NCOR1_HUMAN
ID NCOR1_HUMAN Reviewed; 2440 AA.
AC O75376; B3DLF8; E9PGV6; Q86YY0; Q9UPV5; Q9UQ18;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Nuclear receptor corepressor 1;
DE Short=N-CoR;
DE Short=N-CoR1;
GN Name=NCOR1; Synonyms=KIAA1047;
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 1).
RC TISSUE=Fetal brain;
RX PubMed=9724795; DOI=10.1073/pnas.95.18.10860;
RA Wang J., Hoshino T., Redner R.L., Kajigaya S., Liu J.M.;
RT "ETO, fusion partner in t(8;21) acute myeloid leukemia, represses
RT transcription by interaction with the human N-CoR/mSin3/HDAC1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10860-10865(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Yu L.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 974-2440 (ISOFORM 1).
RX PubMed=10444336; DOI=10.1006/geno.1998.5694;
RA Nagaya T., Chen K.-S., Fujieda M., Ohmori S., Richer J.K., Horwitz K.B.,
RA Lupski J.R., Seo H.;
RT "Localization of the human nuclear receptor co-repressor (hN-CoR) gene
RT between the CMT1A and the SMS critical regions of chromosome 17p11.2.";
RL Genomics 59:339-341(1999).
RN [9]
RP INTERACTION WITH RORA.
RX PubMed=9328355; DOI=10.1210/mend.11.11.0002;
RA Harding H.P., Atkins G.B., Jaffe A.B., Seo W.J., Lazar M.A.;
RT "Transcriptional activation and repression by RORalpha, an orphan nuclear
RT receptor required for cerebellar development.";
RL Mol. Endocrinol. 11:1737-1746(1997).
RN [10]
RP INTERACTION WITH TRIM28.
RX PubMed=11013263; DOI=10.1074/jbc.m007864200;
RA Underhill C., Qutob M.S., Yee S.P., Torchia J.;
RT "A novel nuclear receptor corepressor complex, N-CoR, contains components
RT of the mammalian SWI/SNF complex and the corepressor KAP-1.";
RL J. Biol. Chem. 275:40463-40470(2000).
RN [11]
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 [12]
RP COMPONENT OF THE N-COR COMPLEX WITH TBL1X; TBL1R; NCOR2; GPS2 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 [13]
RP INTERACTION WITH HDAC9.
RX PubMed=12590135; DOI=10.1074/jbc.m212935200;
RA Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
RA Zelent A.;
RT "The histone deacetylase 9 gene encodes multiple protein isoforms.";
RL J. Biol. Chem. 278:16059-16072(2003).
RN [14]
RP INTERACTION WITH DACH1.
RX PubMed=14525983; DOI=10.1074/jbc.m310021200;
RA Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K.,
RA Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.;
RT "DACH1 inhibits transforming growth factor-beta signaling through binding
RT Smad4.";
RL J. Biol. Chem. 278:51673-51684(2003).
RN [15]
RP FUNCTION, AND INTERACTION WITH CORO2A; GPS2; HDAC3; TBL1R; TBL1X AND
RP ZBTB33.
RX PubMed=14527417; DOI=10.1016/j.molcel.2003.08.008;
RA Yoon H.-G., Chan D.W., Reynolds A.B., Qin J., Wong J.;
RT "N-CoR mediates DNA methylation-dependent repression through a methyl CpG
RT binding protein Kaiso.";
RL Mol. Cell 12:723-734(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 KDM3A.
RX PubMed=16024779; DOI=10.1128/mcb.25.15.6404-6414.2005;
RA Zhang D., Yoon H.-G., Wong J.;
RT "JMJD2A is a novel N-CoR-interacting protein and is involved in repression
RT of the human transcription factor achaete scute-like homologue 2
RT (ASCL2/Hash2).";
RL Mol. Cell. Biol. 25:6404-6414(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-999 AND SER-2151,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [20]
RP INTERACTION WITH HEXIM1.
