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Protein

Nuclear receptor corepressor 1

Gene

NCOR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 BCL6.1 Publication

GO - Molecular functioni

  • histone deacetylase binding Source: BHF-UCL
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • nuclear hormone receptor binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • thyroid hormone receptor binding Source: GO_Central
  • transcription corepressor activity Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  • cellular lipid metabolic process Source: Reactome
  • chromatin modification Source: UniProtKB-KW
  • circadian rhythm Source: Reactome
  • negative regulation of JNK cascade Source: UniProtKB
  • negative regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of fatty acid transport Source: BHF-UCL
  • regulation of glycolytic process by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • spindle assembly Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141027-MONOMER.
ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-1368071. NR1D1 (REV-ERBA) represses gene expression.
R-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SIGNORiO75376.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor corepressor 1
Short name:
N-CoR
Short name:
N-CoR1
Gene namesi
Name:NCOR1
Synonyms:KIAA1047
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7672. NCOR1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • spindle microtubule Source: UniProtKB
  • transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi9611.
OpenTargetsiENSG00000141027.
PharmGKBiPA31477.

Chemistry databases

ChEMBLiCHEMBL3038484.

Polymorphism and mutation databases

BioMutaiNCOR1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000556171 – 2440Nuclear receptor corepressor 1Add BLAST2440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172PhosphoserineCombined sources1
Modified residuei224PhosphoserineCombined sources1
Modified residuei999PhosphoserineCombined sources1
Cross-linki1106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1111PhosphoserineCombined sources1
Modified residuei1195PhosphoserineCombined sources1
Modified residuei1196PhosphoserineCombined sources1
Modified residuei1249PhosphoserineCombined sources1
Modified residuei1263PhosphoserineCombined sources1
Modified residuei1281PhosphoserineCombined sources1
Modified residuei1322PhosphoserineCombined sources1
Modified residuei1336N6-acetyllysineBy similarity1
Modified residuei1367PhosphothreonineBy similarity1
Modified residuei1412N6-acetyllysineCombined sources1
Modified residuei1450PhosphoserineCombined sources1
Modified residuei1472PhosphoserineCombined sources1
Modified residuei1592PhosphoserineCombined sources1
Modified residuei1977PhosphoserineCombined sources1
Modified residuei1981PhosphoserineCombined sources1
Modified residuei2102PhosphoserineBy similarity1
Modified residuei2120PhosphoserineCombined sources1
Modified residuei2136PhosphoserineCombined sources1
Modified residuei2151PhosphoserineCombined sources1
Modified residuei2184PhosphoserineCombined sources1
Modified residuei2399PhosphothreonineCombined sources1
Modified residuei2436PhosphoserineCombined sources1
Modified residuei2438PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated; mediated by SIAH2 and leading to its subsequent proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75376.
MaxQBiO75376.
PaxDbiO75376.
PeptideAtlasiO75376.
PRIDEiO75376.

PTM databases

iPTMnetiO75376.
PhosphoSitePlusiO75376.

Expressioni

Gene expression databases

BgeeiENSG00000141027.
CleanExiHS_NCOR1.
ExpressionAtlasiO75376. baseline and differential.
GenevisibleiO75376. HS.

Organism-specific databases

HPAiCAB072830.
HPA043246.
HPA050288.
HPA051168.

Interactioni

Subunit structurei

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.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DACH1Q9UI362EBI-347233,EBI-347111
DHX30Q7L2E33EBI-347233,EBI-1211456
HDAC3O153795EBI-347233,EBI-607682
HTTP428583EBI-347233,EBI-466029
NR1H2P550556EBI-347233,EBI-745354
NR1H3Q131332EBI-347233,EBI-781356
NR2E3Q9Y5X42EBI-347233,EBI-7216962
PPARAQ078692EBI-347233,EBI-78615
RARAP102763EBI-347233,EBI-413374
SKIP127554EBI-347233,EBI-347281
TRIM28Q132634EBI-347233,EBI-78139

GO - Molecular functioni

  • histone deacetylase binding Source: BHF-UCL
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • nuclear hormone receptor binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • thyroid hormone receptor binding Source: GO_Central

Protein-protein interaction databases

BioGridi114973. 167 interactors.
DIPiDIP-29402N.
IntActiO75376. 65 interactors.
MINTiMINT-205170.
STRINGi9606.ENSP00000268712.

