NCOR1_MOUSE
ID NCOR1_MOUSE Reviewed; 2453 AA.
AC Q60974; Q60812;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Nuclear receptor corepressor 1;
DE Short=N-CoR;
DE Short=N-CoR1;
DE AltName: Full=Retinoid X receptor-interacting protein 13;
DE Short=RIP13;
GN Name=Ncor1; Synonyms=Rxrip13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pituitary;
RX PubMed=7566114; DOI=10.1038/377397a0;
RA Hoerlein A.J., Naeaer A.M., Heinzel T., Torchia J., Gloss B., Kurokawa R.,
RA Ryan A., Kamei Y., Soederstroem M., Glass C.K., Rosenfeld M.G.;
RT "Ligand-independent repression by the thyroid hormone receptor mediated by
RT a nuclear receptor co-repressor.";
RL Nature 377:397-404(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1792-2453 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=7760852; DOI=10.1210/mend.9.1.7760852;
RA Seol W., Choi H.S., Moore D.D.;
RT "Isolation of proteins that interact specifically with the retinoid X
RT receptor: two novel orphan receptors.";
RL Mol. Endocrinol. 9:72-85(1995).
RN [3]
RP INTERACTION WITH RARB; RXRA AND THRB, AND DOMAINS ID1 AND ID2.
RX PubMed=8961273; DOI=10.1210/mend.10.12.8961273;
RA Seol W., Mahon M.J., Lee Y.-K., Moore D.D.;
RT "Two receptor interacting domains in the nuclear hormone receptor
RT corepressor RIP13/N-CoR.";
RL Mol. Endocrinol. 10:1646-1655(1996).
RN [4]
RP INTERACTION WITH SIN3A AND SIN3B.
RX PubMed=9139820; DOI=10.1038/387043a0;
RA Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M., Laherty C.D.,
RA Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E.,
RA Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G.;
RT "A complex containing N-CoR, mSin3 and histone deacetylase mediates
RT transcriptional repression.";
RL Nature 387:43-48(1997).
RN [5]
RP INTERACTION WITH C1D.
RX PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
RA Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.;
RT "Cloning and characterization of a corepressor and potential component of
RT the nuclear hormone receptor repression complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
RN [6]
RP INTERACTION WITH SIAH2, AND DEGRADATION.
RX PubMed=9637679; DOI=10.1101/gad.12.12.1775;
RA Zhang J., Guenther M.G., Carthew R.W., Lazar M.A.;
RT "Proteasomal regulation of nuclear receptor corepressor-mediated
RT repression.";
RL Genes Dev. 12:1775-1780(1998).
RN [7]
RP INTERACTION WITH SAP30 AND SIN3A.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [8]
RP INTERACTION WITH HDAC7.
RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT "Identification of a nuclear domain with deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN [9]
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 [10]
RP INTERACTION WITH DACH1.
RX PubMed=12130660; DOI=10.1126/science.1073263;
RA Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.;
RT "Tissue-specific regulation of retinal and pituitary precursor cell
RT proliferation.";
RL Science 297:1180-1183(2002).
RN [11]
RP INTERACTION WITH RARA.
RX PubMed=17205979; DOI=10.1074/mcp.m600223-mcp200;
RA Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.;
RT "Lysine trimethylation of retinoic acid receptor-alpha: a novel means to
RT regulate receptor function.";
RL Mol. Cell. Proteomics 6:677-688(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1481; SER-2449 AND SER-2451,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP FUNCTION, INTERACTION WITH HDAC3, AND MUTAGENESIS OF TYR-478.
RX PubMed=19037247; DOI=10.1038/nature07541;
RA Alenghat T., Meyers K., Mullican S.E., Leitner K., Adeniji-Adele A.,
RA Avila J., Bucan M., Ahima R.S., Kaestner K.H., Lazar M.A.;
RT "Nuclear receptor corepressor and histone deacetylase 3 govern circadian
RT metabolic physiology.";
RL Nature 456:997-1000(2008).
RN [14]
RP INTERACTION WITH RARA.
RX PubMed=19078967; DOI=10.1038/emboj.2008.256;
RA Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H.,
RA Rochette-Egly C.;
RT "A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs
RT RARalpha to target promoters.";
RL EMBO J. 28:34-47(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-1481, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011; SER-1122; THR-1378;
RP SER-1459; SER-1481; SER-1993 AND SER-2198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP INTERACTION WITH RORA AND RORC.