RX PubMed=17452463; DOI=10.1128/mcb.00857-06;
RA Fu J., Yoon H.-G., Qin J., Wong J.;
RT "Regulation of P-TEFb elongation complex activity by CDK9 acetylation.";
RL Mol. Cell. Biol. 27:4641-4651(2007).
RN [21]
RP INTERACTION WITH BAZ1A.
RX PubMed=17519354; DOI=10.1210/me.2007-0095;
RA Ewing A.K., Attner M., Chakravarti D.;
RT "Novel regulatory role for human Acf1 in transcriptional repression of
RT vitamin D3 receptor-regulated genes.";
RL Mol. Endocrinol. 21:1791-1806(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; SER-1472; SER-1977;
RP SER-1981; SER-2184; THR-2399; SER-2436 AND SER-2438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-1977; SER-2151;
RP SER-2184 AND SER-2436, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-1412, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-2184 AND SER-2438,
RP AND IDENTIFICATION BY 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 [29]
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 [30]
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195; SER-1472; SER-2151;
RP SER-2436 AND SER-2438, 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 [32]
RP INTERACTION WITH BCL6.
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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-224; SER-1111;
RP SER-1196; SER-1249; SER-1263; SER-1281; SER-1322; SER-1450; SER-1472;
RP SER-1592; SER-1977; SER-2120; SER-2151 AND SER-2184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [34]
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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-1472; SER-2136 AND
RP SER-2151, AND IDENTIFICATION BY MASS 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 [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106; LYS-1184; LYS-1389;
RP LYS-1412 AND LYS-1518, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [40]
RP INTERACTION WITH VDR.
RX PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
RA Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
RA Kitanaka S.;
RT "Functional analyses of a novel missense and other mutations of the vitamin
RT D receptor in association with alopecia.";
RL Sci. Rep. 7:5102-5102(2017).
RN [41]
RP STRUCTURE BY NMR OF 433-486.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first SANT domain from human nuclear receptor
RT corepressor 1.";
RL Submitted (APR-2008) to the PDB data bank.
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2047-2065 IN COMPLEX WITH RARA AND
RP RARA AGONIST BMS493, AND INTERACTION WITH RARA.
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).
CC -!- FUNCTION: Mediates transcriptional repression by certain nuclear
CC receptors (PubMed:20812024). Part of a complex which promotes histone
CC deacetylation and the formation of repressive chromatin structures
CC which may impede the access of basal transcription factors.
CC Participates in the transcriptional repressor activity produced by
CC BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on
CC target genes, negatively regulates androgen receptor signaling and
CC androgen-induced cell proliferation (PubMed:20812024). Mediates the
CC NR1D1-dependent repression and circadian regulation of TSHB expression
CC (By similarity). The NCOR1-HDAC3 complex regulates the circadian
CC expression of the core clock gene ARTNL/BMAL1 and the genes involved in
CC lipid metabolism in the liver (By similarity).
CC {ECO:0000250|UniProtKB:Q60974, ECO:0000269|PubMed:14527417,
CC ECO:0000269|PubMed:20812024}.
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 receptor (TR) and the retinoid acid receptor (RAR) in the
CC absence of ligand. Interacts directly with RARA; the interaction is
CC facilitated with RARA trimethylation. Component of the N-Cor repressor
CC complex, at least composed of CBFA2T3, HEXIM1, NCOR1, NCOR2, HDAC3,
CC TBL1X, TBL1XR1, CORO2A and GPS2. Interacts with ZBTB33; the interaction
CC serves to recruit the N-CoR complex to promoter regions containing
CC methylated CpG dinucleotides. Interacts with TRIM28 and KDM3A.
CC Interacts (via the RD1 domain) with BAZ1A (via its N-terminal); the
CC interaction corepresses a number of NCOR1-regulated genes. Interacts
CC with BCL6, C1D, DACH1, HEXIM1, HDAC7, RORA, RORC, SAP30, SIAH2, SIN3A
CC and SIN3B. May interact with DEAF1. Interacts with RXRA. Interacts with
CC SETD5 (By similarity). Interacts with VDR (PubMed:28698609). Interacts
CC with ZBTB7A (PubMed:20812024). Interacts with AR (PubMed:20812024).
