O75376 (NCOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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.
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.12
Subunit structure	Interacts with C1D, 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 directly with RARA; the interaction is faciliated with RARA trimethylation. 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 KDM3A. Interacts with ZBTB33; the interaction serves to recruit the N-CoR complex to promoter regions containing methylated CpG dinucleotides. Interacts with HDAC9 (via its catalytic domain). Interacts with CBFA2T3 and HEXIM1. Interacts (via the RRFD1 domain) with BAZ1A (via its N-terminal); the interaction corepresses a number of NCOR1-regulated genes. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.28
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.
Sequence caution	The sequence BAA82999.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular lipid metabolic process Traceable author statement. Source: Reactome chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of JNK cascade Inferred from direct assay Ref.9. Source: UniProtKB regulation of fatty acid transport Inferred by curator. Source: BHF-UCL regulation of glycolysis by negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL spindle assembly Inferred from mutant phenotype. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	nuclear chromatin Inferred from direct assay. Source: BHF-UCL spindle microtubule Inferred from direct assay. Source: UniProtKB transcriptional repressor complex Inferred from direct assay. Source: UniProtKB
Molecular function	histone deacetylase binding Inferred from physical interaction. Source: BHF-UCL transcription corepressor activity Inferred from mutant phenotype. Source: UniProtKB transcription regulatory region DNA binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DACH1	Q9UI36	2	EBI-347233,EBI-347111
HDAC3	O15379	2	EBI-347233,EBI-607682
TRIM28	Q13263	4	EBI-347233,EBI-78139

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

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

2047 – 2050

4

Required for interaction with RARA in the absence of its ligand 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

157

1

Phosphoserine Ref.22

Modified residue

158

1

Phosphoserine Ref.13 Ref.22

Modified residue

172

1

Phosphoserine Ref.13 Ref.22

Modified residue

224

1

Phosphoserine Ref.15 Ref.21

Modified residue

999

1

Phosphoserine Ref.15

Modified residue

1111

1

Phosphoserine Ref.21

Modified residue

1336

1

N6-acetyllysine Ref.25

Modified residue

1412

1

N6-acetyllysine Ref.25

Modified residue

1450

1

Phosphoserine Ref.19

Modified residue

1472

1

Phosphoserine Ref.19 Ref.20 Ref.21 Ref.22 Ref.24

Modified residue

1476

1

Phosphotyrosine Ref.23

Modified residue

1479

1

Phosphothreonine Ref.23

Modified residue

1977

1

Phosphoserine Ref.13 Ref.21 Ref.24

Modified residue

1981

1

Phosphoserine Ref.21

Modified residue

2102

1

Phosphoserine By similarity

Modified residue

2120

1

Phosphoserine Ref.13 Ref.16 Ref.21

Modified residue

2151

1

Phosphoserine Ref.15 Ref.24

Modified residue

2184

1

Phosphoserine Ref.13 Ref.16 Ref.21 Ref.22 Ref.24

Modified residue

2202

1

Phosphoserine Ref.22

Modified residue

2395

1

Phosphoserine Ref.21

Modified residue

2399

1

Phosphothreonine Ref.21

Modified residue

2432

1

Phosphotyrosine Ref.15

Modified residue

2434

1

Phosphothreonine Ref.15

Modified residue

2436

1

Phosphoserine Ref.15 Ref.21 Ref.24

Modified residue

2438

1

Phosphoserine Ref.15 Ref.21

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

Secondary structure

1

.

.

.

.

.

.

.

2440

Helix Strand Turn

Details...

Helix

442 – 454

13

Helix

462 – 465

4

Helix

471 – 481

11

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 [UniParc]. 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]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"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).
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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: Cervix carcinoma.
[14]	"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 KDM3A.
[15]	"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: Cervix carcinoma.
[16]	"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: Cervix carcinoma.
[17]	"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.
[18]	"Novel regulatory role for human Acf1 in transcriptional repression of vitamin D3 receptor-regulated genes." Ewing A.K., Attner M., Chakravarti D. Mol. Endocrinol. 21:1791-1806(2007) [PubMed: 17519354] [Abstract] Cited for: INTERACTION WITH BAZ1A.
[19]	"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. Tissue: Cervix carcinoma.
[20]	"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. Tissue: Cervix carcinoma.
[21]	"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. Tissue: Cervix carcinoma.
[22]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-158; SER-172; SER-1472; SER-2184 AND SER-2202, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[23]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1476 AND THR-1479, MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-1977; SER-2151; SER-2184 AND SER-2436, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1336 AND LYS-1412, MASS SPECTROMETRY.
[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"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.
[28]	"A unique secondary-structure switch controls constitutive gene repression by retinoic acid receptor." 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. Nat. Struct. Mol. Biol. 17:801-807(2010) [PubMed: 20543827] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2047-2065 IN COMPLEX WITH RARA AND RARA AGONIST BMS493, INTERACTION WITH RARA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF044209 mRNA. Translation: AAC33550.1.
AB028970 mRNA. Translation: BAA82999.2. Different initiation.
CH471222 Genomic DNA. Translation: EAX04494.1.
BC167431 mRNA. Translation: AAI67431.1.
AB019524 mRNA. Translation: BAA75814.1.

IPI

IPI00410351.
IPI00939364.

RefSeq

NP_001177369.1. NM_001190440.1.
NP_006302.2. NM_006311.3.

UniGene

Hs.462323.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EQR	NMR	-	A	433-486	[»]
3H52	X-ray	2.80	M/N	2258-2276	[»]
3KMZ	X-ray	2.10	C/D	2047-2065	[»]
3N00	X-ray	2.60	B	2045-2065	[»]

ProteinModelPortal

O75376.

SMR

O75376. Positions 176-216, 433-486, 624-683.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29402N.

IntAct

O75376. 25 interactions.

MINT

MINT-205170.

STRING

O75376.

PTM databases

PhosphoSite

O75376.

Proteomic databases

PRIDE

O75376.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268712; ENSP00000268712; ENSG00000141027.

GeneID

9611.

KEGG

hsa:9611.

UCSC

uc002gpn.1. human.
uc002gpo.1. human.

Organism-specific databases

CTD

9611.

GeneCards

GC17M015875.

H-InvDB

HIX0040781.

HGNC

HGNC:7672. NCOR1.

MIM

600849. gene.

neXtProt

NX_O75376.

PharmGKB

PA31477.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12496.

HOVERGEN

HBG052587.

OrthoDB

EOG4J6RQ2.

PhylomeDB

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_111045. Developmental Biology.
REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

O75376.

Bgee

O75376.

CleanEx

HS_NCOR1.

Genevestigator

O75376.

GermOnline

ENSG00000141027. Homo sapiens.

Family and domain databases

InterPro

IPR009057. Homeodomain-like.
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.

KO

K04650.

Pfam

PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]

SMART

SM00717. SANT. 2 hits.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51293. SANT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

36055.

SOURCE

Search...

Entry information

Entry name

NCOR1_HUMAN

Accession

Primary (citable) accession number: O75376
Secondary accession number(s): B3DLF8, Q9UPV5, Q9UQ18

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 10, 2004
Last modified:	December 14, 2011
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.