RX PubMed=21499262; DOI=10.1038/nature10075;
RA Solt L.A., Kumar N., Nuhant P., Wang Y., Lauer J.L., Liu J., Istrate M.A.,
RA Kamenecka T.M., Roush W.R., Vidovic D., Schuerer S.C., Xu J., Wagoner G.,
RA Drew P.D., Griffin P.R., Burris T.P.;
RT "Suppression of TH17 differentiation and autoimmunity by a synthetic ROR
RT ligand.";
RL Nature 472:491-494(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1347, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [21]
RP FUNCTION.
RX PubMed=24794873; DOI=10.1074/jbc.m114.569723;
RA Aninye I.O., Matsumoto S., Sidhaye A.R., Wondisford F.E.;
RT "Circadian regulation of Tshb gene expression by Rev-Erbalpha (NR1D1) and
RT nuclear corepressor 1 (NCOR1).";
RL J. Biol. Chem. 289:17070-17077(2014).
RN [22]
RP INTERACTION WITH SETD5.
RX PubMed=27864380; DOI=10.1242/dev.141465;
RA Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
RT "Setd5 is essential for mammalian development and the co-transcriptional
RT regulation of histone acetylation.";
RL Development 143:4595-4607(2016).
CC -!- FUNCTION: Mediates transcriptional repression by certain nuclear
CC receptors. Part of a complex which promotes histone deacetylation and
CC the formation of repressive chromatin structures which may impede the
CC access of basal transcription factors. Participates in the
CC transcriptional repressor activity produced by BCL6. Recruited by
CC ZBTB7A to the androgen response elements/ARE on target genes,
CC negatively regulates androgen receptor signaling and androgen-induced
CC cell proliferation (By similarity). Mediates the NR1D1-dependent
CC repression and circadian regulation of TSHB expression
CC (PubMed:24794873). 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 (PubMed:19037247).
CC {ECO:0000250|UniProtKB:O75376, ECO:0000269|PubMed:19037247,
CC ECO:0000269|PubMed:24794873}.
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 (PubMed:10984530). May interact with DEAF1. Interacts with
CC RXRA. Interacts with SETD5 (PubMed:27864380). Interacts with VDR (By
CC similarity). Interacts with ZBTB7A (By similarity). Interacts with AR
CC (By similarity). Interacts with HDAC3 (PubMed:19037247).
CC {ECO:0000250|UniProtKB:O75376, ECO:0000269|PubMed:10984530,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12130660,
CC ECO:0000269|PubMed:17205979, ECO:0000269|PubMed:19037247,
CC ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:19786558,
CC ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:27864380,
CC ECO:0000269|PubMed:8961273, ECO:0000269|PubMed:9139820,
CC ECO:0000269|PubMed:9405624, ECO:0000269|PubMed:9637679,
CC ECO:0000269|PubMed:9702189}.
CC -!- INTERACTION:
CC Q60974; Q01147: Creb1; NbExp=4; IntAct=EBI-349004, EBI-2291098;
CC Q60974; Q9QYB2: Dach1; NbExp=2; IntAct=EBI-349004, EBI-348961;
CC Q60974; O88574: Sap30; NbExp=3; IntAct=EBI-349004, EBI-593511;
CC Q60974; Q923E4: Sirt1; NbExp=3; IntAct=EBI-349004, EBI-1802585;
CC Q60974; P03372: ESR1; Xeno; NbExp=2; IntAct=EBI-349004, EBI-78473;
CC Q60974; Q92731: ESR2; Xeno; NbExp=6; IntAct=EBI-349004, EBI-78505;
CC Q60974; O15379: HDAC3; Xeno; NbExp=2; IntAct=EBI-349004, EBI-607682;
CC Q60974; Q9UKV0-3: HDAC9; Xeno; NbExp=2; IntAct=EBI-349004, EBI-765476;
CC Q60974; Q9UKV0-7: HDAC9; Xeno; NbExp=3; IntAct=EBI-349004, EBI-1372717;
CC Q60974; P51608: MECP2; Xeno; NbExp=4; IntAct=EBI-349004, EBI-1189067;
CC Q60974; Q96EB6: SIRT1; Xeno; NbExp=2; IntAct=EBI-349004, EBI-1802965;
CC Q60974; P12755: SKI; Xeno; NbExp=5; IntAct=EBI-349004, EBI-347281;
CC Q60974; P12757: SKIL; Xeno; NbExp=2; IntAct=EBI-349004, EBI-2902468;
CC Q60974; Q13573: SNW1; Xeno; NbExp=3; IntAct=EBI-349004, EBI-632715;
CC Q60974; P10828: THRB; Xeno; NbExp=2; IntAct=EBI-349004, EBI-78558;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60974-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60974-2; Sequence=VSP_003411;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The N-terminal region contains three independent domains that
CC are capable of mediating transcriptional repression (RD1, RD2 and RD3).
CC {ECO:0000269|PubMed:8961273}.