CC Interacts with HDAC3 (By similarity). {ECO:0000250|UniProtKB:Q60974,
CC ECO:0000269|PubMed:11013263, ECO:0000269|PubMed:11533236,
CC ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:14525983,
CC ECO:0000269|PubMed:14527417, ECO:0000269|PubMed:15454082,
CC ECO:0000269|PubMed:16024779, ECO:0000269|PubMed:17452463,
CC ECO:0000269|PubMed:17519354, ECO:0000269|PubMed:20543827,
CC ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:23372760,
CC ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:28698609,
CC ECO:0000269|PubMed:9328355}.
CC -!- INTERACTION:
CC O75376; Q9UI36: DACH1; NbExp=2; IntAct=EBI-347233, EBI-347111;
CC O75376; O15379: HDAC3; NbExp=5; IntAct=EBI-347233, EBI-607682;
CC O75376; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-347233, EBI-746704;
CC O75376; P42858: HTT; NbExp=3; IntAct=EBI-347233, EBI-466029;
CC O75376; O00629: KPNA4; NbExp=4; IntAct=EBI-347233, EBI-396343;
CC O75376; I6L9F6: NEFL; NbExp=3; IntAct=EBI-347233, EBI-10178578;
CC O75376; P20393: NR1D1; NbExp=3; IntAct=EBI-347233, EBI-2811738;
CC O75376; P55055: NR1H2; NbExp=6; IntAct=EBI-347233, EBI-745354;
CC O75376; Q13133: NR1H3; NbExp=2; IntAct=EBI-347233, EBI-781356;
CC O75376; Q07869: PPARA; NbExp=3; IntAct=EBI-347233, EBI-78615;
CC O75376; P37231: PPARG; NbExp=2; IntAct=EBI-347233, EBI-781384;
CC O75376; P62937: PPIA; NbExp=3; IntAct=EBI-347233, EBI-437708;
CC O75376; P10276: RARA; NbExp=6; IntAct=EBI-347233, EBI-413374;
CC O75376; Q06455: RUNX1T1; NbExp=5; IntAct=EBI-347233, EBI-743342;
CC O75376; Q99719: SEPTIN5; NbExp=3; IntAct=EBI-347233, EBI-373345;
CC O75376; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-347233, EBI-11522811;
CC O75376; P12755: SKI; NbExp=4; IntAct=EBI-347233, EBI-347281;
CC O75376; P61764: STXBP1; NbExp=3; IntAct=EBI-347233, EBI-960169;
CC O75376; Q13263: TRIM28; NbExp=4; IntAct=EBI-347233, EBI-78139;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75376-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75376-2; Sequence=VSP_010207, VSP_010208;
CC Name=3; Synonyms=b;
CC IsoId=O75376-3; Sequence=VSP_046468, VSP_010207, VSP_046469,
CC VSP_046470;
CC -!- DOMAIN: The N-terminal region contains three independent domains that
CC are capable of mediating transcriptional repression (RD1, RD2 and RD3).
CC -!- DOMAIN: The C-terminal region contains two separate nuclear receptor-
CC interacting domains (ID1 and ID2), each of which contains a conserved
CC sequence referred to as the CORNR box. This motif is necessary and
CC sufficient for binding to unligated nuclear hormone receptors, while
CC sequences flanking the CORNR box determine the precise nuclear hormone
CC receptor specificity (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by SIAH2 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82999.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF044209; AAC33550.1; -; mRNA.
DR EMBL; AF303586; AAO32942.1; -; mRNA.
DR EMBL; AB028970; BAA82999.2; ALT_INIT; mRNA.
DR EMBL; AC002553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471222; EAX04494.1; -; Genomic_DNA.
DR EMBL; BC167431; AAI67431.1; -; mRNA.
DR EMBL; AB019524; BAA75814.1; -; mRNA.
