Reviewed, UniProtKB/Swiss-Prot O75376 (NCOR1_HUMAN)

Names and origin

Protein names

Recommended name:
    Nuclear receptor corepressor 1
      Short name=N-CoR1
      Short name=N-CoR

Gene names

Name:	NCOR1
Synonyms:	KIAA1047

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.10
Subunit structure	Interacts with SIAH2, HDAC7, SAP30, SIN3A and SIN3B By similarity. Forms a large corepressor complex that contains SIN3A/B and histone deacetylases HDAC1 and HDAC2. This complex associates with the thyroid (TR) and the retinoid acid receptors (RAR) in the absence of ligand. Interacts with DACH1. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Interacts with TRIM28 and MJD2A/JHDM3A. Interacts with ZBTB33/KAISO, and this interaction serves to recruit the N-CoR complex to promoter regions containing methylated CpG dinucleotides. Interacts with the catalytic domain of HDAC9. Interacts with CBFA2T3 and HEXIM1. Interacts with C1D By similarity.
Subcellular location	Nucleus By similarity.
Domain	The N-terminal region contains three independent domains that are capable of mediating transcriptional repression (RD1, RD2 and RD3). 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.
Post-translational modification	Ubiquitinated; mediated by SIAH2 and leading to its subsequent proteasomal degradation By similarity.
Sequence similarities	Belongs to the N-CoR nuclear receptor corepressors family. Contains 2 SANT domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Ligand	DNA-binding
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of specific transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	nucleus Inferred by curator. Source: UniProtKB
Molecular function	transcription corepressor activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DACH1	Q9UI36	2	EBI-347233,EBI-347111
HDAC9	Q9UKV0	1	EBI-347233,EBI-765444
RDBP	P18615	1	EBI-347233,EBI-348444
SKI	P12755	1	EBI-347233,EBI-347281

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75376-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O75376-2)

The sequence of this isoform differs from the canonical sequence as follows:
     727-727: E → EGAENSSDTESAPSPSP
     1842-1961: SKHEAARLEE...SQSSDSSSSL → I

