ID NCOR2_HUMAN Reviewed; 2514 AA. AC Q9Y618; O00613; O15416; O15421; Q13354; Q56D06; Q59GM0; Q9Y5U0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 3. DT 27-MAR-2024, entry version 238. DE RecName: Full=Nuclear receptor corepressor 2 {ECO:0000305}; DE Short=N-CoR2 {ECO:0000305}; DE AltName: Full=CTG repeat protein 26; DE AltName: Full=SMAP270; DE AltName: Full=Silencing mediator of retinoic acid and thyroid hormone receptor {ECO:0000305}; DE Short=SMRT {ECO:0000305}; DE AltName: Full=T3 receptor-associating factor; DE Short=TRAC; DE AltName: Full=Thyroid-, retinoic-acid-receptor-associated corepressor; GN Name=NCOR2 {ECO:0000312|HGNC:HGNC:7673}; Synonyms=CTG26; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Fetal liver; RX PubMed=8813722; DOI=10.1210/mend.10.7.8813722; RA Sande S., Privalsky M.L.; RT "Identification of TRACs (T3 receptor-associating cofactors), a family of RT cofactors that associate with, and modulate the activity of, nuclear RT hormone receptors."; RL Mol. Endocrinol. 10:813-825(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT THR-1699. RC TISSUE=Pituitary; RX PubMed=10077563; DOI=10.1073/pnas.96.6.2639; RA Ordentlich P., Downes M., Xie W., Genin A., Spinner N.B., Evans R.M.; RT "Unique forms of human and mouse nuclear receptor corepressor SMRT."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2639-2644(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT THR-1699. RC TISSUE=Cervix adenocarcinoma; RX PubMed=10097068; DOI=10.1073/pnas.96.7.3519; RA Park E.J., Schroen D.J., Yang M., Li H., Li L., Chen J.D.; RT "SMRTe, a silencing mediator for retinoid and thyroid hormone receptors- RT extended isoform that is more related to the nuclear receptor RT corepressor."; RL Proc. Natl. Acad. Sci. U.S.A. 96:3519-3524(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT THR-1699. RA Chen J.D.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1451, AND VARIANT GLU-781. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 428-613. RC TISSUE=Brain cortex; RX PubMed=9225980; DOI=10.1007/s004390050476; RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.; RT "cDNAs with long CAG trinucleotide repeats from human brain."; RL Hum. Genet. 100:114-122(1997). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1023-2514, AND VARIANT THR-1699. RC TISSUE=Cervix adenocarcinoma; RX PubMed=7566127; DOI=10.1038/377454a0; RA Chen J.D., Evans R.M.; RT "A transcriptional co-repressor that interacts with nuclear hormone RT receptors."; RL Nature 377:454-457(1995). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE N-COR COMPLEX RP WITH TBL1X AND HDAC3. RX PubMed=10809664; RA Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., RA Shiekhattar R.; RT "A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat RT protein linked to deafness."; RL Genes Dev. 14:1048-1057(2000). RN [10] RP COMPONENT OF THE N-COR COMPLEX WITH TBL1X AND HDAC3. RX PubMed=10944117; DOI=10.1093/emboj/19.16.4342; RA Li J., Wang J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J.; RT "Both corepressor proteins SMRT and N-CoR exist in large protein complexes RT containing HDAC3."; RL EMBO J. 19:4342-4350(2000). RN [11] RP INTERACTION WITH MINT. RX PubMed=11331609; DOI=10.1101/gad.871201; RA Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., RA Evans R.M.; RT "Sharp, an inducible cofactor that integrates nuclear receptor repression RT and activation."; RL Genes Dev. 15:1140-1151(2001). RN [12] RP INTERACTION WITH CBFA2T3. RX PubMed=11533236; DOI=10.1128/mcb.21.19.6470-6483.2001; RA Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., RA Downing J.R., Meyers S., Hiebert S.W.; RT "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with RT multiple histone deacetylases and binds mSin3A through its oligomerization RT domain."; RL Mol. Cell. Biol. 21:6470-6483(2001). RN [13] RP COMPONENT OF THE N-COR COMPLEX WITH NCOR1; GPS2; TBL1X; TBL1R AND HDAC3. RX PubMed=11931768; DOI=10.1016/s1097-2765(02)00468-9; RA Zhang J., Kalkum M., Chait B.T., Roeder R.G.; RT "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK RT pathway through the integral subunit GPS2."; RL Mol. Cell 9:611-623(2002). RN [14] RP INTERACTION WITH HDAC10. RX PubMed=11739383; DOI=10.1074/jbc.m108055200; RA Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R., RA Trogani N., Widmer R., Atadja P., Cohen D.; RT "Isolation and characterization of a novel class II histone deacetylase, RT HDAC10."; RL J. Biol. Chem. 277:6656-6666(2002). RN [15] RP INTERACTION WITH RARB. RX PubMed=12554770; DOI=10.1210/me.2002-0340; RA Hauksdottir H., Farboud B., Privalsky M.L.; RT "Retinoic acid receptors beta and gamma do not repress, but instead RT activate target gene transcription in both the absence and presence of RT hormone ligand."; RL Mol. Endocrinol. 17:373-385(2003). RN [16] RP INTERACTION WITH BCL6. RX PubMed=15454082; DOI=10.1016/j.cell.2004.09.014; RA Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., RA Wade P.A.; RT "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte RT differentiation."; RL Cell 119:75-86(2004). RN [17] RP INTERACTION WITH ATXN1L. RX PubMed=16121196; DOI=10.1038/sj.emboj.7600785; RA Mizutani A., Wang L., Rajan H., Vig P.J.S., Alaynick W.A., Thaler J.P., RA Tsai C.-C.; RT "Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin- RT 1."; RL EMBO J. 24:3339-3351(2005). RN [18] RP ALTERNATIVE SPLICING (ISOFORM 4). RX PubMed=15632172; DOI=10.1074/jbc.m411514200; RA Goodson M.L., Jonas B.A., Privalsky M.L.; RT "Alternative mRNA splicing of SMRT creates functional diversity by RT generating corepressor isoforms with different affinities for different RT nuclear receptors."; RL J. Biol. Chem. 280:7493-7503(2005). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-215; THR-1383; RP SER-2005 AND SER-2258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [21] RP FUNCTION AS BCL6 COREPRESSOR, AND INTERACTION WITH BCL6. RX PubMed=18212045; DOI=10.1128/mcb.01400-07; RA Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A., RA Ye B.H.; RT "CtBP is an essential corepressor for BCL6 autoregulation."; RL Mol. Cell. Biol. 28:2175-2186(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-156; RP SER-750; SER-753; SER-1251; THR-1383; SER-1479; SER-2054; THR-2062; RP SER-2223 AND SER-2258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [24] RP IDENTIFICATION IN THE N-COR COMPLEX. RX PubMed=19858209; DOI=10.1074/jbc.m109.062109; RA Cheng X., Kao H.Y.; RT "G protein pathway suppressor 2 (GPS2) is a transcriptional corepressor RT important for estrogen receptor alpha-mediated transcriptional RT regulation."; RL J. Biol. Chem. 284:36395-36404(2009). RN [25] RP INTERACTION WITH RXRA. RX PubMed=19786558; DOI=10.1124/mol.109.057000; RA Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., RA Makishima M.; RT "The basic helix-loop-helix proteins differentiated embryo chondrocyte RT (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."; RL Mol. Pharmacol. 76:1360-1369(2009). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-149; SER-152; RP THR-553; SER-554; SER-939; SER-1323; SER-2046; SER-2054; SER-2057; RP SER-2058; SER-2223 AND SER-2258, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [27] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-878; LYS-959; LYS-1210; LYS-1240; RP LYS-1959 AND LYS-2026, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [28] RP INTERACTION WITH RARA, AND MUTAGENESIS OF ARG-2128; VAL-2130 AND THR-2131. RX PubMed=20543827; DOI=10.1038/nsmb.1855; RA le Maire A., Teyssier C., Erb C., Grimaldi M., Alvarez S., de Lera A.R., RA Balaguer P., Gronemeyer H., Royer C.A., Germain P., Bourguet W.; RT "A unique secondary-structure switch controls constitutive gene repression RT by retinoic acid receptor."; RL Nat. Struct. Mol. Biol. 17:801-807(2010). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-554; RP SER-956; SER-1861; SER-2203; SER-2223 AND SER-2258, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [31] RP FUNCTION, AND INTERACTION WITH AR AND ZBTB7A. RX PubMed=20812024; DOI=10.1007/s00018-010-0511-7; RA Cui J., Yang Y., Zhang C., Hu P., Kan W., Bai X., Liu X., Song H.; RT "FBI-1 functions as a novel AR co-repressor in prostate cancer cells."; RL Cell. Mol. Life Sci. 68:1091-1103(2011). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-956; RP SER-1778 AND SER-2258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [33] RP FUNCTION AS BCL6 COREPRESSOR, INTERACTION WITH BCL6 AND HDAC3, AND RP IDENTIFICATION IN A COMPLEX WITH BCL6 AND BCOR. RX PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016; RA Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D., RA Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M., RA Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W., RA Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.; RT "A hybrid mechanism of action for BCL6 in B cells defined by formation of RT functionally distinct complexes at enhancers and promoters."; RL Cell Rep. 4:578-588(2013). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-67; SER-215; SER-493; RP SER-939; THR-946; SER-956; SER-1173; SER-1251; SER-1323; THR-1383; RP SER-1479; SER-1539; SER-1619; SER-1775; SER-1778; SER-2054; SER-2077; RP SER-2223; SER-2258 AND SER-2413, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [35] RP INTERACTION WITH DEAF1. RX PubMed=23372760; DOI=10.1371/journal.pone.0054715; RA Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M., RA Franzmann T.M., Buchner J., Ansieau S., Sattler M.; RT "Structural and functional analysis of the DEAF-1 and BS69 MYND domains."; RL PLoS ONE 8:E54715-E54715(2013). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-215; RP SER-956; SER-2005; SER-2054 AND THR-2062, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [37] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1653, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [38] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1168, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [39] RP INTERACTION WITH TBL1Y. RX PubMed=30341416; DOI=10.1038/s41431-018-0282-4; RA Di Stazio M., Collesi C., Vozzi D., Liu W., Myers M., Morgan A., RA D Adamo P.A., Girotto G., Rubinato E., Giacca M., Gasparini P.; RT "TBL1Y: a new gene involved in syndromic hearing loss."; RL Eur. J. Hum. Genet. 27:466-474(2019). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1414-1430 IN COMPLEX WITH BL6. RX PubMed=14690607; DOI=10.1016/s1097-2765(03)00454-4; RA Ahmad K.F., Melnick A., Lax S., Bouchard D., Liu J., Kiang C.L., Mayer S., RA Takahashi S., Licht J.D., Prive G.G.; RT "Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain."; RL Mol. Cell 12:1551-1564(2003). RN [41] {ECO:0007744|PDB:2L5G} RP STRUCTURE BY NMR OF 167-207, IDENTIFICATION IN THE N-COR COMPLEX, AND RP MUTAGENESIS OF 242-HIS--LEU-245. RX PubMed=21240272; DOI=10.1038/nsmb.1983; RA Oberoi J., Fairall L., Watson P.J., Yang J.C., Czimmerer Z., Kampmann T., RA Goult B.T., Greenwood J.A., Gooch J.T., Kallenberger B.C., Nagy L., RA Neuhaus D., Schwabe J.W.; RT "Structural basis for the assembly of the SMRT/NCoR core transcriptional RT repression machinery."; RL Nat. Struct. Mol. Biol. 18:177-184(2011). CC -!- FUNCTION: Transcriptional corepressor (PubMed:20812024). Mediates the CC transcriptional repression activity of some nuclear receptors by CC promoting chromatin condensation, thus preventing access of the basal CC transcription. Isoform 1 and isoform 4 have different affinities for CC different nuclear receptors. Involved in the regulation BCL6-dependent CC of the germinal center (GC) reactions, mainly through the control of CC the GC B-cells proliferation and survival. Recruited by ZBTB7A to the CC androgen response elements/ARE on target genes, negatively regulates CC androgen receptor signaling and androgen-induced cell proliferation CC (PubMed:20812024). {ECO:0000269|PubMed:18212045, CC ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:23911289}. CC -!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B and CC histone deacetylases HDAC1 and HDAC2. This complex associates with the CC thyroid (TR) and the retinoid acid receptors (RAR) in the absence of CC ligand, and may stabilize their interaction with TFIIB. Interacts CC directly with RARA in the absence of ligand; the interaction represses CC RARA activity. Interacts (isoform SMRT) with HDAC10. Interacts with CC MINT. Component of the N-Cor repressor complex, at least composed of CC NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2 (PubMed:10809664, CC PubMed:10944117, PubMed:11931768, PubMed:19858209, PubMed:21240272). CC Interacts with CBFA2T3 and ATXN1L. Interacts with RARB; the interaction CC is weak and does not repress RARB transactivational activity. Interacts CC with HDAC7 and C1D. Interacts with NR4A2; this interaction increases in CC the absence of PITX3. Interacts with BCL6 (via the BTB domain), CC required for BCL6 transcriptional repressor activity on a subset of CC target genes. Forms ternary complexes with BCOR and BCL6 on target gene CC promoters but, on enhancer elements, interacts with BCL6 and HDAC3 to CC repress proximal gene expression. May interact with DEAF1. Interacts CC with RXRA. Interacts with MECP2 (By similarity). Interacts