DR CCDS; CCDS11175.1; -. [O75376-1]
DR CCDS; CCDS54094.1; -. [O75376-3]
DR CCDS; CCDS54095.1; -. [O75376-2]
DR RefSeq; NP_001177367.1; NM_001190438.1. [O75376-3]
DR RefSeq; NP_001177369.1; NM_001190440.1. [O75376-2]
DR RefSeq; NP_006302.2; NM_006311.3. [O75376-1]
DR RefSeq; XP_011522388.1; XM_011524086.2. [O75376-2]
DR PDB; 2EQR; NMR; -; A=433-486.
DR PDB; 3H52; X-ray; 2.80 A; M/N=2258-2276.
DR PDB; 3KMZ; X-ray; 2.10 A; C/D=2047-2065.
DR PDB; 3N00; X-ray; 2.60 A; B=2045-2065.
DR PDB; 4MDD; X-ray; 2.40 A; C/D=2260-2274.
DR PDB; 4WVD; X-ray; 2.90 A; C/D=2259-2275.
DR PDB; 6ONI; X-ray; 1.80 A; D=2256-2278.
DR PDB; 6WMQ; X-ray; 2.55 A; E/F=2044-2066.
DR PDB; 6WMS; X-ray; 2.00 A; E/F=2256-2278.
DR PDB; 6XXS; X-ray; 3.25 A; C/D/G/H=1340-1356.
DR PDB; 6XYX; X-ray; 1.44 A; C/D=1340-1356.
DR PDB; 6XZZ; X-ray; 1.39 A; B=1726-1742.
DR PDB; 6Y17; X-ray; 1.56 A; A/B=1733-1741, C/D=1340-1356.
DR PDB; 6ZBU; X-ray; 2.46 A; A/B/E/F/I/J=1733-1741, C/D/G/H/K/L=1340-1356.
DR PDBsum; 2EQR; -.
DR PDBsum; 3H52; -.
DR PDBsum; 3KMZ; -.
DR PDBsum; 3N00; -.
DR PDBsum; 4MDD; -.
DR PDBsum; 4WVD; -.
DR PDBsum; 6ONI; -.
DR PDBsum; 6WMQ; -.
DR PDBsum; 6WMS; -.
DR PDBsum; 6XXS; -.
DR PDBsum; 6XYX; -.
DR PDBsum; 6XZZ; -.
DR PDBsum; 6Y17; -.
DR PDBsum; 6ZBU; -.
DR AlphaFoldDB; O75376; -.
DR SMR; O75376; -.
DR BioGRID; 114973; 284.
DR CORUM; O75376; -.
DR DIP; DIP-29402N; -.
DR ELM; O75376; -.
DR IntAct; O75376; 130.
DR MINT; O75376; -.
DR STRING; 9606.ENSP00000268712; -.
DR BindingDB; O75376; -.
DR ChEMBL; CHEMBL3038484; -.
DR DrugCentral; O75376; -.
DR CarbonylDB; O75376; -.
DR GlyConnect; 2903; 1 O-Linked glycan (1 site).
DR GlyGen; O75376; 35 sites, 2 O-linked glycans (35 sites).
DR iPTMnet; O75376; -.
DR MetOSite; O75376; -.
DR PhosphoSitePlus; O75376; -.
DR SwissPalm; O75376; -.
DR BioMuta; NCOR1; -.
DR EPD; O75376; -.
DR jPOST; O75376; -.
DR MassIVE; O75376; -.
DR MaxQB; O75376; -.
DR PaxDb; O75376; -.
DR PeptideAtlas; O75376; -.
DR PRIDE; O75376; -.
DR ProteomicsDB; 20402; -.
DR ProteomicsDB; 49948; -. [O75376-1]
DR ProteomicsDB; 49949; -. [O75376-2]
DR Antibodypedia; 13188; 451 antibodies from 37 providers.
DR CPTC; O75376; 3 antibodies.
DR DNASU; 9611; -.