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2440	2440	Nuclear receptor corepressor 1		PRO_0000055617
Regions
	Domain	435 – 486	52	SANT 1
	Domain	623 – 674	52	SANT 2
	Region	1 – 373	373	Interaction with ZBTB33 and HEXIM1
	Region	254 – 312	59	Interaction with SIN3A/B
	Region	988 – 1816	829	Interaction with ETO
	Region	1501 – 2440	940	Interaction with C1D By similarity
	Region	2032 – 2115	84	ID1 By similarity
	Region	2212 – 2273	62	ID2 By similarity
	Coiled coil	174 – 216	43	Potential
	Coiled coil	299 – 328	30	Potential
	Coiled coil	501 – 557	57	Potential
	Motif	1933 – 1937	5	CORNR box 1
	Motif	2055 – 2059	5	CORNR box 2
	Motif	2263 – 2267	5	CORNR box 3
	Compositional bias	58 – 64	7	Poly-Gln
	Compositional bias	593 – 603	11	Poly-Ala
	Compositional bias	607 – 617	11	Pro-rich
	Compositional bias	1032 – 1035	4	Poly-Pro
	Compositional bias	1707 – 1712	6	Poly-Ala
	Compositional bias	1952 – 1963	12	Poly-Ser
Amino acid modifications
	Modified residue	158	1	Phosphoserine Ref.11
	Modified residue	172	1	Phosphoserine Ref.11
	Modified residue	224	1	Phosphoserine Ref.13 Ref.18
	Modified residue	999	1	Phosphoserine Ref.13
	Modified residue	1111	1	Phosphoserine Ref.18
	Modified residue	1450	1	Phosphoserine Ref.16
	Modified residue	1472	1	Phosphoserine Ref.18 Ref.16 Ref.17
	Modified residue	1977	1	Phosphoserine Ref.11 Ref.18
	Modified residue	1981	1	Phosphoserine Ref.18
	Modified residue	2120	1	Phosphoserine Ref.11 Ref.18 Ref.14
	Modified residue	2151	1	Phosphoserine Ref.13
	Modified residue	2184	1	Phosphoserine Ref.11 Ref.18 Ref.14
	Modified residue	2395	1	Phosphoserine Ref.18
	Modified residue	2399	1	Phosphothreonine Ref.18
	Modified residue	2432	1	Phosphotyrosine Ref.13
	Modified residue	2434	1	Phosphothreonine Ref.13
	Modified residue	2436	1	Phosphoserine Ref.13 Ref.18
	Modified residue	2438	1	Phosphoserine Ref.13 Ref.18
Natural variations
	Alternative sequence	727	1	E → EGAENSSDTESAPSPSP in isoform 2.		VSP_010207
	Alternative sequence	1842 – 1961	120	SKHEA…SSSSL → I in isoform 2.		VSP_010208
Experimental info
	Sequence conflict	1014	1	V → L in AAC33550. Ref.1
	Sequence conflict	1508 – 1509	2	SS → PP in AAC33550. Ref.1
	Sequence conflict	1561	1	R → W in AAC33550. Ref.1
	Sequence conflict	1567	1	H → Q in AAC33550. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 1647FE060373A125	FASTA	2,440	270,210
	10 20 30 40 50 60 MSSSGYPPNQ GAFSTEQSRY PPHSVQYTFP NTRHQQEFAV PDYRSSHLEV SQASQLLQQQ 70 80 90 100 110 120 QQQQLRRRPS LLSEFHPGSD RPQERRTSYE PFHPGPSPVD HDSLESKRPR LEQVSDSHFQ 130 140 150 160 170 180 RVSAAVLPLV HPLPEGLRAS ADAKKDPAFG GKHEAPSSPI SGQPCGDDQN ASPSKLSKEE 190 200 210 220 230 240 LIQSMDRVDR EIAKVEQQIL KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY 250 260 270 280 290 300 DENRKKAEEA HKIFEGLGPK VELPLYNQPS DTKVYHENIK TNQVMRKKLI LFFKRRNHAR 310 320 330 340 350 360 KQREQKICQR YDQLMEAWEK KVDRIENNPR RKAKESKTRE YYEKQFPEIR KQREQQERFQ 370 380 390 400 410 420 RVGQRGAGLS ATIARSEHEI SEIIDGLSEQ ENNEKQMRQL SVIPPMMFDA EQRRVKFINM 430 440 450 460 470 480 NGLMEDPMKV YKDRQFMNVW TDHEKEIFKD KFIQHPKNFG LIASYLERKS VPDCVLYYYL 490 500 510 520 530 540 TKKNENYKAL VRRNYGKRRG RNQQIARPSQ EEKVEEKEED KAEKTEKKEE EKKDEEEKDE 550 560 570 580 590 600 KEDSKENTKE KDKIDGTAEE TEEREQATPR GRKTANSQGR RKGRITRSMT NEAAAASAAA 610 620 630 640 650 660 AAATEEPPPP LPPPPEPIST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI AKMVGTKSEA 670 680 690 700 710 720 QCKNFYFNYK RRHNLDNLLQ QHKQKTSRKP REERDVSQCE SVASTVSAQE DEDIEASNEE 730 740 750 760 770 780 ENPEDSEVEA VKPSEDSPEN ATSRGNTEPA VELEPTTETA PSTSPSLAVP STKPAEDESV 790 800 810 820 830 840 ETQVNDSISA ETAEQMDVDQ QEHSAEEGSV CDPPPATKAD SVDVEVRVPE NHASKVEGDN 850 860 870 880 890 900 TKERDLDRAS EKVEPRDEDL VVAQQINAQR PEPQSDNDSS ATCSADEDVD GEPERQRMFP 910 920 930 940 950 960 MDSKPSLLNP TGSILVSSPL KPNPLDLPQL QHRAAVIPPM VSCTPCNIPI GTPVSGYALY 970 980 990 1000 1010 1020 QRHIKAMHES ALLEEQRQRQ EQIDLECRSS TSPCGTSKSP NREWEVLQPA PHQVITNLPE 1030 1040 1050 1060 1070 1080 GVRLPTTRPT RPPPPLIPSS KTTVASEKPS FIMGGSISQG TPGTYLTSHN QASYTQETPK 1090 1100 1110 1120 1130 1140 PSVGSISLGL PRQQESAKSA TLPYIKQEEF SPRSQNSQPE GLLVRAQHEG VVRGTAGAIQ 1150 1160 1170 1180 1190 1200 EGSITRGTPT SKISVESIPS LRGSITQGTP ALPQTGIPTE ALVKGSISRM PIEDSSPEKG 1210 1220 1230 1240 1250 1260 REEAASKGHV IYEGKSGHIL SYDNIKNARE GTRSPRTAHE ISLKRSYESV EGNIKQGMSM 1270 1280 1290 1300 1310 1320 RESPVSAPLE GLICRALPRG SPHSDLKERT VLSGSIMQGT PRATTESFED GLKYPKQIKR 1330 1340 1350 1360 1370 1380 ESPPIRAFEG AITKGKPYDG ITTIKEMGRS IHEIPRQDIL TQESRKTPEV VQSTRPIIEG 1390 1400 1410 1420 1430 1440 SISQGTPIKF DNNSGQSAIK HNVKSLITGP SKLSRGMPPL EIVPENIKVV ERGKYEDVKA 1450 1460 1470 1480 1490 1500 GETVRSRHTS VVSSGPSVLR STLHEAPKAQ LSPGIYDDTS ARRTPVSYQN TMSRGSPMMN 1510 1520 1530 1540 1550 1560 RTSDVTISSN KSTNHERKST LTPTQRESIP AKSPVPGVDP VVSHSPFDPH HRGSTAGEVY 1570 1580 1590 1600 1610 1620 RSHLPTHLDP AMPFHRALDP AAAAYLFQRQ LSPTPGYPSQ YQLYAMENTR QTILNDYITS 1630 1640 1650 1660 1670 1680 QQMQVNLRPD VARGLSPREQ PLGLPYPATR GIIDLTNMPP TILVPHPGGT STPPMDRITY 1690 1700 1710 1720 1730 1740 IPGTQITFPP RPYNSASMSP GHPTHLAAAA SAERERERER EKERERERIA AASSDLYLRP 1750 1760 1770 1780 1790 1800 GSEQPGRPGS HGYVRSPSPS VRTQETMLQQ RPSVFQGTNG TSVITPLDPT AQLRIMPLPA 1810 1820 1830 1840 1850 1860 GGPSISQGLP ASRYNTAADA LAALVDAAAS APQMDVSKTK ESKHEAARLE ENLRSRSAAV 1870 1880 1890 1900 1910 1920 SEQQQLEQKT LEVEKRSVQC LYTSSAFPSG KPQPHSSVVY SEAGKDKGPP PKSRYEEELR 1930 1940 1950 1960 1970 1980 TRGKTTITAA NFIDVIITRQ IASDKDARER GSQSSDSSSS LSSHRYETPS DAIEVISPAS 1990 2000 2010 2020 2030 2040 SPAPPQEKLQ TYQPEVVKAN QAENDPTRQY EGPLHHYRPQ QESPSPQQQL PPSSQAEGMG 2050 2060 2070 2080 2090 2100 QVPRTHRLIT LADHICQIIT QDFARNQVSS QTPQQPPTST FQNSPSALVS TPVRTKTSNR 2110 2120 2130 2140 2150 2160 YSPESQAQSV HHQRPGSRVS PENLVDKSRG SRPGKSPERS HVSSEPYEPI SPPQVPVVHE 2170 2180 2190 2200 2210 2220 KQDSLLLLSQ RGAEPAEQRN DARSPGSISY LPSFFTKLEN TSPMVKSKKQ EIFRKLNSSG 2230 2240 2250 2260 2270 2280 GGDSDMAAAQ PGTEIFNLPA VTTSGSVSSR GHSFADPASN LGLEDIIRKA LMGSFDDKVE 2290 2300 2310 2320 2330 2340 DHGVVMSQPM GVVPGTANTS VVTSGETRRE EGDPSPHSGG VCKPKLISKS NSRKSKSPIP 2350 2360 2370 2380 2390 2400 GQGYLGTERP SSVSSVHSEG DYHRQTPGWA WEDRPSSTGS TQFPYNPLTM RMLSSTPPTP 2410 2420 2430 2440 IACAPSAVNQ AAPHQQNRIW EREPAPLLSA QYETLSDSDD
	Isoform 2. Checksum: 6837EA3886E1E03C	FASTA	2,337	258,602
	10 20 30 40 50 60 MSSSGYPPNQ GAFSTEQSRY PPHSVQYTFP NTRHQQEFAV PDYRSSHLEV SQASQLLQQQ 70 80 90 100 110 120 QQQQLRRRPS LLSEFHPGSD RPQERRTSYE PFHPGPSPVD HDSLESKRPR LEQVSDSHFQ 130 140 150 160 170 180 RVSAAVLPLV HPLPEGLRAS ADAKKDPAFG GKHEAPSSPI SGQPCGDDQN ASPSKLSKEE 190 200 210 220 230 240 LIQSMDRVDR EIAKVEQQIL KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY 250 260 270 280 290 300 DENRKKAEEA HKIFEGLGPK VELPLYNQPS DTKVYHENIK TNQVMRKKLI LFFKRRNHAR 310 320 330 340 350 360 KQREQKICQR YDQLMEAWEK KVDRIENNPR RKAKESKTRE YYEKQFPEIR KQREQQERFQ 370 380 390 400 410 420 