Chemistry databases

BindingDBiO75376.

Structurei

Secondary structure

12440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi442 – 454Combined sources13
Helixi459 – 465Combined sources7
Helixi471 – 481Combined sources11
Beta strandi2048 – 2050Combined sources3
Helixi2051 – 2063Combined sources13
Helixi2262 – 2272Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EQRNMR-A433-486[»]
3H52X-ray2.80M/N2258-2276[»]
3KMZX-ray2.10C/D2047-2065[»]
3N00X-ray2.60B2045-2065[»]
4MDDX-ray2.40C/D2260-2274[»]
4WVDX-ray2.90C/D2259-2275[»]
ProteinModelPortaliO75376.
SMRiO75376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75376.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini435 – 486SANT 1PROSITE-ProRule annotationAdd BLAST52
Domaini623 – 674SANT 2PROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 373Interaction with ZBTB33 and HEXIM12 PublicationsAdd BLAST373
Regioni254 – 312Interaction with SIN3A/BAdd BLAST59
Regioni988 – 1816Interaction with ETOAdd BLAST829
Regioni1501 – 2440Interaction with C1DBy similarityAdd BLAST940
Regioni2032 – 2115ID1By similarityAdd BLAST84
Regioni2047 – 2050Required for interaction with RARA in the absence of its ligandBy similarity4
Regioni2212 – 2273ID2By similarityAdd BLAST62

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili174 – 216Sequence analysisAdd BLAST43
Coiled coili299 – 328Sequence analysisAdd BLAST30
Coiled coili501 – 557Sequence analysisAdd BLAST57

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1933 – 1937CORNR box 15
Motifi2055 – 2059CORNR box 25
Motifi2263 – 2267CORNR box 35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi58 – 64Poly-Gln7
Compositional biasi593 – 603Poly-AlaAdd BLAST11
Compositional biasi607 – 617Pro-richAdd BLAST11
Compositional biasi1032 – 1035Poly-Pro4
Compositional biasi1707 – 1712Poly-Ala6
Compositional biasi1952 – 1963Poly-SerAdd BLAST12

