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Nuclear receptor corepressor 1 (N-CoR) (N-CoR1)

 NCOR1_HUMAN             Reviewed;        2440 AA.
O75376; B3DLF8; E9PGV6; Q86YY0; Q9UPV5; Q9UQ18;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
22-NOV-2017, entry version 192.
RecName: Full=Nuclear receptor corepressor 1;
Short=N-CoR;
Short=N-CoR1;
Name=NCOR1; Synonyms=KIAA1047;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=9724795; DOI=10.1073/pnas.95.18.10860;
Wang J., Hoshino T., Redner R.L., Kajigaya S., Liu J.M.;
"ETO, fusion partner in t(8;21) acute myeloid leukemia, represses
transcription by interaction with the human N-CoR/mSin3/HDAC1
complex.";
Proc. Natl. Acad. Sci. U.S.A. 95:10860-10865(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Yu L.;
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[4]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 974-2440 (ISOFORM 1).
PubMed=10444336; DOI=10.1006/geno.1998.5694;
Nagaya T., Chen K.-S., Fujieda M., Ohmori S., Richer J.K.,
Horwitz K.B., Lupski J.R., Seo H.;
"Localization of the human nuclear receptor co-repressor (hN-CoR) gene
between the CMT1A and the SMS critical regions of chromosome
17p11.2.";
Genomics 59:339-341(1999).
[9]
INTERACTION WITH RORA.
PubMed=9328355; DOI=10.1210/mend.11.11.0002;
Harding H.P., Atkins G.B., Jaffe A.B., Seo W.J., Lazar M.A.;
"Transcriptional activation and repression by RORalpha, an orphan
nuclear receptor required for cerebellar development.";
Mol. Endocrinol. 11:1737-1746(1997).
[10]
INTERACTION WITH TRIM28.
PubMed=11013263; DOI=10.1074/jbc.M007864200;
Underhill C., Qutob M.S., Yee S.P., Torchia J.;
"A novel nuclear receptor corepressor complex, N-CoR, contains
components of the mammalian SWI/SNF complex and the corepressor KAP-
1.";
J. Biol. Chem. 275:40463-40470(2000).
[11]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[12]
COMPONENT OF THE N-COR COMPLEX WITH TBL1X; TBL1R; NCOR2; GPS2 AND
HDAC3.
PubMed=11931768; DOI=10.1016/S1097-2765(02)00468-9;
Zhang J., Kalkum M., Chait B.T., Roeder R.G.;
"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK
pathway through the integral subunit GPS2.";
Mol. Cell 9:611-623(2002).
[13]
INTERACTION WITH HDAC9.
PubMed=12590135; DOI=10.1074/jbc.M212935200;
Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
Zelent A.;
"The histone deacetylase 9 gene encodes multiple protein isoforms.";
J. Biol. Chem. 278:16059-16072(2003).
[14]
INTERACTION WITH DACH1.
PubMed=14525983; DOI=10.1074/jbc.M310021200;
Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K.,
Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.;
"DACH1 inhibits transforming growth factor-beta signaling through
binding Smad4.";
J. Biol. Chem. 278:51673-51684(2003).
[15]
FUNCTION, AND INTERACTION WITH CORO2A; GPS2; HDAC3; TBL1R; TBL1X AND
ZBTB33.
PubMed=14527417; DOI=10.1016/j.molcel.2003.08.008;
Yoon H.-G., Chan D.W., Reynolds A.B., Qin J., Wong J.;
"N-CoR mediates DNA methylation-dependent repression through a methyl
CpG binding protein Kaiso.";
Mol. Cell 12:723-734(2003).
[16]
INTERACTION WITH BCL6.
PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R.,
Boss J.M., Wade P.A.;
"MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
differentiation.";
Cell 119:75-86(2004).
[17]
INTERACTION WITH KDM3A.