RVGQRGAGLS ATIARSEHEI SEIIDGLSEQ ENNEKQMRQL SVIPPMMFDA EQRRVKFINM 430 440 450 460 470 480 NGLMEDPMKV YKDRQFMNVW TDHEKEIFKD KFIQHPKNFG LIASYLERKS VPDCVLYYYL 490 500 510 520 530 540 TKKNENYKAL VRRNYGKRRG RNQQIARPSQ EEKVEEKEED KAEKTEKKEE EKKDEEEKDE 550 560 570 580 590 600 KEDSKENTKE KDKIDGTAEE TEEREQATPR GRKTANSQGR RKGRITRSMT NEAAAASAAA 610 620 630 640 650 660 AAATEEPPPP LPPPPEPIST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI AKMVGTKSEA 670 680 690 700 710 720 QCKNFYFNYK RRHNLDNLLQ QHKQKTSRKP REERDVSQCE SVASTVSAQE DEDIEASNEE 730 740 750 760 770 780 ENPEDSEGAE NSSDTESAPS PSPVEAVKPS EDSPENATSR GNTEPAVELE PTTETAPSTS 790 800 810 820 830 840 PSLAVPSTKP AEDESVETQV NDSISAETAE QMDVDQQEHS AEEGSVCDPP PATKADSVDV 850 860 870 880 890 900 EVRVPENHAS KVEGDNTKER DLDRASEKVE PRDEDLVVAQ QINAQRPEPQ SDNDSSATCS 910 920 930 940 950 960 ADEDVDGEPE RQRMFPMDSK PSLLNPTGSI LVSSPLKPNP LDLPQLQHRA AVIPPMVSCT 970 980 990 1000 1010 1020 PCNIPIGTPV SGYALYQRHI KAMHESALLE EQRQRQEQID LECRSSTSPC GTSKSPNREW 1030 1040 1050 1060 1070 1080 EVLQPAPHQV ITNLPEGVRL PTTRPTRPPP PLIPSSKTTV ASEKPSFIMG GSISQGTPGT 1090 1100 1110 1120 1130 1140 YLTSHNQASY TQETPKPSVG SISLGLPRQQ ESAKSATLPY IKQEEFSPRS QNSQPEGLLV 1150 1160 1170 1180 1190 1200 RAQHEGVVRG TAGAIQEGSI TRGTPTSKIS VESIPSLRGS ITQGTPALPQ TGIPTEALVK 1210 1220 1230 1240 1250 1260 GSISRMPIED SSPEKGREEA ASKGHVIYEG KSGHILSYDN IKNAREGTRS PRTAHEISLK 1270 1280 1290 1300 1310 1320 RSYESVEGNI KQGMSMRESP VSAPLEGLIC RALPRGSPHS DLKERTVLSG SIMQGTPRAT 1330 1340 1350 1360 1370 1380 TESFEDGLKY PKQIKRESPP IRAFEGAITK GKPYDGITTI KEMGRSIHEI PRQDILTQES 1390 1400 1410 1420 1430 1440 RKTPEVVQST RPIIEGSISQ GTPIKFDNNS GQSAIKHNVK SLITGPSKLS RGMPPLEIVP 1450 1460 1470 1480 1490 1500 ENIKVVERGK YEDVKAGETV RSRHTSVVSS GPSVLRSTLH EAPKAQLSPG IYDDTSARRT 1510 1520 1530 1540 1550 1560 PVSYQNTMSR GSPMMNRTSD VTISSNKSTN HERKSTLTPT QRESIPAKSP VPGVDPVVSH 1570 1580 1590 1600 1610 1620 SPFDPHHRGS TAGEVYRSHL PTHLDPAMPF HRALDPAAAA YLFQRQLSPT PGYPSQYQLY 1630 1640 1650 1660 1670 1680 AMENTRQTIL NDYITSQQMQ VNLRPDVARG LSPREQPLGL PYPATRGIID LTNMPPTILV 1690 1700 1710 1720 1730 1740 PHPGGTSTPP MDRITYIPGT QITFPPRPYN SASMSPGHPT HLAAAASAER EREREREKER 1750 1760 1770 1780 1790 1800 ERERIAAASS DLYLRPGSEQ PGRPGSHGYV RSPSPSVRTQ ETMLQQRPSV FQGTNGTSVI 1810 1820 1830 1840 1850 1860 TPLDPTAQLR IMPLPAGGPS ISQGLPASRY NTAADALAAL VDAAASAPQM DVSKTKEISS 1870 1880 1890 1900 1910 1920 HRYETPSDAI EVISPASSPA PPQEKLQTYQ PEVVKANQAE NDPTRQYEGP LHHYRPQQES 1930 1940 1950 1960 1970 1980 PSPQQQLPPS SQAEGMGQVP RTHRLITLAD HICQIITQDF ARNQVSSQTP QQPPTSTFQN 1990 2000 2010 2020 2030 2040 SPSALVSTPV RTKTSNRYSP ESQAQSVHHQ RPGSRVSPEN LVDKSRGSRP GKSPERSHVS 2050 2060 2070 2080 2090 2100 SEPYEPISPP QVPVVHEKQD SLLLLSQRGA EPAEQRNDAR SPGSISYLPS FFTKLENTSP 2110 2120 2130 2140 2150 2160 MVKSKKQEIF RKLNSSGGGD SDMAAAQPGT EIFNLPAVTT SGSVSSRGHS FADPASNLGL 2170 2180 2190 2200 2210 2220 EDIIRKALMG SFDDKVEDHG VVMSQPMGVV PGTANTSVVT SGETRREEGD PSPHSGGVCK 2230 2240 2250 2260 2270 2280 PKLISKSNSR KSKSPIPGQG YLGTERPSSV SSVHSEGDYH RQTPGWAWED RPSSTGSTQF 2290 2300 2310 2320 2330 PYNPLTMRML SSTPPTPIAC APSAVNQAAP HQQNRIWERE PAPLLSAQYE TLSDSDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex." Wang J., Hoshino T., Redner R.L., Kajigaya S., Liu J.M. Proc. Natl. Acad. Sci. U.S.A. 95:10860-10865(1998) [PubMed: 9724795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain.