DR Ensembl; ENST00000268712.8; ENSP00000268712.2; ENSG00000141027.22. [O75376-1]
DR Ensembl; ENST00000395848.5; ENSP00000379189.1; ENSG00000141027.22. [O75376-3]
DR Ensembl; ENST00000395851.5; ENSP00000379192.1; ENSG00000141027.22. [O75376-2]
DR GeneID; 9611; -.
DR KEGG; hsa:9611; -.
DR MANE-Select; ENST00000268712.8; ENSP00000268712.2; NM_006311.4; NP_006302.2.
DR UCSC; uc002gpn.4; human. [O75376-1]
DR CTD; 9611; -.
DR DisGeNET; 9611; -.
DR GeneCards; NCOR1; -.
DR HGNC; HGNC:7672; NCOR1.
DR HPA; ENSG00000141027; Low tissue specificity.
DR MIM; 600849; gene.
DR neXtProt; NX_O75376; -.
DR OpenTargets; ENSG00000141027; -.
DR PharmGKB; PA31477; -.
DR VEuPathDB; HostDB:ENSG00000141027; -.
DR eggNOG; KOG1878; Eukaryota.
DR GeneTree; ENSGT00940000155093; -.
DR HOGENOM; CLU_000922_0_0_1; -.
DR InParanoid; O75376; -.
DR OMA; SIMQEGT; -.
DR OrthoDB; 12227at2759; -.
DR PhylomeDB; O75376; -.
DR TreeFam; TF106423; -.
DR PathwayCommons; O75376; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-1368071; NR1D1 (REV-ERBA) represses gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
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-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
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 Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; O75376; -.
DR SIGNOR; O75376; -.
DR BioGRID-ORCS; 9611; 57 hits in 1121 CRISPR screens.
DR ChiTaRS; NCOR1; human.
DR EvolutionaryTrace; O75376; -.
DR GeneWiki; Nuclear_receptor_co-repressor_1; -.
DR GenomeRNAi; 9611; -.
DR Pharos; O75376; Tchem.
DR PRO; PR:O75376; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75376; protein.
DR Bgee; ENSG00000141027; Expressed in sural nerve and 195 other tissues.
DR ExpressionAtlas; O75376; baseline and differential.
DR Genevisible; O75376; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; 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:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IMP:BHF-UCL.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IMP:BHF-UCL.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA: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; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR CDD; cd00167; SANT; 2.
DR IDEAL; IID00189; -.
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; Biological rhythms;
KW Chromatin regulator; Coiled coil; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..2440
FT /note="Nuclear receptor corepressor 1"
FT /id="PRO_0000055617"
FT DOMAIN 435..486
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 623..674
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..373
FT /note="Interaction with ZBTB33 and HEXIM1"
FT /evidence="ECO:0000269|PubMed:14527417,
FT ECO:0000269|PubMed:17452463"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..312
FT /note="Interaction with SIN3A/B"
FT REGION 497..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1816
FT /note="Interaction with ETO"
FT REGION 1022..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..2440
FT /note="Interaction with C1D"
FT /evidence="ECO:0000250"