PubMed=16024779; DOI=10.1128/MCB.25.15.6404-6414.2005;
Zhang D., Yoon H.-G., Wong J.;
"JMJD2A is a novel N-CoR-interacting protein and is involved in
repression of the human transcription factor achaete scute-like
homologue 2 (ASCL2/Hash2).";
Mol. Cell. Biol. 25:6404-6414(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-999 AND
SER-2151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2184, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[20]
INTERACTION WITH HEXIM1.
PubMed=17452463; DOI=10.1128/MCB.00857-06;
Fu J., Yoon H.-G., Qin J., Wong J.;
"Regulation of P-TEFb elongation complex activity by CDK9
acetylation.";
Mol. Cell. Biol. 27:4641-4651(2007).
[21]
INTERACTION WITH BAZ1A.
PubMed=17519354; DOI=10.1210/me.2007-0095;
Ewing A.K., Attner M., Chakravarti D.;
"Novel regulatory role for human Acf1 in transcriptional repression of
vitamin D3 receptor-regulated genes.";
Mol. Endocrinol. 21:1791-1806(2007).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; SER-1472;
SER-1977; SER-1981; SER-2184; THR-2399; SER-2436 AND SER-2438, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-1977;
SER-2151; SER-2184 AND SER-2436, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1412, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-2184 AND
SER-2438, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195; SER-1472;
SER-2151; SER-2436 AND SER-2438, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[31]
INTERACTION WITH BCL6.
PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
"A hybrid mechanism of action for BCL6 in B cells defined by formation
of functionally distinct complexes at enhancers and promoters.";
Cell Rep. 4:578-588(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-224; SER-1111;
SER-1196; SER-1249; SER-1263; SER-1281; SER-1322; SER-1450; SER-1472;
SER-1592; SER-1977; SER-2120; SER-2151 AND SER-2184, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
INTERACTION WITH DEAF1.
PubMed=23372760; DOI=10.1371/journal.pone.0054715;
Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R.,
Bottomley M., Franzmann T.M., Buchner J., Ansieau S., Sattler M.;
"Structural and functional analysis of the DEAF-1 and BS69 MYND
domains.";
PLoS ONE 8:E54715-E54715(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-1472; SER-2136
AND SER-2151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106; LYS-1184; LYS-1389;
LYS-1412 AND LYS-1518, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[39]
INTERACTION WITH VDR.
PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
Kitanaka S.;
"Functional analyses of a novel missense and other mutations of the
vitamin D receptor in association with alopecia.";
Sci. Rep. 7:5102-5102(2017).
[40]
STRUCTURE BY NMR OF 433-486.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first SANT domain from human nuclear
receptor corepressor 1.";
Submitted (APR-2008) to the PDB data bank.
[41]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2047-2065 IN COMPLEX WITH
RARA AND RARA AGONIST BMS493, AND INTERACTION WITH RARA.
PubMed=20543827; DOI=10.1038/nsmb.1855;
le Maire A., Teyssier C., Erb C., Grimaldi M., Alvarez S.,
de Lera A.R., Balaguer P., Gronemeyer H., Royer C.A., Germain P.,
Bourguet W.;
"A unique secondary-structure switch controls constitutive gene
repression by retinoic acid receptor.";
Nat. Struct. Mol. Biol. 17:801-807(2010).
-!- FUNCTION: Mediates transcriptional repression by certain nuclear
receptors. Part of a complex which promotes histone deacetylation
and the formation of repressive chromatin structures which may
impede the access of basal transcription factors. Participates in
the transcriptional repressor activity produced by BCL6.
{ECO:0000269|PubMed:14527417}.
-!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B
and histone deacetylases HDAC1 and HDAC2. This complex associates
with the thyroid receptor (TR) and the retinoid acid receptor
(RAR) in the absence of ligand. Interacts directly with RARA; the
interaction is facilitated with RARA trimethylation. Component of
the N-Cor repressor complex, at least composed of CBFA2T3, HEXIM1,
NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Interacts
with ZBTB33; the interaction serves to recruit the N-CoR complex
to promoter regions containing methylated CpG dinucleotides.