with ZBTB7A CC (PubMed:20812024). Interacts with AR (PubMed:20812024). Interacts with CC TBL1Y (PubMed:30341416). Interacts with SANBR (via the BTB domain) (By CC similarity). {ECO:0000250|UniProtKB:Q9WU42, CC ECO:0000269|PubMed:10809664, ECO:0000269|PubMed:10944117, CC ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11533236, CC ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:11931768, CC ECO:0000269|PubMed:12554770, ECO:0000269|PubMed:14690607, CC ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:16121196, CC ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:19786558, CC ECO:0000269|PubMed:19858209, ECO:0000269|PubMed:20543827, CC ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:21240272, CC ECO:0000269|PubMed:23372760, ECO:0000269|PubMed:23911289, CC ECO:0000269|PubMed:30341416}. CC -!- INTERACTION: CC Q9Y618; P35869: AHR; NbExp=2; IntAct=EBI-80830, EBI-80780; CC Q9Y618; P27540: ARNT; NbExp=2; IntAct=EBI-80830, EBI-80809; CC Q9Y618; Q01094: E2F1; NbExp=2; IntAct=EBI-80830, EBI-448924; CC Q9Y618; Q13547: HDAC1; NbExp=2; IntAct=EBI-80830, EBI-301834; CC Q9Y618; O15379: HDAC3; NbExp=13; IntAct=EBI-80830, EBI-607682; CC Q9Y618; O00629: KPNA4; NbExp=32; IntAct=EBI-80830, EBI-396343; CC Q9Y618; Q15156: PML-RAR; NbExp=2; IntAct=EBI-80830, EBI-867256; CC Q9Y618; P10276: RARA; NbExp=4; IntAct=EBI-80830, EBI-413374; CC Q9Y618; Q06330: RBPJ; NbExp=3; IntAct=EBI-80830, EBI-632552; CC Q9Y618; Q13573: SNW1; NbExp=4; IntAct=EBI-80830, EBI-632715; CC Q9Y618; Q96T58: SPEN; NbExp=5; IntAct=EBI-80830, EBI-765739; CC Q9Y618; P10828-1: THRB; NbExp=3; IntAct=EBI-80830, EBI-3955784; CC Q9Y618; P04637: TP53; NbExp=7; IntAct=EBI-80830, EBI-366083; CC Q9Y618; O88513: Gmnn; Xeno; NbExp=3; IntAct=EBI-80830, EBI-445922; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=SMRT-alpha {ECO:0000303|PubMed:15632172}, TRAC-2, CC h-SMRT; CC IsoId=Q9Y618-1; Sequence=Displayed; CC Name=2; Synonyms=TRAC-1; CC IsoId=Q9Y618-2; Sequence=VSP_003412, VSP_003413; CC Name=3; Synonyms=SMRTe; CC IsoId=Q9Y618-4; Sequence=VSP_036595; CC Name=4; Synonyms=SMRT-tau {ECO:0000303|PubMed:15632172}; CC IsoId=Q9Y618-5; Sequence=VSP_036595, VSP_003413; CC -!- TISSUE SPECIFICITY: Ubiquitous. High levels of expression are detected CC in lung, spleen and brain. CC -!- INDUCTION: Regulated during cell cycle progression. CC -!- DOMAIN: The N-terminal region contains repression functions that are CC divided into three independent repression domains (RD1, RD2 and RD3). CC The C-terminal region contains the nuclear receptor-interacting domains CC that are divided in two separate interaction domains (ID1 and ID2). CC -!- DOMAIN: The two interaction domains (ID) contain a conserved sequence CC referred to as the CORNR box. This motif is required and sufficient to CC permit binding to unligated TR and RARS. Sequences flanking the CORNR CC box determine nuclear hormone receptor specificity. CC -!- MISCELLANEOUS: [Isoform 2]: Contains only the C-terminal receptor- CC interacting domain and acts as an antirepressor. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB91452.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC Sequence=AAC50236.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305}; CC Sequence=AAD20946.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAD92326.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; S83390; AAB50847.1; -; mRNA. DR EMBL; AF113003; AAD20946.1; ALT_FRAME; mRNA. DR EMBL; AF125672; AAD22973.1; -; mRNA. DR EMBL; AY965853; AAX77219.1; -; mRNA. DR EMBL; AC069261; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC073916; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB209089; BAD92326.1; ALT_INIT; mRNA. DR EMBL; U80750; AAB91446.1; -; mRNA. DR EMBL; U80761; AAB91452.1; ALT_SEQ; mRNA. DR EMBL; U37146; AAC50236.1; ALT_SEQ; mRNA. DR CCDS; CCDS41858.2; -. [Q9Y618-1] DR PIR; S60255; S60255. DR RefSeq; NP_001070729.2; NM_001077261.3. DR RefSeq; NP_001193583.1; NM_001206654.1. DR RefSeq; NP_006303.4; NM_006312.5. [Q9Y618-1] DR PDB; 1KKQ; X-ray; 3.00 A; E/F/G/H=2336-2354. DR PDB; 1R2B; X-ray; 2.20 A; C/D=1414-1430. DR PDB; 1XC5; NMR; -; A=412-480. DR PDB; 2GPV; X-ray; 2.85 A; G/H/I=2335-2356. DR PDB; 2L5G; NMR; -; B=167-207. DR PDB; 2LTP; NMR; -; A=615-685. DR PDB; 2ODD; NMR; -; B=1101-1113. DR PDB; 2RT5; NMR; -; B=2507-2514. DR PDB; 3R29; X-ray; 2.90 A; C/D=2335-2350. DR PDB; 3R2A; X-ray; 3.00 A; E/F=2335-2350. DR PDB; 