FT REGION 1690..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1884..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1943..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2006..2041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2032..2115
FT /note="ID1"
FT /evidence="ECO:0000250"
FT REGION 2047..2050
FT /note="Required for interaction with RARA in the absence of
FT its ligand"
FT /evidence="ECO:0000250"
FT REGION 2067..2155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2212..2273
FT /note="ID2"
FT /evidence="ECO:0000250"
FT REGION 2287..2440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 174..216
FT /evidence="ECO:0000255"
FT COILED 299..328
FT /evidence="ECO:0000255"
FT COILED 501..557
FT /evidence="ECO:0000255"
FT MOTIF 1933..1937
FT /note="CORNR box 1"
FT MOTIF 2055..2059
FT /note="CORNR box 2"
FT MOTIF 2263..2267
FT /note="CORNR box 3"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1953..1967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2347..2361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60974"
FT MOD_RES 1367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60974"
FT MOD_RES 1412
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB5"
FT MOD_RES 2120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2399
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 2438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 1106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1518
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 37..145
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_046468"
FT VAR_SEQ 727
FT /note="E -> EGAENSSDTESAPSPSP (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_010207"
FT VAR_SEQ 1006..1007
FT /note="VL -> GR (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_046469"
FT VAR_SEQ 1008..2440
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_046470"
FT VAR_SEQ 1842..1961
FT /note="SKHEAARLEENLRSRSAAVSEQQQLEQKTLEVEKRSVQCLYTSSAFPSGKPQ
FT PHSSVVYSEAGKDKGPPPKSRYEEELRTRGKTTITAANFIDVIITRQIASDKDARERGS
FT QSSDSSSSL -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010208"
FT CONFLICT 5
FT /note="G -> V (in Ref. 2; AAO32942)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="Y -> S (in Ref. 2; AAO32942)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="Q -> K (in Ref. 2; AAO32942)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="N -> S (in Ref. 2; AAO32942)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="R -> H (in Ref. 2; AAO32942)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="N -> S (in Ref. 2; AAO32942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="V -> L (in Ref. 1; AAC33550)"
FT /evidence="ECO:0000305"
FT CONFLICT 1508..1509
FT /note="SS -> PP (in Ref. 1; AAC33550)"
FT /evidence="ECO:0000305"
FT CONFLICT 1561
FT /note="R -> W (in Ref. 1; AAC33550)"
FT /evidence="ECO:0000305"
FT CONFLICT 1567
FT /note="H -> Q (in Ref. 1; AAC33550)"
FT /evidence="ECO:0000305"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:2EQR"
FT HELIX 459..465
FT /evidence="ECO:0007829|PDB:2EQR"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:2EQR"