Domaini

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).By similarity

Sequence similaritiesi

Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1878. Eukaryota.
ENOG410YDXP. LUCA.
GeneTreeiENSGT00840000129748.
HOGENOMiHOG000113746.
HOVERGENiHBG052587.
InParanoidiO75376.
KOiK04650.
OMAiPAMPFHR.
OrthoDBiEOG091G0379.
PhylomeDBiO75376.
TreeFamiTF106423.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR031557. N-CoR_GPS2_interact.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF15784. GPS2_interact. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75376-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSSSGYPPNQ GAFSTEQSRY PPHSVQYTFP NTRHQQEFAV PDYRSSHLEV
60 70 80 90 100
SQASQLLQQQ QQQQLRRRPS LLSEFHPGSD RPQERRTSYE PFHPGPSPVD
110 120 130 140 150
HDSLESKRPR LEQVSDSHFQ RVSAAVLPLV HPLPEGLRAS ADAKKDPAFG
160 170 180 190 200
GKHEAPSSPI SGQPCGDDQN ASPSKLSKEE LIQSMDRVDR EIAKVEQQIL
210 220 230 240 250
KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY DENRKKAEEA
260 270 280 290 300
HKIFEGLGPK VELPLYNQPS DTKVYHENIK TNQVMRKKLI LFFKRRNHAR
310 320 330 340 350
KQREQKICQR YDQLMEAWEK KVDRIENNPR RKAKESKTRE YYEKQFPEIR
360 370 380 390 400
KQREQQERFQ RVGQRGAGLS ATIARSEHEI SEIIDGLSEQ ENNEKQMRQL
410 420 430 440 450
SVIPPMMFDA EQRRVKFINM NGLMEDPMKV YKDRQFMNVW TDHEKEIFKD
460 470 480 490 500
KFIQHPKNFG LIASYLERKS VPDCVLYYYL TKKNENYKAL VRRNYGKRRG
510 520 530 540 550
RNQQIARPSQ EEKVEEKEED KAEKTEKKEE EKKDEEEKDE KEDSKENTKE
560 570 580 590 600
KDKIDGTAEE TEEREQATPR GRKTANSQGR RKGRITRSMT NEAAAASAAA
610 620 630 640 650
AAATEEPPPP LPPPPEPIST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI
660 670 680 690 700
AKMVGTKSEA QCKNFYFNYK RRHNLDNLLQ QHKQKTSRKP REERDVSQCE
710 720 730 740 750
SVASTVSAQE DEDIEASNEE ENPEDSEVEA VKPSEDSPEN ATSRGNTEPA
760 770 780 790 800
VELEPTTETA PSTSPSLAVP STKPAEDESV ETQVNDSISA ETAEQMDVDQ
810 820 830 840 850
QEHSAEEGSV CDPPPATKAD SVDVEVRVPE NHASKVEGDN TKERDLDRAS
860 870 880 890 900
EKVEPRDEDL VVAQQINAQR PEPQSDNDSS ATCSADEDVD GEPERQRMFP
910 920 930 940 950
MDSKPSLLNP TGSILVSSPL KPNPLDLPQL QHRAAVIPPM VSCTPCNIPI
960 970 980 990 1000
GTPVSGYALY QRHIKAMHES ALLEEQRQRQ EQIDLECRSS TSPCGTSKSP
1010 1020 1030 1040 1050
NREWEVLQPA PHQVITNLPE GVRLPTTRPT RPPPPLIPSS KTTVASEKPS
1060 1070 1080 1090 1100
FIMGGSISQG TPGTYLTSHN QASYTQETPK PSVGSISLGL PRQQESAKSA
1110 1120 1130 1140 1150
TLPYIKQEEF SPRSQNSQPE GLLVRAQHEG VVRGTAGAIQ EGSITRGTPT
1160 1170 1180 1190 1200
SKISVESIPS LRGSITQGTP ALPQTGIPTE ALVKGSISRM PIEDSSPEKG
1210 1220 1230 1240 1250
REEAASKGHV IYEGKSGHIL SYDNIKNARE GTRSPRTAHE ISLKRSYESV
1260 1270 1280 1290 1300
EGNIKQGMSM RESPVSAPLE GLICRALPRG SPHSDLKERT VLSGSIMQGT
1310 1320 1330 1340 1350
PRATTESFED GLKYPKQIKR ESPPIRAFEG AITKGKPYDG ITTIKEMGRS
1360 1370 1380 1390 1400
IHEIPRQDIL TQESRKTPEV VQSTRPIIEG SISQGTPIKF DNNSGQSAIK
1410 1420 1430 1440 1450
HNVKSLITGP SKLSRGMPPL EIVPENIKVV ERGKYEDVKA GETVRSRHTS
1460 1470 1480 1490 1500
VVSSGPSVLR STLHEAPKAQ LSPGIYDDTS ARRTPVSYQN TMSRGSPMMN
1510 1520 1530 1540 1550
RTSDVTISSN KSTNHERKST LTPTQRESIP AKSPVPGVDP VVSHSPFDPH
1560 1570 1580 1590 1600
HRGSTAGEVY RSHLPTHLDP AMPFHRALDP AAAAYLFQRQ LSPTPGYPSQ
1610 1620 1630 1640 1650
YQLYAMENTR QTILNDYITS QQMQVNLRPD VARGLSPREQ PLGLPYPATR
1660 1670 1680 1690 1700
GIIDLTNMPP TILVPHPGGT STPPMDRITY IPGTQITFPP RPYNSASMSP
1710 1720 1730 1740 1750
GHPTHLAAAA SAERERERER EKERERERIA AASSDLYLRP GSEQPGRPGS
1760 1770 1780 1790 1800
HGYVRSPSPS VRTQETMLQQ RPSVFQGTNG TSVITPLDPT AQLRIMPLPA
1810 1820 1830 1840 1850
GGPSISQGLP ASRYNTAADA LAALVDAAAS APQMDVSKTK ESKHEAARLE
1860 1870 1880 1890 1900
ENLRSRSAAV SEQQQLEQKT LEVEKRSVQC LYTSSAFPSG KPQPHSSVVY
1910 1920 1930 1940 1950
SEAGKDKGPP PKSRYEEELR TRGKTTITAA NFIDVIITRQ IASDKDARER
1960 1970 1980 1990 2000
GSQSSDSSSS LSSHRYETPS DAIEVISPAS SPAPPQEKLQ TYQPEVVKAN
2010 2020 2030 2040 2050
QAENDPTRQY EGPLHHYRPQ QESPSPQQQL PPSSQAEGMG QVPRTHRLIT
2060 2070 2080 2090 2100
LADHICQIIT QDFARNQVSS QTPQQPPTST FQNSPSALVS TPVRTKTSNR
2110 2120 2130 2140 2150
YSPESQAQSV HHQRPGSRVS PENLVDKSRG SRPGKSPERS HVSSEPYEPI
2160 2170 2180 2190 2200
SPPQVPVVHE KQDSLLLLSQ RGAEPAEQRN DARSPGSISY LPSFFTKLEN
2210 2220 2230 2240 2250
TSPMVKSKKQ EIFRKLNSSG GGDSDMAAAQ PGTEIFNLPA VTTSGSVSSR
2260 2270 2280 2290 2300
GHSFADPASN LGLEDIIRKA LMGSFDDKVE DHGVVMSQPM GVVPGTANTS
2310 2320 2330 2340 2350
VVTSGETRRE EGDPSPHSGG VCKPKLISKS NSRKSKSPIP GQGYLGTERP
2360 2370 2380 2390 2400
SSVSSVHSEG DYHRQTPGWA WEDRPSSTGS TQFPYNPLTM RMLSSTPPTP
2410 2420 2430 2440
IACAPSAVNQ AAPHQQNRIW EREPAPLLSA QYETLSDSDD
Length:2,440
Mass (Da):270,210
Last modified:May 10, 2004 - v2
Checksum:i1647FE060373A125
GO
Isoform 2 (identifier: O75376-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,337
Mass (Da):258,602
Checksum:i6837EA3886E1E03C
GO
Isoform 3 (identifier: O75376-3) [UniParc]FASTAAdd to basket
Also known as: b