Interacts with TRIM28 and KDM3A. Interacts (via the RD1 domain)
with BAZ1A (via its N-terminal); the interaction corepresses a
number of NCOR1-regulated genes. Interacts with BCL6, C1D, DACH1,
HEXIM1, HDAC7, RORA, RORC, SAP30, SIAH2, SIN3A and SIN3B. May
interact with DEAF1. Interacts with RXRA. Interacts with SETD5 (By
similarity). Interacts with VDR (PubMed:28698609).
{ECO:0000250|UniProtKB:Q60974, ECO:0000269|PubMed:11013263,
ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12590135,
ECO:0000269|PubMed:14525983, ECO:0000269|PubMed:14527417,
ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:16024779,
ECO:0000269|PubMed:17452463, ECO:0000269|PubMed:17519354,
ECO:0000269|PubMed:20543827, ECO:0000269|PubMed:23372760,
ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:28698609,
ECO:0000269|PubMed:9328355}.
-!- INTERACTION:
Q9UI36:DACH1; NbExp=2; IntAct=EBI-347233, EBI-347111;
Q7L2E3:DHX30; NbExp=3; IntAct=EBI-347233, EBI-1211456;
O15379:HDAC3; NbExp=5; IntAct=EBI-347233, EBI-607682;
P42858:HTT; NbExp=3; IntAct=EBI-347233, EBI-466029;
P20393:NR1D1; NbExp=3; IntAct=EBI-347233, EBI-2811738;
P55055:NR1H2; NbExp=6; IntAct=EBI-347233, EBI-745354;
Q13133:NR1H3; NbExp=2; IntAct=EBI-347233, EBI-781356;
Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-347233, EBI-7216962;
Q07869:PPARA; NbExp=3; IntAct=EBI-347233, EBI-78615;
P10276:RARA; NbExp=6; IntAct=EBI-347233, EBI-413374;
Q06455:RUNX1T1; NbExp=5; IntAct=EBI-347233, EBI-743342;
P12755:SKI; NbExp=4; IntAct=EBI-347233, EBI-347281;
Q13263:TRIM28; NbExp=4; IntAct=EBI-347233, EBI-78139;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75376-1; Sequence=Displayed;
Name=2;
IsoId=O75376-2; Sequence=VSP_010207, VSP_010208;
Name=3; Synonyms=b;
IsoId=O75376-3; Sequence=VSP_046468, VSP_010207, VSP_046469,
VSP_046470;
Note=No experimental confirmation available.;
-!- DOMAIN: The N-terminal region contains three independent domains
that are capable of mediating transcriptional repression (RD1, RD2
and RD3).
-!- DOMAIN: The C-terminal region contains two separate nuclear
receptor-interacting domains (ID1 and ID2), each of which contains
a conserved sequence referred to as the CORNR box. This motif is
necessary and sufficient for binding to unligated nuclear hormone
receptors, while sequences flanking the CORNR box determine the
precise nuclear hormone receptor specificity (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated; mediated by SIAH2 and leading to its
subsequent proteasomal degradation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA82999.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF044209; AAC33550.1; -; mRNA.
EMBL; AF303586; AAO32942.1; -; mRNA.
EMBL; AB028970; BAA82999.2; ALT_INIT; mRNA.
EMBL; AC002553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471222; EAX04494.1; -; Genomic_DNA.
EMBL; BC167431; AAI67431.1; -; mRNA.
EMBL; AB019524; BAA75814.1; -; mRNA.
CCDS; CCDS11175.1; -. [O75376-1]
CCDS; CCDS54094.1; -. [O75376-3]
CCDS; CCDS54095.1; -. [O75376-2]
RefSeq; NP_001177367.1; NM_001190438.1. [O75376-3]
RefSeq; NP_001177369.1; NM_001190440.1. [O75376-2]
RefSeq; NP_006302.2; NM_006311.3. [O75376-1]
RefSeq; XP_011522388.1; XM_011524086.2. [O75376-2]
UniGene; Hs.462323; -.