[2]	"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." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	Ohara O., Nagase T., Kikuno R. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Localization of the human nuclear receptor co-repressor (hN-CoR) gene between the CMT1A and the SMS critical regions of chromosome 17p11.2." Nagaya T., Chen K.-S., Fujieda M., Ohmori S., Richer J.K., Horwitz K.B., Lupski J.R., Seo H. Genomics 59:339-341(1999) [PubMed: 10444336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 974-2440 (ISOFORM 1).
[5]	"A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1." Underhill C., Qutob M.S., Yee S.P., Torchia J. J. Biol. Chem. 275:40463-40470(2000) [PubMed: 11013263] [Abstract] Cited for: INTERACTION WITH TRIM28.
[6]	"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain." Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W. Mol. Cell. Biol. 21:6470-6483(2001) [PubMed: 11533236] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[7]	"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2." Zhang J., Kalkum M., Chait B.T., Roeder R.G. Mol. Cell 9:611-623(2002) [PubMed: 11931768] [Abstract] Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1X; TBL1R; NCOR2; GPS2 AND HDAC3.
[8]	"The histone deacetylase 9 gene encodes multiple protein isoforms." Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M., Zelent A. J. Biol. Chem. 278:16059-16072(2003) [PubMed: 12590135] [Abstract] Cited for: INTERACTION WITH HDAC9.
[9]	"DACH1 inhibits transforming growth factor-beta signaling through binding Smad4." 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. J. Biol. Chem. 278:51673-51684(2003) [PubMed: 14525983] [Abstract] Cited for: INTERACTION WITH DACH1.
[10]	"N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso." Yoon H.-G., Chan D.W., Reynolds A.B., Qin J., Wong J. Mol. Cell 12:723-734(2003) [PubMed: 14527417] [Abstract] Cited for: FUNCTION, INTERACTION WITH CORO2A; GPS2; HDAC3; TBL1R; TBL1X AND ZBTB33.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-172; SER-1977; SER-2120 AND SER-2184, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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)." Zhang D., Yoon H.-G., Wong J. Mol. Cell. Biol. 25:6404-6414(2005) [PubMed: 16024779] [Abstract] Cited for: INTERACTION WITH JMJD2A.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-999; SER-2151; TYR-2432; THR-2434; SER-2436 AND SER-2438, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2120 AND SER-2184, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Regulation of P-TEFb elongation complex activity by CDK9 acetylation." Fu J., Yoon H.-G., Qin J., Wong J. Mol. Cell. Biol. 27:4641-4651(2007) [PubMed: 17452463] [Abstract] Cited for: INTERACTION WITH HEXIM1.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1450 AND SER-1472, MASS SPECTROMETRY.
[17]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, MASS SPECTROMETRY.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-1111; SER-1472; SER-1977; SER-1981; SER-2120; SER-2184; SER-2395; THR-2399; SER-2436 AND SER-2438, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Solution structure of the first SANT domain from human nuclear receptor corepressor 1." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 433-486.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF044209 mRNA. Translation: AAC33550.1.
AB028970 mRNA. Translation: BAA82999.2. Different initiation.
AB019524 mRNA. Translation: BAA75814.1.