4A69; X-ray; 2.06 A; C/D=389-480. DR PDB; 4OAR; X-ray; 2.41 A; B=2335-2351. DR PDB; 5X8Q; X-ray; 2.20 A; B/D/F/H=2335-2356. DR PDB; 5X8X; X-ray; 2.60 A; B/D/F/H=2335-2356. DR PDB; 5ZOO; X-ray; 1.85 A; A=1350-1363. DR PDB; 5ZOP; X-ray; 2.70 A; A=1448-1459. DR PDB; 6A22; X-ray; 2.55 A; B/D/F/H=2335-2356. DR PDB; 6IVX; X-ray; 2.35 A; B/D/F/H=2335-2356. DR PDB; 6PDZ; X-ray; 2.10 A; C/D=2335-2356. DR PDB; 7SQA; X-ray; 2.50 A; C/D=2335-2356. DR PDB; 8AQM; X-ray; 2.30 A; C/D=2332-2354. DR PDB; 8AQN; X-ray; 1.90 A; C/D=2332-2354. DR PDB; 8B8W; X-ray; 1.86 A; C/D=2332-2354. DR PDB; 8B8X; X-ray; 1.78 A; C/D=2332-2354. DR PDB; 8B8Y; X-ray; 2.00 A; C/D=2332-2354. DR PDB; 8B8Z; X-ray; 2.22 A; C/D=2332-2354. DR PDB; 8B90; X-ray; 2.10 A; C/D=2332-2354. DR PDB; 8B91; X-ray; 2.23 A; C/D=2332-2354. DR PDB; 8B92; X-ray; 1.66 A; C/D=2332-2354. DR PDB; 8B93; X-ray; 2.21 A; C/D=2332-2354. DR PDB; 8B94; X-ray; 1.55 A; C/D=2332-2354. DR PDB; 8B95; X-ray; 1.72 A; C/D=2332-2354. DR PDBsum; 1KKQ; -. DR PDBsum; 1R2B; -. DR PDBsum; 1XC5; -. DR PDBsum; 2GPV; -. DR PDBsum; 2L5G; -. DR PDBsum; 2LTP; -. DR PDBsum; 2ODD; -. DR PDBsum; 2RT5; -. DR PDBsum; 3R29; -. DR PDBsum; 3R2A; -. DR PDBsum; 4A69; -. DR PDBsum; 4OAR; -. DR PDBsum; 5X8Q; -. DR PDBsum; 5X8X; -. DR PDBsum; 5ZOO; -. DR PDBsum; 5ZOP; -. DR PDBsum; 6A22; -. DR PDBsum; 6IVX; -. DR PDBsum; 6PDZ; -. DR PDBsum; 7SQA; -. DR PDBsum; 8AQM; -. DR PDBsum; 8AQN; -. DR PDBsum; 8B8W; -. DR PDBsum; 8B8X; -. DR PDBsum; 8B8Y; -. DR PDBsum; 8B8Z; -. DR PDBsum; 8B90; -. DR PDBsum; 8B91; -. DR PDBsum; 8B92; -. DR PDBsum; 8B93; -. DR PDBsum; 8B94; -. DR PDBsum; 8B95; -. DR AlphaFoldDB; Q9Y618; -. DR BMRB; Q9Y618; -. DR SMR; Q9Y618; -. DR BioGRID; 114974; 242. DR CORUM; Q9Y618; -. DR DIP; DIP-951N; -. DR ELM; Q9Y618; -. DR IntAct; Q9Y618; 111. DR MINT; Q9Y618; -. DR STRING; 9606.ENSP00000384018; -. DR BindingDB; Q9Y618; -. DR ChEMBL; CHEMBL2111363; -. DR ChEMBL; CHEMBL3885590; -. DR ChEMBL; CHEMBL3885591; -. DR DrugCentral; Q9Y618; -. DR GlyCosmos; Q9Y618; 20 sites, 1 glycan. DR GlyGen; Q9Y618; 30 sites, 1 O-linked glycan (30 sites). DR iPTMnet; Q9Y618; -. DR MetOSite; Q9Y618; -. DR PhosphoSitePlus; Q9Y618; -. DR BioMuta; NCOR2; -. DR DMDM; 226713806; -. DR EPD; Q9Y618; -. DR jPOST; Q9Y618; -. DR MassIVE; Q9Y618; -. DR MaxQB; Q9Y618; -. DR PaxDb; 9606-ENSP00000384018; -. DR PeptideAtlas; Q9Y618; -. DR ProteomicsDB; 86582; -. [Q9Y618-1] DR ProteomicsDB; 86583; -. [Q9Y618-2] DR ProteomicsDB; 86585; -. [Q9Y618-4] DR ProteomicsDB; 86586; -. [Q9Y618-5] DR Pumba; Q9Y618; -. DR Antibodypedia; 1103; 315 antibodies from 36 providers. DR DNASU; 9612; -. DR Ensembl; ENST00000405201.6; ENSP00000384018.1; ENSG00000196498.15. [Q9Y618-1] DR GeneID; 9612; -. DR KEGG; hsa:9612; -. DR MANE-Select; ENST00000405201.6; ENSP00000384018.1; NM_006312.6; NP_006303.4. DR UCSC; uc058uwu.1; human. [Q9Y618-1] DR AGR; HGNC:7673; -. DR CTD; 9612; -. DR DisGeNET; 9612; -. DR GeneCards; NCOR2; -. DR HGNC; HGNC:7673; NCOR2. DR HPA; ENSG00000196498; Low tissue specificity. DR MIM; 600848; gene. DR neXtProt; NX_Q9Y618; -. DR OpenTargets; ENSG00000196498; -. DR PharmGKB; PA31478; -. DR VEuPathDB; HostDB:ENSG00000196498; -. DR eggNOG; KOG1878; Eukaryota. DR GeneTree; ENSGT00940000159022; -. DR InParanoid; Q9Y618; -. DR OMA; RAMPHDS; -. DR OrthoDB; 5482374at2759; -. DR PhylomeDB; Q9Y618; -. DR PathwayCommons; Q9Y618; -. DR Reactome; R-HSA-1989781; PPARA activates gene expression. DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; R-HSA-3214815; HDACs deacetylate histones. DR Reactome; R-HSA-350054; Notch-HLH transcription pathway. DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha. DR Reactome; R-HSA-9022537; Loss of MECP2 binding ability to the NCoR/SMRT complex. DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity. DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR SignaLink; Q9Y618; -. DR SIGNOR; Q9Y618; -. DR BioGRID-ORCS; 9612; 47 hits in 1186 CRISPR screens. DR ChiTaRS; NCOR2; human. DR EvolutionaryTrace; Q9Y618; -. DR GeneWiki; Nuclear_receptor_co-repressor_2; -. DR GenomeRNAi; 9612; -. DR Pharos; Q9Y618; Tchem. DR PRO; PR:Q9Y618; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9Y618; Protein. DR Bgee; ENSG00000196498; Expressed in sural nerve and 201 other cell types or tissues. DR ExpressionAtlas; Q9Y618; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:MGI. DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0017053; C:transcription repressor complex; IDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB. DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IEA:Ensembl. DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl. DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0007595; P:lactation; IEA:Ensembl. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:1902894; P:negative regulation of miRNA transcription; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0010565; P:regulation of cellular ketone metabolic process; IMP:BHF-UCL. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl. DR CDD; cd00167; SANT; 1. DR Gene3D; 1.20.5.430; -; 1. DR Gene3D; 1.20.58.1880; -; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR IDEAL; IID00109; -. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR031557; N-CoR_GPS2_interact. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR017884; SANT_dom. DR PANTHER; PTHR13992; NUCLEAR RECEPTOR CO-REPRESSOR RELATED NCOR; 1. DR PANTHER; PTHR13992:SF21; NUCLEAR RECEPTOR COREPRESSOR 2; 1. DR Pfam; PF15784; GPS2_interact; 1. DR Pfam; PF00249; Myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS51293; SANT; 2. DR Genevisible; Q9Y618; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; DNA-binding; KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..2514 FT /note="Nuclear receptor corepressor 2" FT /id="PRO_0000055622" FT DOMAIN 427..478 FT /note="SANT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT DOMAIN 610..661 FT /note="SANT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 120..162 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 190..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 254..312 FT /note="Interaction with SIN3A/B" FT /evidence="ECO:0000250" FT REGION 487..622 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 674..1081 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1165..1186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1287..1307 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1440..1482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1506..1609 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1763..1867 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1937..2124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2128..2131 FT /note="Required for interaction with RARA in the absence of FT its ligand" FT REGION 2174..2235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2248..2269 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2384..2500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 174..215 FT /evidence="ECO:0000255" FT COILED 522..561 FT /evidence="ECO:0000255" FT MOTIF 2136..2140 FT /note="CORNR box of ID1" FT MOTIF 2339..2343 FT /note="CORNR box of ID2" FT COMPBIAS 190..209 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 492..514 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 515..567 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 578..611 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 738..760 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..794 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..821 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 842..901 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 902..922 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 990..1008 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1049..1065 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1454..1472 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1563..1583 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1584..1609 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1766..1790 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1791..1816 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1817..1867 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2065..2085 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2252..2269 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2425..2439 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 18 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9WU42" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:23186163" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 149 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 156 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 493 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 553 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 