PDB; 2EQR; NMR; -; A=433-486.
PDB; 3H52; X-ray; 2.80 A; M/N=2258-2276.
PDB; 3KMZ; X-ray; 2.10 A; C/D=2047-2065.
PDB; 3N00; X-ray; 2.60 A; B=2045-2065.
PDB; 4MDD; X-ray; 2.40 A; C/D=2260-2274.
PDB; 4WVD; X-ray; 2.90 A; C/D=2259-2275.
PDBsum; 2EQR; -.
PDBsum; 3H52; -.
PDBsum; 3KMZ; -.
PDBsum; 3N00; -.
PDBsum; 4MDD; -.
PDBsum; 4WVD; -.
ProteinModelPortal; O75376; -.
SMR; O75376; -.
BioGrid; 114973; 173.
CORUM; O75376; -.
DIP; DIP-29402N; -.
ELM; O75376; -.
IntAct; O75376; 72.
MINT; MINT-205170; -.
STRING; 9606.ENSP00000268712; -.
BindingDB; O75376; -.
ChEMBL; CHEMBL3038484; -.
iPTMnet; O75376; -.
PhosphoSitePlus; O75376; -.
BioMuta; NCOR1; -.
EPD; O75376; -.
MaxQB; O75376; -.
PaxDb; O75376; -.
PeptideAtlas; O75376; -.
PRIDE; O75376; -.
Ensembl; ENST00000268712; ENSP00000268712; ENSG00000141027. [O75376-1]
Ensembl; ENST00000395848; ENSP00000379189; ENSG00000141027. [O75376-3]
Ensembl; ENST00000395851; ENSP00000379192; ENSG00000141027. [O75376-2]
GeneID; 9611; -.
KEGG; hsa:9611; -.
UCSC; uc002gpn.4; human. [O75376-1]
CTD; 9611; -.
DisGeNET; 9611; -.
EuPathDB; HostDB:ENSG00000141027.20; -.
GeneCards; NCOR1; -.
HGNC; HGNC:7672; NCOR1.
HPA; CAB072830; -.
HPA; HPA043246; -.
HPA; HPA050288; -.
HPA; HPA051168; -.
MIM; 600849; gene.
neXtProt; NX_O75376; -.
OpenTargets; ENSG00000141027; -.
PharmGKB; PA31477; -.
eggNOG; KOG1878; Eukaryota.
eggNOG; ENOG410YDXP; LUCA.
GeneTree; ENSGT00840000129748; -.
HOGENOM; HOG000113746; -.
HOVERGEN; HBG052587; -.
InParanoid; O75376; -.
KO; K04650; -.
OMA; AKMVGTK; -.
OrthoDB; EOG091G0379; -.
PhylomeDB; O75376; -.
TreeFam; TF106423; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1368071; NR1D1 (REV-ERBA) represses gene expression.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SIGNOR; O75376; -.
ChiTaRS; NCOR1; human.
EvolutionaryTrace; O75376; -.
GeneWiki; Nuclear_receptor_co-repressor_1; -.
GenomeRNAi; 9611; -.
PRO; PR:O75376; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141027; -.
CleanEx; HS_NCOR1; -.
ExpressionAtlas; O75376; baseline and differential.
Genevisible; O75376; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IBA:GO_Central.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0046966; F:thyroid hormone receptor binding; IBA:GO_Central.
GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:BHF-UCL.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:2000191; P:regulation of fatty acid transport; IC:BHF-UCL.
GO; GO:0072362; P:regulation of glycolytic process by negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0072368; P:regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
CDD; cd00167; SANT; 2.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR031557; N-CoR_GPS2_interact.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
Pfam; PF15784; GPS2_interact; 1.
Pfam; PF00249; Myb_DNA-binding; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF46689; SSF46689; 2.
PROSITE; PS51293; SANT; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Coiled coil; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 2440 Nuclear receptor corepressor 1.
/FTId=PRO_0000055617.
DOMAIN 435 486 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 623 674 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
REGION 1 373 Interaction with ZBTB33 and HEXIM1.