The sequence of this isoform differs from the canonical sequence as follows:
     37-145: Missing.
     727-727: E → EGAENSSDTESAPSPSP
     1006-1007: VL → GR
     1008-2440: Missing.

Note: No experimental confirmation available.
Show »
Length:914
Mass (Da):103,919
Checksum:i8210E2A279ACD8A8
GO

Sequence cautioni

The sequence BAA82999 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5G → V in AAO32942 (Ref. 2) Curated1
Sequence conflicti20Y → S in AAO32942 (Ref. 2) Curated1
Sequence conflicti26Q → K in AAO32942 (Ref. 2) Curated1
Sequence conflicti31N → S in AAO32942 (Ref. 2) Curated1
Sequence conflicti33R → H in AAO32942 (Ref. 2) Curated1
Sequence conflicti392N → S in AAO32942 (Ref. 2) Curated1
Sequence conflicti1014V → L in AAC33550 (PubMed:9724795).Curated1
Sequence conflicti1508 – 1509SS → PP in AAC33550 (PubMed:9724795).Curated2
Sequence conflicti1561R → W in AAC33550 (PubMed:9724795).Curated1
Sequence conflicti1567H → Q in AAC33550 (PubMed:9724795).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04646837 – 145Missing in isoform 3. 1 PublicationAdd BLAST109
Alternative sequenceiVSP_010207727E → EGAENSSDTESAPSPSP in isoform 2 and isoform 3. 3 Publications1
Alternative sequenceiVSP_0464691006 – 1007VL → GR in isoform 3. 1 Publication2
Alternative sequenceiVSP_0464701008 – 2440Missing in isoform 3. 1 PublicationAdd BLAST1433
Alternative sequenceiVSP_0102081842 – 1961SKHEA…SSSSL → I in isoform 2. 2 PublicationsAdd BLAST120

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044209 mRNA. Translation: AAC33550.1.
AF303586 mRNA. Translation: AAO32942.1.
AB028970 mRNA. Translation: BAA82999.2. Different initiation.
AC002553 Genomic DNA. No translation available.
AC005971 Genomic DNA. No translation available.
CH471222 Genomic DNA. Translation: EAX04494.1.
BC167431 mRNA. Translation: AAI67431.1.
AB019524 mRNA. Translation: BAA75814.1.
CCDSiCCDS11175.1. [O75376-1]
CCDS54094.1. [O75376-3]
CCDS54095.1. [O75376-2]
RefSeqiNP_001177367.1. NM_001190438.1. [O75376-3]
NP_001177369.1. NM_001190440.1. [O75376-2]
NP_006302.2. NM_006311.3. [O75376-1]
XP_011522388.1. XM_011524086.2. [O75376-2]
UniGeneiHs.462323.

Genome annotation databases

EnsembliENST00000268712; ENSP00000268712; ENSG00000141027. [O75376-1]
ENST00000395848; ENSP00000379189; ENSG00000141027. [O75376-3]
ENST00000395851; ENSP00000379192; ENSG00000141027. [O75376-2]
GeneIDi9611.
KEGGihsa:9611.
UCSCiuc002gpn.4. human. [O75376-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044209 mRNA. Translation: AAC33550.1.
AF303586 mRNA. Translation: AAO32942.1.
AB028970 mRNA. Translation: BAA82999.2. Different initiation.
AC002553 Genomic DNA. No translation available.
AC005971 Genomic DNA. No translation available.
CH471222 Genomic DNA. Translation: EAX04494.1.
BC167431 mRNA. Translation: AAI67431.1.
AB019524 mRNA. Translation: BAA75814.1.
CCDSiCCDS11175.1. [O75376-1]
CCDS54094.1. [O75376-3]
CCDS54095.1. [O75376-2]
RefSeqiNP_001177367.1. NM_001190438.1. [O75376-3]
NP_001177369.1. NM_001190440.1. [O75376-2]
NP_006302.2. NM_006311.3. [O75376-1]
XP_011522388.1. XM_011524086.2. [O75376-2]
UniGeneiHs.462323.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EQRNMR-A433-486[»]
3H52X-ray2.80M/N2258-2276[»]
3KMZX-ray2.10C/D2047-2065[»]
3N00X-ray2.60B2045-2065[»]
4MDDX-ray2.40C/D2260-2274[»]
4WVDX-ray2.90C/D2259-2275[»]
ProteinModelPortaliO75376.
SMRiO75376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114973. 167 interactors.
DIPiDIP-29402N.
IntActiO75376. 65 interactors.
MINTiMINT-205170.
STRINGi9606.ENSP00000268712.

Chemistry databases

BindingDBiO75376.
ChEMBLiCHEMBL3038484.

PTM databases

iPTMnetiO75376.
PhosphoSitePlusiO75376.

Polymorphism and mutation databases

BioMutaiNCOR1.

Proteomic databases

EPDiO75376.
MaxQBiO75376.
PaxDbiO75376.
PeptideAtlasiO75376.
PRIDEiO75376.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268712; ENSP00000268712; ENSG00000141027. [O75376-1]
ENST00000395848; ENSP00000379189; ENSG00000141027. [O75376-3]
ENST00000395851; ENSP00000379192; ENSG00000141027. [O75376-2]
GeneIDi9611.
KEGGihsa:9611.
UCSCiuc002gpn.4. human. [O75376-1]

Organism-specific databases

CTDi9611.
DisGeNETi9611.
GeneCardsiNCOR1.
HGNCiHGNC:7672. NCOR1.
HPAiCAB072830.
HPA043246.
HPA050288.
HPA051168.
MIMi600849. gene.
neXtProtiNX_O75376.
OpenTargetsiENSG00000141027.
PharmGKBiPA31477.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1878. Eukaryota.
ENOG410YDXP. LUCA.
GeneTreeiENSGT00840000129748.
HOGENOMiHOG000113746.
HOVERGENiHBG052587.
InParanoidiO75376.
KOiK04650.
OMAiPAMPFHR.
OrthoDBiEOG091G0379.
PhylomeDBiO75376.
TreeFamiTF106423.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141027-MONOMER.
ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-1368071. NR1D1 (REV-ERBA) represses gene expression.
R-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SIGNORiO75376.

Miscellaneous databases

ChiTaRSiNCOR1. human.
EvolutionaryTraceiO75376.
GeneWikiiNuclear_receptor_co-repressor_1.
GenomeRNAii9611.
PROiO75376.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141027.
CleanExiHS_NCOR1.
ExpressionAtlasiO75376. baseline and differential.
GenevisibleiO75376. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR031557. N-CoR_GPS2_interact.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF15784. GPS2_interact. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCOR1_HUMAN
AccessioniPrimary (citable) accession number: O75376
Secondary accession number(s): B3DLF8
, E9PGV6, Q86YY0, Q9UPV5, Q9UQ18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2004
Last modified: November 30, 2016
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.