554 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 750 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 753 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 878 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 939 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 946 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 956 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 959 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1210 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1240 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1251 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1323 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1383 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1479 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1539 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1595 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WU42" FT MOD_RES 1619 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1653 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1775 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1778 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1861 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1959 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 2005 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2026 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 2046 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2054 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2057 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2058 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2060 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WU42" FT MOD_RES 2062 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2077 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 2223 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2258 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 1168 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..1702 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8813722" FT /id="VSP_003412" FT VAR_SEQ 724..740 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:10097068, ECO:0000303|Ref.4" FT /id="VSP_036595" FT VAR_SEQ 2350..2395 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:8813722, ECO:0000303|Ref.4" FT /id="VSP_003413" FT VARIANT 781 FT /note="G -> E (in dbSNP:rs7978237)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_060073" FT VARIANT 1699 FT /note="A -> T (in dbSNP:rs2229840)" FT /evidence="ECO:0000269|PubMed:10077563, FT ECO:0000269|PubMed:10097068, ECO:0000269|PubMed:7566127, FT ECO:0000269|Ref.4" FT /id="VAR_054751" FT VARIANT 2001 FT /note="P -> S (in dbSNP:rs2230944)" FT /id="VAR_060074" FT MUTAGEN 242..245 FT /note="HRIL->AEIA: Abolishes interaction with TBL1X." FT /evidence="ECO:0000269|PubMed:21240272" FT MUTAGEN 2128 FT /note="R->A: Abolishes interaction with the apo LBD of FT RARA. Restores some interaction on the addition of inverse FT agonist BMS493." FT /evidence="ECO:0000269|PubMed:20543827" FT MUTAGEN 2130 FT /note="V->P: Abolishes interaction with the apo LBD of FT RARA. No change on interaction on the addition of inverse FT agonist BMS493." FT /evidence="ECO:0000269|PubMed:20543827" FT MUTAGEN 2131 FT /note="T->G: Abolishes interaction with the apo LBD of FT RARA. Restores some interaction on the addition of inverse FT agonist BMS493." FT /evidence="ECO:0000269|PubMed:20543827" FT CONFLICT 7 FT /note="P -> L (in Ref. 2; AAD20946)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="E -> K (in Ref. 2; AAD20946)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="W -> L (in Ref. 2; AAD20946)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="Missing (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 365 FT /note="A -> P (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 612..613 FT /note="SS -> EF (in Ref. 7; AAB91446)" FT /evidence="ECO:0000305" FT CONFLICT 711 FT /note="S -> T (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 796 FT /note="P -> S (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 804 FT /note="G -> L (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 814 FT /note="S -> F (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 817 FT /note="A -> S (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 889 FT /note="G -> R (in Ref. 3; AAD22973 and 4; AAX77219)" FT /evidence="ECO:0000305" FT CONFLICT 1562 FT /note="T -> M (in Ref. 2; AAD20946, 3; AAD22973, 4; FT AAX77219 and 8; AAC50236)" FT /evidence="ECO:0000305" FT CONFLICT 1839 FT /note="G -> GSSG (in Ref. 2; AAD20946)" FT /evidence="ECO:0000305" FT CONFLICT 1891 FT /note="T -> K (in Ref. 2; AAD20946, 3; AAD22973, 4; FT AAX77219 and 8; AAC50236)" FT /evidence="ECO:0000305" FT CONFLICT 2491 FT /note="P -> A (in Ref. 1; AAB50847)" FT /evidence="ECO:0000305" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:2L5G" FT HELIX 171..205 FT /evidence="ECO:0007829|PDB:2L5G" FT STRAND 414..417 FT /evidence="ECO:0007829|PDB:4A69" FT HELIX 419..428 FT /evidence="ECO:0007829|PDB:4A69" FT HELIX 434..446 FT /evidence="ECO:0007829|PDB:4A69" FT HELIX 451..456 FT /evidence="ECO:0007829|PDB:4A69" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:1XC5" FT HELIX 463..473 FT /evidence="ECO:0007829|PDB:4A69" FT TURN 474..476 FT /evidence="ECO:0007829|PDB:1XC5" FT HELIX 617..629 FT /evidence="ECO:0007829|PDB:2LTP" FT TURN 630..632 FT /evidence="ECO:0007829|PDB:2LTP" FT HELIX 634..640 FT /evidence="ECO:0007829|PDB:2LTP" FT STRAND 642..644 FT /evidence="ECO:0007829|PDB:2LTP" FT HELIX 646..655 FT /evidence="ECO:0007829|PDB:2LTP" FT HELIX 661..679 FT /evidence="ECO:0007829|PDB:2LTP" FT STRAND 1108..1110 FT /evidence="ECO:0007829|PDB:2ODD" FT STRAND 1352..1354 FT /evidence="ECO:0007829|PDB:5ZOO" FT TURN 1355..1358 FT /evidence="ECO:0007829|PDB:5ZOO" FT STRAND 1359..1362 FT /evidence="ECO:0007829|PDB:5ZOO" FT STRAND 1416..1420 FT /evidence="ECO:0007829|PDB:1R2B" FT TURN 1451..1454 FT /evidence="ECO:0007829|PDB:5ZOP" FT HELIX 2339..2347 FT /evidence="ECO:0007829|PDB:8B94" FT HELIX 2351..2353 FT /evidence="ECO:0007829|PDB:8AQN" SQ SEQUENCE 2514 AA; 273657 MW; 70A89C9A19612AAD CRC64; MSGSTQPVAQ TWRATEPRYP PHSLSYPVQI ARTHTDVGLL EYQHHSRDYA SHLSPGSIIQ PQRRRPSLLS EFQPGNERSQ ELHLRPESHS YLPELGKSEM EFIESKRPRL ELLPDPLLRP SPLLATGQPA GSEDLTKDRS LTGKLEPVSP PSPPHTDPEL ELVPPRLSKE ELIQNMDRVD REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQKFCQ RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMADPM KVYKDRQVMN MWSEQEKETF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK SLVRRSYRRR GKSQQQQQQQ QQQQQQQQQQ PMPRSSQEEK DEKEKEKEAE KEEEKPEVEN DKEDLLKEKT DDTSGEDNDE KEAVASKGRK TANSQGRRKG RITRSMANEA NSEEAITPQQ SAELASMELN ESSRWTEEEM ETAKKGLLEH GRNWSAIARM VGSKTVSQCK NFYFNYKKRQ NLDEILQQHK LKMEKERNAR RKKKKAPAAA SEEAAFPPVV EDEEMEASGV SGNEEEMVEE AEALHASGNE VPRGECSGPA TVNNSSDTES IPSPHTEAAK DTGQNGPKPP ATLGADGPPP GPPTPPPEDI PAPTEPTPAS EATGAPTPPP APPSPSAPPP VVPKEEKEEE TAAAPPVEEG EEQKPPAAEE LAVDTGKAEE PVKSECTEEA EEGPAKGKDA EAAEATAEGA LKAEKKEGGS GRATTAKSSG APQDSDSSAT CSADEVDEAE GGDKNRLLSP RPSLLTPTGD PRANASPQKP LDLKQLKQRA AAIPPIQVTK VHEPPREDAA PTKPAPPAPP PPQNLQPESD APQQPGSSPR GKSRSPAPPA DKEAFAAEAQ KLPGDPPCWT SGLPFPVPPR EVIKASPHAP DPSAFSYAPP GHPLPLGLHD TARPVLPRPP TISNPPPLIS SAKHPSVLER QIGAISQGMS VQLHVPYSEH AKAPVGPVTM GLPLPMDPKK LAPFSGVKQE QLSPRGQAGP PESLGVPTAQ EASVLRGTAL GSVPGGSITK GIPSTRVPSD SAITYRGSIT HGTPADVLYK GTITRIIGED SPSRLDRGRE DSLPKGHVIY EGKKGHVLSY EGGMSVTQCS KEDGRSSSGP PHETAAPKRT YDMMEGRVGR AISSASIEGL MGRAIPPERH SPHHLKEQHH IRGSITQGIP RSYVEAQEDY LRREAKLLKR EGTPPPPPPS RDLTEAYKTQ ALGPLKLKPA HEGLVATVKE AGRSIHEIPR EELRHTPELP LAPRPLKEGS ITQGTPLKYD TGASTTGSKK HDVRSLIGSP GRTFPPVHPL DVMADARALE RACYEESLKS RPGTASSSGG SIARGAPVIV PELGKPRQSP LTYEDHGAPF AGHLPRGSPV TTREPTPRLQ EGSLSSSKAS QDRKLTSTPR EIAKSPHSTV PEHHPHPISP YEHLLRGVSG VDLYRSHIPL AFDPTSIPRG IPLDAAAAYY LPRHLAPNPT YPHLYPPYLI RGYPDTAALE NRQTIINDYI TSQQMHHNAA TAMAQRADML RGLSPRESSL ALNYAAGPRG IIDLSQVPHL PVLVPPTPGT PATAMDRLAY LPTAPQPFSS RHSSSPLSPG GPTHLTKPTT TSSSERERDR DRERDRDRER EKSILTSTTT VEHAPIWRPG TEQSSGSSGG GGGSSSRPAS HSHAHQHSPI SPRTQDALQQ RPSVLHNTGM KGIITAVEPS TPTVLRSTST SSPVRPAATF PPATHCPLGG TLDGVYPTLM EPVLLPKEAP RVARPERPRA DTGHAFLAKP PARSGLEPAS SPSKGSEPRP LVPPVSGHAT IARTPAKNLA PHHASPDPPA PPASASDPHR EKTQSKPFSI QELELRSLGY HGSSYSPEGV EPVSPVSSPS LTHDKGLPKH LEELDKSHLE GELRPKQPGP VKLGGEAAHL PHLRPLPESQ PSSSPLLQTA PGVKGHQRVV TLAQHISEVI TQDYTRHHPQ QLSAPLPAPL YSFPGASCPV LDLRRPPSDL YLPPPDHGAP ARGSPHSEGG KRSPEPNKTS VLGGGEDGIE PVSPPEGMTE PGHSRSAVYP LLYRDGEQTE PSRMGSKSPG NTSQPPAFFS KLTESNSAMV KSKKQEINKK LNTHNRNEPE YNISQPGTEI FNMPAITGTG LMTYRSQAVQ EHASTNMGLE AIIRKALMGK YDQWEESPPL SANAFNPLNA SASLPAAMPI TAADGRSDHT LTSPGGGGKA KVSGRPSSRK AKSPAPGLAS GDRPPSVSSV HSEGDCNRRT PLTNRVWEDR PSSAGSTPFP YNPLIMRLQA GVMASPPPPG LPAGSGPLAG PHHAWDEEPK PLLCSQYETL SDSE //