{ECO:0000269|PubMed:14527417,
ECO:0000269|PubMed:17452463}.
REGION 254 312 Interaction with SIN3A/B.
REGION 988 1816 Interaction with ETO.
REGION 1501 2440 Interaction with C1D. {ECO:0000250}.
REGION 2032 2115 ID1. {ECO:0000250}.
REGION 2047 2050 Required for interaction with RARA in the
absence of its ligand. {ECO:0000250}.
REGION 2212 2273 ID2. {ECO:0000250}.
COILED 174 216 {ECO:0000255}.
COILED 299 328 {ECO:0000255}.
COILED 501 557 {ECO:0000255}.
MOTIF 1933 1937 CORNR box 1.
MOTIF 2055 2059 CORNR box 2.
MOTIF 2263 2267 CORNR box 3.
COMPBIAS 58 64 Poly-Gln.
COMPBIAS 593 603 Poly-Ala.
COMPBIAS 607 617 Pro-rich.
COMPBIAS 1032 1035 Poly-Pro.
COMPBIAS 1707 1712 Poly-Ala.
COMPBIAS 1952 1963 Poly-Ser.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 999 999 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1111 1111 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1195 1195 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1196 1196 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1249 1249 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1263 1263 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1281 1281 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1322 1322 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1336 1336 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q60974}.
MOD_RES 1367 1367 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60974}.
MOD_RES 1412 1412 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1450 1450 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1472 1472 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1592 1592 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1977 1977 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1981 1981 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2102 2102 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WUB5}.
MOD_RES 2120 2120 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2136 2136 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2151 2151 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2184 2184 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2399 2399 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2436 2436 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 2438 2438 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 1106 1106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1106 1106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1184 1184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1389 1389 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1412 1412 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 1518 1518 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 37 145 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_046468.
VAR_SEQ 727 727 E -> EGAENSSDTESAPSPSP (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_010207.
VAR_SEQ 1006 1007 VL -> GR (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_046469.
VAR_SEQ 1008 2440 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_046470.
VAR_SEQ 1842 1961 SKHEAARLEENLRSRSAAVSEQQQLEQKTLEVEKRSVQCLY
TSSAFPSGKPQPHSSVVYSEAGKDKGPPPKSRYEEELRTRG
KTTITAANFIDVIITRQIASDKDARERGSQSSDSSSSL ->
I (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010208.
CONFLICT 5 5 G -> V (in Ref. 2; AAO32942).
{ECO:0000305}.
CONFLICT 20 20 Y -> S (in Ref. 2; AAO32942).
{ECO:0000305}.
CONFLICT 26 26 Q -> K (in Ref. 2; AAO32942).
{ECO:0000305}.
CONFLICT 31 31 N -> S (in Ref. 2; AAO32942).
{ECO:0000305}.
CONFLICT 33 33 R -> H (in Ref. 2; AAO32942).
{ECO:0000305}.
CONFLICT 392 392 N -> S (in Ref. 2; AAO32942).
{ECO:0000305}.
CONFLICT 1014 1014 V -> L (in Ref. 1; AAC33550).
{ECO:0000305}.
CONFLICT 1508 1509 SS -> PP (in Ref. 1; AAC33550).
{ECO:0000305}.
CONFLICT 1561 1561 R -> W (in Ref. 1; AAC33550).
{ECO:0000305}.
CONFLICT 1567 1567 H -> Q (in Ref. 1; AAC33550).
{ECO:0000305}.
HELIX 442 454 {ECO:0000244|PDB:2EQR}.
HELIX 459 465 {ECO:0000244|PDB:2EQR}.
HELIX 471 481 {ECO:0000244|PDB:2EQR}.
STRAND 2048 2050 {ECO:0000244|PDB:3KMZ}.
HELIX 2051 2063 {ECO:0000244|PDB:3KMZ}.
HELIX 2262 2272 {ECO:0000244|PDB:4MDD}.
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


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