NCOR2_HUMAN
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 03-AUG-2022, entry version 229.
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=10; 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; 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};
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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 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 AlphaFoldDB; Q9Y618; -.
DR BMRB; Q9Y618; -.
DR SMR; Q9Y618; -.
DR BioGRID; 114974; 217.
DR CORUM; Q9Y618; -.
DR DIP; DIP-951N; -.
DR ELM; Q9Y618; -.
DR IntAct; Q9Y618; 109.
DR MINT; Q9Y618; -.
DR STRING; 9606.ENSP00000384018; -.
DR BindingDB; Q9Y618; -.
DR ChEMBL; CHEMBL2111363; -.
DR ChEMBL; CHEMBL3885590; -.
DR ChEMBL; CHEMBL3885591; -.
DR DrugCentral; Q9Y618; -.
DR GlyGen; Q9Y618; 20 sites, 1 O-linked glycan (20 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; Q9Y618; -.
DR PeptideAtlas; Q9Y618; -.
DR PRIDE; Q9Y618; -.
DR ProteomicsDB; 86582; -. [Q9Y618-1]
DR ProteomicsDB; 86583; -. [Q9Y618-2]
DR ProteomicsDB; 86585; -. [Q9Y618-4]
DR ProteomicsDB; 86586; -. [Q9Y618-5]
DR Antibodypedia; 1103; 279 antibodies from 36 providers.
DR DNASU; 9612; -.
DR Ensembl; ENST00000405201.5; ENSP00000384018.1; ENSG00000196498.13. [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 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; VMRPSSH; -.
DR OrthoDB; 12227at2759; -.
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; 43 hits in 1107 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 199 other tissues.
DR ExpressionAtlas; Q9Y618; baseline and differential.
DR Genevisible; Q9Y618; HS.
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:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
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:1903799; P:negative regulation of miRNA maturation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0010565; P:regulation of cellular ketone metabolic process; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 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 Pfam; PF15784; GPS2_interact; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 2.
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 2338..2347
FT /evidence="ECO:0007829|PDB:6PDZ"
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