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. {ECO:0000269|PubMed:8961273}.
CC -!- PTM: Ubiquitinated; mediated by SIAH2 and leading to its subsequent
CC proteasomal degradation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC {ECO:0000305}.
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DR EMBL; U35312; AAB17125.1; -; mRNA.
DR EMBL; U22016; AAC52168.1; -; mRNA.
DR PIR; S60254; S60254.
DR AlphaFoldDB; Q60974; -.
DR SASBDB; Q60974; -.
DR SMR; Q60974; -.
DR CORUM; Q60974; -.
DR DIP; DIP-32548N; -.
DR IntAct; Q60974; 29.
DR MINT; Q60974; -.
DR STRING; 10090.ENSMUSP00000068974; -.
DR iPTMnet; Q60974; -.
DR PhosphoSitePlus; Q60974; -.
DR EPD; Q60974; -.
DR jPOST; Q60974; -.
DR MaxQB; Q60974; -.
DR PaxDb; Q60974; -.
DR PeptideAtlas; Q60974; -.
DR PRIDE; Q60974; -.
DR ProteomicsDB; 287458; -. [Q60974-1]
DR ProteomicsDB; 287459; -. [Q60974-2]
DR MGI; MGI:1349717; Ncor1.
DR eggNOG; KOG1878; Eukaryota.
DR InParanoid; Q60974; -.
DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-MMU-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR ChiTaRS; Ncor1; mouse.
DR PRO; PR:Q60974; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60974; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0035033; F:histone deacetylase regulator activity; IDA:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IGI:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IGI:MGI.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IGI:MGI.
DR GO; GO:0061436; P:establishment of skin barrier; IGI:MGI.
DR GO; GO:0010467; P:gene expression; IGI:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; ISO:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IGI:MGI.
DR GO; GO:1901725; P:regulation of histone deacetylase activity; IGI:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0051225; P:spindle assembly; ISO:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0021794; P:thalamus development; IMP:MGI.
DR CDD; cd00167; SANT; 2.
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 Acetylation; Alternative splicing; Biological rhythms; Chromatin regulator;
KW Coiled coil; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..2453
FT /note="Nuclear receptor corepressor 1"
FT /id="PRO_0000055618"
FT DOMAIN 435..486
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 622..673
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:0000250"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..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..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..2453
FT /note="Interaction with C1D"
FT /evidence="ECO:0000269|PubMed:9405624"
FT REGION 1697..1780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2129
FT /note="ID1"
FT REGION 2065..2068
FT /note="Required for interaction with RARA in the absence of
FT its ligand"
FT /evidence="ECO:0000250"
FT REGION 2088..2174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2226..2287
FT /note="ID2"
FT REGION 2303..2396
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..550
FT /evidence="ECO:0000255"
FT MOTIF 1949..1953
FT /note="CORNR box 1"
FT MOTIF 2073..2077
FT /note="CORNR box 2"
FT MOTIF 2277..2281
FT /note="CORNR box 3"
FT COMPBIAS 1..33
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 571..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..730
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1923..1939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2088..2127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2142..2156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2344..2374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1347
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1378
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1423
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 1993
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1997
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 2116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB5"
FT MOD_RES 2134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 2150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 2165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 2198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT MOD_RES 2449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 2451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CROSSLNK 1117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT CROSSLNK 1117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT CROSSLNK 1195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT CROSSLNK 1400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT CROSSLNK 1423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT CROSSLNK 1525
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75376"
FT VAR_SEQ 2333..2371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7566114"
FT /id="VSP_003411"
FT MUTAGEN 478
FT /note="Y->A: In DADm mutant; loss of ability to interact
FT with HDAC3 which causes aberrant regulation of clock genes
FT and results in abnormal circadian behavior. Mice are also
FT leaner and more insulin sensitive due to increased energy
FT expenditure and exhibit dramatic alterations in cyclic
FT expression of several critical genes involved in lipid
FT metabolism in the liver."
