0000250|UniProtKB:Q13263}.
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:0000250|UniProtKB:Q13263}.
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:0000250|UniProtKB:Q13263}.
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:0000250|UniProtKB:Q13263}.
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:0000250|UniProtKB:Q13263}.
CC -!- PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
CC {ECO:0000250|UniProtKB:Q13263}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
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:0000269|PubMed:25247314}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with arrest at stage E5.5.
CC Gastrulation fails and expression of the critical mesoderm
CC differentiation factor T/brachyury is lost.
CC {ECO:0000269|PubMed:22110054}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; X99644; CAA67963.1; -; mRNA.
DR EMBL; U67303; AAB17272.1; -; mRNA.
DR EMBL; AF230878; AAG02638.1; -; Genomic_DNA.
DR EMBL; AF230391; AAG50170.1; -; mRNA.
DR EMBL; AF230392; AAG50171.1; -; mRNA.
DR EMBL; BC058391; AAH58391.1; -; mRNA.
DR EMBL; AK089084; BAC40742.1; -; mRNA.
DR CCDS; CCDS20823.1; -. [Q62318-1]
DR RefSeq; NP_035718.2; NM_011588.3. [Q62318-1]
DR PDB; 6O5K; X-ray; 1.60 A; A/B=135-203.
DR PDBsum; 6O5K; -.
DR AlphaFoldDB; Q62318; -.
DR BMRB; Q62318; -.
DR SASBDB; Q62318; -.
DR SMR; Q62318; -.
DR BioGRID; 204197; 79.
DR DIP; DIP-31477N; -.
DR ELM; Q62318; -.
DR IntAct; Q62318; 61.
DR MINT; Q62318; -.
DR STRING; 10090.ENSMUSP00000005705; -.
DR iPTMnet; Q62318; -.
DR PhosphoSitePlus; Q62318; -.
DR SwissPalm; Q62318; -.
DR REPRODUCTION-2DPAGE; IPI00312128; -.
DR REPRODUCTION-2DPAGE; Q62318; -.
DR EPD; Q62318; -.
DR jPOST; Q62318; -.
DR MaxQB; Q62318; -.
DR PaxDb; Q62318; -.
DR PeptideAtlas; Q62318; -.
DR PRIDE; Q62318; -.
DR ProteomicsDB; 259189; -. [Q62318-1]
DR ProteomicsDB; 259190; -. [Q62318-2]
DR Antibodypedia; 4109; 806 antibodies from 49 providers.
DR DNASU; 21849; -.
DR Ensembl; ENSMUST00000005705; ENSMUSP00000005705; ENSMUSG00000005566. [Q62318-1]
DR GeneID; 21849; -.
DR KEGG; mmu:21849; -.
DR UCSC; uc009ffb.2; mouse. [Q62318-1]
DR CTD; 10155; -.
DR MGI; MGI:109274; Trim28.
DR VEuPathDB; HostDB:ENSMUSG00000005566; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160527; -.
DR HOGENOM; CLU_005817_2_0_1; -.
DR InParanoid; Q62318; -.
DR OMA; DCKDEVP; -.
DR PhylomeDB; Q62318; -.
DR TreeFam; TF106455; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 21849; 32 hits in 118 CRISPR screens.
DR ChiTaRS; Trim28; mouse.
DR PRO; PR:Q62318; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62318; protein.
DR Bgee; ENSMUSG00000005566; Expressed in floor plate of midbrain and 276 other tissues.
DR ExpressionAtlas; Q62318; baseline and differential.
DR Genevisible; Q62318; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:MGI.
DR GO; GO:0043045; P:DNA methylation involved in embryo development; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:HGNC-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IDA:MGI.
DR GO; GO:1901536; P:negative regulation of DNA demethylation; IMP:MGI.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0016925; P:protein sumoylation; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:2000653; P:regulation of genetic imprinting; IMP:MGI.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR CDD; cd16765; RING-HC_TIF1beta; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037373; KAP1.
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; PTHR25462:SF274; PTHR25462:SF274; 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; SSF57903; SSF57903; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Bromodomain; Chromatin regulator; Citrullination; Coiled coil;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT CHAIN 2..834
FT /note="Transcription intermediary factor 1-beta"
FT /id="PRO_0000056393"
FT DOMAIN 697..801
FT /note="Bromo"
FT ZN_FING 66..122
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 149..196
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 205..246
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 13..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..377
FT /note="Leucine zipper alpha helical coiled-coil region"
FT REGION 248..377
FT /note="Interaction with MAGEC2"
FT /evidence="ECO:0000250"
FT REGION 367..371
FT /note="Involved in binding PPP1CA"
FT /evidence="ECO:0000250"
FT REGION 412..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..513
FT /note="HP1 box"
FT REGION 581..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 481..494
FT /note="PxVxL motif"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 238
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:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08629"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 305
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 341
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 378
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 470
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 472
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 755
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 770
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 774
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 779
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 824
FT /note="Phosphoserine; by ATM and ATR and dsDNA kinase"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 320
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 575
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 770
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT VAR_SEQ 500
FT /note="D -> L (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010899"
FT VAR_SEQ 501..834
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010900"
FT MUTAGEN 713..714
FT /note="CH->WN: In chatwo; hypomorphic mutation with reduced
FT protein stability and impaired transcriptional corepression
FT activity. Embryonic development arrests prior to stage E9,
FT with pronounced convergent extention defects and defective
FT morphogenesis of extra-embryonic tissues. The anterior-
FT posterior axis is shortened and embryos fail to undergo gut
FT closure. No effect on interaction with ZFP568."
FT /evidence="ECO:0000269|PubMed:22110054"
FT CONFLICT 530
FT /note="A -> S (in Ref. 2; AAB17272)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="G -> C (in Ref. 5; AAH58391)"
FT /evidence="ECO:0000305"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6O5K"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6O5K"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6O5K"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6O5K"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:6O5K"
FT TURN 186..190
FT /evidence="ECO:0007829|PDB:6O5K"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6O5K"
SQ SEQUENCE 834 AA; 88847 MW; DE87AAA5DC67BB8B CRC64;
MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ
ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV
CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE
AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD
HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI
LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT
ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG
PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG
LLRKVPRVSL ERLDLDLTSD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG
APGAPPLPGM AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS
SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP
GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL
HQLATDSTFS MEQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA
DVQSIIGLQR FFETRMNDAF GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP
