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 27-MAR-2024, entry version 237. 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, RC Pancreas, 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 proteasomal 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). Interacts with PHF13 (By CC similarity). Interacts with ZNF354C (By similarity). Interacts with CC ZNF432; the interaction is independent of PARP1 (By similarity). CC {ECO:0000250|UniProtKB:O08629, ECO:0000250|UniProtKB:Q13263, CC ECO:0000269|PubMed:10330177, ECO:0000269|PubMed:10562550, CC ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:19321449, CC ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22110054, CC ECO:0000269|PubMed:25247314, ECO:0000269|PubMed:27123980, CC ECO:0000269|PubMed:27658112, ECO:0000269|PubMed:30017584, CC 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; P17918: Pcna; NbExp=2; IntAct=EBI-346909, EBI-1173716; 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 (PubMed:10330177). Localizes to sites of DNA damage (By similarity). CC {ECO:0000250|UniProtKB:Q13263, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 82. DR DIP; DIP-31477N; -. DR ELM; Q62318; -. DR IntAct; Q62318; 62. DR MINT; Q62318; -. DR STRING; 10090.ENSMUSP00000005705; -. DR GlyGen; Q62318; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q62318; -. DR MetOSite; 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; 10090-ENSMUSP00000005705; -. DR PeptideAtlas; Q62318; -. DR ProteomicsDB; 259189; -. [Q62318-1] DR ProteomicsDB; 259190; -. [Q62318-2] DR Pumba; Q62318; -. DR Antibodypedia; 4109; 981 antibodies from 49 providers. DR DNASU; 21849; -. DR Ensembl; ENSMUST00000005705.8; ENSMUSP00000005705.8; ENSMUSG00000005566.15. [Q62318-1] DR GeneID; 21849; -. DR KEGG; mmu:21849; -. DR UCSC; uc009ffb.2; mouse. [Q62318-1] DR AGR; MGI:109274; -. 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 OrthoDB; 56754at2759; -. DR PhylomeDB; Q62318; -. DR TreeFam; TF106455; -. DR Reactome; R-MMU-212436; Generic Transcription Pathway. DR UniPathway; UPA00886; -. DR BioGRID-ORCS; 21849; 32 hits in 124 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 278 other cell types or tissues. DR ExpressionAtlas; Q62318; baseline and differential. 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:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0060028; P:convergent extension involved in axis elongation; 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:0071514; P:genomic imprinting; IMP:MGI. 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:0045892; P:negative regulation of DNA-templated transcription; IDA: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:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IMP:UniProtKB. DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:HGNC-UCL. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB. DR GO; GO:0043045; P:post-fertilization epigenetic regulation of gene expression; IMP:MGI. DR GO; GO:0016925; P:protein sumoylation; ISO:MGI. DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI. DR CDD; cd19846; Bbox1_TIF1b_C-VI; 1. DR CDD; cd19829; Bbox2_TIF1b_C-VI; 1. DR CDD; cd15623; PHD_TIF1beta; 1. DR CDD; cd16765; RING-HC_TIF1beta; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR InterPro; IPR003649; Bbox_C. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR037373; KAP1. DR InterPro; IPR047059; TIF1b_Bbox1_Znf. DR InterPro; IPR047058; TIF1b_Bbox2_Znf. DR InterPro; IPR042713; TIF1beta_RING-HC. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1. DR PANTHER; PTHR45915:SF9; TRIPARTITE MOTIF CONTAINING 28; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF00643; zf-B_box; 2. DR Pfam; PF14634; zf-RING_5; 1. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 2. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00184; RING; 2. DR SUPFAM; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50119; ZF_BBOX; 2. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q62318; MM. 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 FT anterior-posterior axis is shortened and embryos fail to FT undergo gut 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 //