FT /evidence="ECO:0000269|PubMed:19037247"
FT CONFLICT 1952
FT /note="I -> T (in Ref. 2; AAC52168)"
FT /evidence="ECO:0000305"
FT CONFLICT 2090
FT /note="A -> P (in Ref. 2; AAC52168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2453 AA; 270642 MW; 52208B40382F7E6A CRC64;
MSSSGYPPNQ GAFSTEQSRY PSHSVQYTFP SARHQQEFAV PDYRSSHLEV SQASQLLQQQ
QQQQLRRRPS LLSEFHPGSD RPQERRSGYE QFHPGPSPVD HDSLESKRPR LEQVSDSHFQ
RISAAVLPLV HTLPEGLRSS ANAKKDPAFG VKHEAPSSPL 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 EKKDDEEKDD
KEDSKETTKE KDRTEATAEE PEEREQVTPR GRKTANSQGR GKGRVTRSMT SEAAAANAAA
AATEEPPPPL PPPPEPISTE PVETSRWTEE EMEVAKKGLV EHGRNWAAIA KMVGTKSEAQ
CKNFYFNYKR RHNLDNLLQQ HKQKASRKPR EERDVSQCES VASTVSAQED EDIEASNEEE
NPEDSEGAEN SSDTESAPSP SPVEAAKSSE DSSENAASRG NTEPVAELEA TTDPAPCASP
SSAVPTTKPA ERESVEAQVT DSASAETAEP MDVDHEECGA EGSSVLDPPA PTKADSVDPE
MQVPENTASK GEGDAKERDL ESTSEKTEAR DEDVVVAEQI ERPEPQSDDD SSATCSADEG
VDGEPERQRV FPMDAKPSLL TPPGSILISS PIKPNLLDLP QLQHRAAVIP PMVSCTPCNI
PIGTPVSGYA LYQRHIKAMH ESALLEEQRQ RQEQVDLECR SSTSPCSTSK SPNREWEVLQ
PAPHQVITNL PEGVRLPTTR PTRPPPPLIP SSKTTVASEK PSFIMGGSIS QGTPGTYLSS
HNQAYPQEAP KPSVGSISLG LPRQQESTKA APLTYIKQEE FSPRSQNSQP EGLLVRAQHE
GVVRGTAGAV QEGSITRGTP ASKISVETIS SLRGSITQGT PALPQAGIPT EALVKGPVSR
MPIEESSPEK VREEAASKGH VIYEGKSGHI LSYDNIKNAR EGTRSPRTAH EMSLKRSYEA
VEGSIKQGMS MRESPVSAPL EGLICRALPR GSPHSDLKER TVLSGSIMQG TPRATAESFE
DGLKYPKQIK RESPPIRAFE GAITKGKPYD GITTIKEMGR SIHEIPRQDI LTQESRKTPE
VVQSTRPIIE GSISQGTPIK FDNNSGQSAI KHNVKSLITG PSKLPRGMLE IVPENIKVVE
RGKYEDVKAG EPVRARHTSV VSSGPSVLRS TLHEAPKAQL SPGLYDDSSA RRTPVSYQNT
ISRGSPMMNR TSDVSSSKSA SHERKSTLTP TQRESIPAKS PVPGVDPIVS HSPFDPHHRS
SAAGEVYRSH LPTHLDPAMP FHRALDPAAA YLLQRQLSPT PGYPSQYQLY AMENTRQTIL
NDYITSQQMQ VNLRPDVTRG LSPREQPLGL PYPATRGIID LTNMPPTILV PHAGGTSTPP
MDRITYIPGT QVTFPPRPYN AASLSPGHPT HLAAAASAER EREREREKER ERERERERER
ERERIAAAPA DLYLRPGSEQ PGRPGSHGYV RSPSPSVRTQ ETILQQRPSV FQGTNGTSVI
TPLDPTAQLR IMPLPSGGPS ISQGLPASRY NTAADALAAL VDAAASAPQM DVSKTKESKH
EAARLEENLR SRSAAVSEQQ QLEQKNLEVE KRSVQCVCTS SALPSGKAQP HASVVYSEAG
KDKGPPPKSR YEEELRTRGK TTITAANFID VIITRQIASD KDARERGSQS SDSSSSLSSH
RYETASDAIE VISPASSPAP PQEKPQAYQP DMVKANQAEN ESTRQYEGPL HHYRSQQESP
SPQQQPPLPP SSQSEGMGQV PRTHRLITLA DHICQIITQD FARNQVPSQA STSTFQTSPS
ALSSTPVRTK TSSRYSPESQ SQTVLHPRPG PRVSPENLVD KSRGSRPGKS PERSHIPSEP
YEPISPPQGP AVHEKQDSML LLSQRGVDPA EQRSDSRSPG SISYLPSFFT KLESTSPMVK
SKKQEIFRKL NSSGGGDSDM AAAQPGTEIF NLPAVTTSGA VSSRSHSFAD PASNLGLEDI
IRKALMGSFD DKVEDHGVVM SHPVGIMPGS ASTSVVTSSE ARRDEGEPSP HAGVCKPKLI
NKSNSRKSKS PIPGQSYLGT ERPSSVSSVH SEGDYHRQTP GWAWEDRPSS TGSTQFPYNP
LTIRMLSSTP PTQIACAPSA ITQAAPHQQN RIWEREPAPL LSAQYETLSD SDD