IPI

IPI00289344.
IPI00410351.

RefSeq

NP_006302.2.

UniGene

Hs.462323

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EQR	NMR	-	A	433-486	[»]

SMR

O75376. Positions 421-488.

ModBase

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Protein-protein interaction databases

IntAct

O75376. 7 interactions.

PTM databases

PhosphoSite

O75376.

Proteomic databases

PRIDE

O75376.

Genome annotation databases

Ensembl

ENSG00000141027. Homo sapiens. [Contig view]

GeneID

9611.

KEGG

hsa:9611.

Organism-specific databases

GeneCards

GC17M015875.

H-InvDB

HIX0013566.
HIX0040781.
HIX0059694.

HGNC

HGNC:7672. NCOR1.

MIM

600849. gene.

PharmGKB

PA31477.

HUGE

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GenAtlas

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Phylogenomic databases

HOGENOM

O75376.

HOVERGEN

O75376.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O75376.

Bgee

O75376.

CleanEx

HS_NCOR1.

GermOnline

ENSG00000141027. Homo sapiens.

Family and domain databases

InterPro

IPR012287. Homeodomain-rel.
IPR014778. Myb_DNA-bd.
IPR001005. SANT_DNA-bd.
IPR017884. SANT_eukarya.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

Pfam

PF00249. Myb_DNA-binding. 2 hits.
[Graphical view]

SMART

SM00717. SANT. 2 hits.
[Graphical view]

PROSITE

PS51293. SANT. 2 hits.
[Graphical view]

ProtoNet

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Other Resources

NextBio

36055.

SOURCE

Search...

Entry information

Entry name

NCOR1_HUMAN

Accession

Primary (citable) accession number: O75376
Secondary accession number(s): Q9UPV5, Q9UQ18

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 10, 2004
Last modified:	June 16, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)