FT STRAND 1343..1346
FT /evidence="ECO:0007829|PDB:6XYX"
FT STRAND 1736..1740
FT /evidence="ECO:0007829|PDB:6XZZ"
FT STRAND 2048..2050
FT /evidence="ECO:0007829|PDB:3KMZ"
FT HELIX 2051..2063
FT /evidence="ECO:0007829|PDB:3KMZ"
FT HELIX 2261..2270
FT /evidence="ECO:0007829|PDB:6ONI"
SQ SEQUENCE 2440 AA; 270210 MW; 1647FE060373A125 CRC64;
MSSSGYPPNQ GAFSTEQSRY PPHSVQYTFP NTRHQQEFAV PDYRSSHLEV SQASQLLQQQ
QQQQLRRRPS LLSEFHPGSD RPQERRTSYE PFHPGPSPVD HDSLESKRPR LEQVSDSHFQ
RVSAAVLPLV HPLPEGLRAS ADAKKDPAFG GKHEAPSSPI SGQPCGDDQN ASPSKLSKEE
LIQSMDRVDR EIAKVEQQIL KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY
DENRKKAEEA HKIFEGLGPK VELPLYNQPS DTKVYHENIK TNQVMRKKLI LFFKRRNHAR
KQREQKICQR YDQLMEAWEK KVDRIENNPR RKAKESKTRE YYEKQFPEIR KQREQQERFQ
RVGQRGAGLS ATIARSEHEI SEIIDGLSEQ ENNEKQMRQL SVIPPMMFDA EQRRVKFINM
NGLMEDPMKV YKDRQFMNVW TDHEKEIFKD KFIQHPKNFG LIASYLERKS VPDCVLYYYL
TKKNENYKAL VRRNYGKRRG RNQQIARPSQ EEKVEEKEED KAEKTEKKEE EKKDEEEKDE
KEDSKENTKE KDKIDGTAEE TEEREQATPR GRKTANSQGR RKGRITRSMT NEAAAASAAA
AAATEEPPPP LPPPPEPIST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI AKMVGTKSEA
QCKNFYFNYK RRHNLDNLLQ QHKQKTSRKP REERDVSQCE SVASTVSAQE DEDIEASNEE
ENPEDSEVEA VKPSEDSPEN ATSRGNTEPA VELEPTTETA PSTSPSLAVP STKPAEDESV
ETQVNDSISA ETAEQMDVDQ QEHSAEEGSV CDPPPATKAD SVDVEVRVPE NHASKVEGDN
TKERDLDRAS EKVEPRDEDL VVAQQINAQR PEPQSDNDSS ATCSADEDVD GEPERQRMFP
MDSKPSLLNP TGSILVSSPL KPNPLDLPQL QHRAAVIPPM VSCTPCNIPI GTPVSGYALY
QRHIKAMHES ALLEEQRQRQ EQIDLECRSS TSPCGTSKSP NREWEVLQPA PHQVITNLPE
GVRLPTTRPT RPPPPLIPSS KTTVASEKPS FIMGGSISQG TPGTYLTSHN QASYTQETPK
PSVGSISLGL PRQQESAKSA TLPYIKQEEF SPRSQNSQPE GLLVRAQHEG VVRGTAGAIQ
EGSITRGTPT SKISVESIPS LRGSITQGTP ALPQTGIPTE ALVKGSISRM PIEDSSPEKG
REEAASKGHV IYEGKSGHIL SYDNIKNARE GTRSPRTAHE ISLKRSYESV EGNIKQGMSM
RESPVSAPLE GLICRALPRG SPHSDLKERT VLSGSIMQGT PRATTESFED GLKYPKQIKR
ESPPIRAFEG AITKGKPYDG ITTIKEMGRS IHEIPRQDIL TQESRKTPEV VQSTRPIIEG
SISQGTPIKF DNNSGQSAIK HNVKSLITGP SKLSRGMPPL EIVPENIKVV ERGKYEDVKA
GETVRSRHTS VVSSGPSVLR STLHEAPKAQ LSPGIYDDTS ARRTPVSYQN TMSRGSPMMN
RTSDVTISSN KSTNHERKST LTPTQRESIP AKSPVPGVDP VVSHSPFDPH HRGSTAGEVY
RSHLPTHLDP AMPFHRALDP AAAAYLFQRQ LSPTPGYPSQ YQLYAMENTR QTILNDYITS
QQMQVNLRPD VARGLSPREQ PLGLPYPATR GIIDLTNMPP TILVPHPGGT STPPMDRITY
IPGTQITFPP RPYNSASMSP GHPTHLAAAA SAERERERER EKERERERIA AASSDLYLRP
GSEQPGRPGS HGYVRSPSPS VRTQETMLQQ RPSVFQGTNG TSVITPLDPT AQLRIMPLPA
GGPSISQGLP ASRYNTAADA LAALVDAAAS APQMDVSKTK ESKHEAARLE ENLRSRSAAV
SEQQQLEQKT LEVEKRSVQC LYTSSAFPSG KPQPHSSVVY SEAGKDKGPP PKSRYEEELR
TRGKTTITAA NFIDVIITRQ IASDKDARER GSQSSDSSSS LSSHRYETPS DAIEVISPAS
SPAPPQEKLQ TYQPEVVKAN QAENDPTRQY EGPLHHYRPQ QESPSPQQQL PPSSQAEGMG
QVPRTHRLIT LADHICQIIT QDFARNQVSS QTPQQPPTST FQNSPSALVS TPVRTKTSNR
YSPESQAQSV HHQRPGSRVS PENLVDKSRG SRPGKSPERS HVSSEPYEPI SPPQVPVVHE
KQDSLLLLSQ RGAEPAEQRN DARSPGSISY LPSFFTKLEN TSPMVKSKKQ EIFRKLNSSG
GGDSDMAAAQ PGTEIFNLPA VTTSGSVSSR GHSFADPASN LGLEDIIRKA LMGSFDDKVE
DHGVVMSQPM GVVPGTANTS VVTSGETRRE EGDPSPHSGG VCKPKLISKS NSRKSKSPIP
GQGYLGTERP SSVSSVHSEG DYHRQTPGWA WEDRPSSTGS TQFPYNPLTM RMLSSTPPTP
IACAPSAVNQ AAPHQQNRIW EREPAPLLSA QYETLSDSDD
