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O75376

- NCOR1_HUMAN

UniProt

O75376 - NCOR1_HUMAN

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Protein

Nuclear receptor corepressor 1

Gene

NCOR1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. chromatin binding Source: InterPro
  2. histone deacetylase binding Source: BHF-UCL
  3. histone deacetylase regulator activity Source: Ensembl
  4. nuclear hormone receptor binding Source: UniProtKB
  5. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  6. sequence-specific DNA binding Source: Ensembl
  7. sequence-specific DNA binding transcription factor activity Source: Ensembl
  8. transcription corepressor activity Source: UniProtKB
  9. transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  1. CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: Ensembl
  2. cellular lipid metabolic process Source: Reactome
  3. cholesterol homeostasis Source: Ensembl
  4. chromatin modification Source: UniProtKB-KW
  5. circadian regulation of gene expression Source: Ensembl
  6. definitive erythrocyte differentiation Source: Ensembl
  7. gene expression Source: Reactome
  8. negative regulation of JNK cascade Source: UniProtKB
  9. negative regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  10. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. Notch signaling pathway Source: Reactome
  12. positive regulation of histone deacetylation Source: Ensembl
  13. regulation of fatty acid transport Source: BHF-UCL
  14. regulation of glycolytic process by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  15. regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  16. regulation of multicellular organism growth Source: Ensembl
  17. small molecule metabolic process Source: Reactome
  18. spindle assembly Source: UniProtKB
  19. thalamus development Source: Ensembl
  20. transcription, DNA-templated Source: Reactome
  21. transcription from RNA polymerase II promoter Source: ProtInc
  22. transcription initiation from RNA polymerase II promoter Source: Reactome
  23. transforming growth factor beta receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116022. Nuclear signaling by ERBB4.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7672. NCOR1.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. membrane Source: UniProtKB
  3. nuclear chromatin Source: BHF-UCL
  4. nucleoplasm Source: Reactome
  5. nucleus Source: BHF-UCL
  6. spindle microtubule Source: UniProtKB
  7. transcriptional repressor complex Source: UniProtKB
  8. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31477.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24402440Nuclear receptor corepressor 1PRO_0000055617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei999 – 9991Phosphoserine1 Publication
Modified residuei1111 – 11111Phosphoserine1 Publication
Modified residuei1195 – 11951Phosphoserine1 Publication
Modified residuei1336 – 13361N6-acetyllysineBy similarity
Modified residuei1412 – 14121N6-acetyllysine1 Publication
Modified residuei1472 – 14721Phosphoserine6 Publications
Modified residuei1977 – 19771Phosphoserine2 Publications
Modified residuei1981 – 19811Phosphoserine1 Publication
Modified residuei2151 – 21511Phosphoserine3 Publications
Modified residuei2184 – 21841Phosphoserine4 Publications
Modified residuei2399 – 23991Phosphothreonine1 Publication
Modified residuei2436 – 24361Phosphoserine3 Publications
Modified residuei2438 – 24381Phosphoserine3 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO75376.
PaxDbiO75376.
PRIDEiO75376.

PTM databases

PhosphoSiteiO75376.

Expressioni

Gene expression databases

BgeeiO75376.
CleanExiHS_NCOR1.
ExpressionAtlasiO75376. baseline and differential.
GenevestigatoriO75376.

Organism-specific databases

HPAiHPA050288.
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
HDAC3O153793EBI-347233,EBI-607682
HTTP428583EBI-347233,EBI-466029
NR2E3Q9Y5X42EBI-347233,EBI-7216962
PPARAQ078692EBI-347233,EBI-78615
SKIP127552EBI-347233,EBI-347281
TRIM28Q132634EBI-347233,EBI-78139

Protein-protein interaction databases

BioGridi114973. 145 interactions.
DIPiDIP-29402N.
IntActiO75376. 48 interactions.
MINTiMINT-205170.
STRINGi9606.ENSP00000268712.

Structurei

Secondary structure

1
2440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi442 – 45413
Helixi459 – 4657
Helixi471 – 48111
Beta strandi2048 – 20503
Helixi2051 – 206313
Helixi2263 – 227210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQRNMR-A433-486[»]
3H52X-ray2.80M/N2258-2276[»]
3KMZX-ray2.10C/D2047-2065[»]
3N00X-ray2.60B2045-2065[»]
4II6X-ray2.90C/D2259-2275[»]
ProteinModelPortaliO75376.
SMRiO75376. Positions 176-216, 433-486, 628-694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75376.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini435 – 48652SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini623 – 67452SANT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 373373Interaction with ZBTB33 and HEXIM1Add
BLAST
Regioni254 – 31259Interaction with SIN3A/BAdd
BLAST
Regioni988 – 1816829Interaction with ETOAdd
BLAST
Regioni1501 – 2440940Interaction with C1DBy similarityAdd
BLAST
Regioni2032 – 211584ID1By similarityAdd
BLAST
Regioni2047 – 20504Required for interaction with RARA in the absence of its ligandBy similarity
Regioni2212 – 227362ID2By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili174 – 21643Sequence AnalysisAdd
BLAST
Coiled coili299 – 32830Sequence AnalysisAdd
BLAST
Coiled coili501 – 55757Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1933 – 19375CORNR box 1
Motifi2055 – 20595CORNR box 2
Motifi2263 – 22675CORNR box 3

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 647Poly-Gln
Compositional biasi593 – 60311Poly-AlaAdd
BLAST
Compositional biasi607 – 61711Pro-richAdd
BLAST
Compositional biasi1032 – 10354Poly-Pro
Compositional biasi1707 – 17126Poly-Ala
Compositional biasi1952 – 196312Poly-SerAdd
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00730000110846.
HOGENOMiHOG000113746.
HOVERGENiHBG052587.
InParanoidiO75376.
KOiK04650.
OMAiPIRAFEG.
OrthoDBiEOG75TMB0.
PhylomeDBiO75376.
TreeFamiTF106423.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF00249. 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. Align

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 BAA82999.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51G → V in AAO32942. 1 PublicationCurated
Sequence conflicti20 – 201Y → S in AAO32942. 1 PublicationCurated
Sequence conflicti26 – 261Q → K in AAO32942. 1 PublicationCurated
Sequence conflicti31 – 311N → S in AAO32942. 1 PublicationCurated
Sequence conflicti33 – 331R → H in AAO32942. 1 PublicationCurated
Sequence conflicti392 – 3921N → S in AAO32942. 1 PublicationCurated
Sequence conflicti1014 – 10141V → L in AAC33550. (PubMed:9724795)Curated
Sequence conflicti1508 – 15092SS → PP in AAC33550. (PubMed:9724795)Curated
Sequence conflicti1561 – 15611R → W in AAC33550. (PubMed:9724795)Curated
Sequence conflicti1567 – 15671H → Q in AAC33550. (PubMed:9724795)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 145109Missing in isoform 3. 1 PublicationVSP_046468Add
BLAST
Alternative sequencei727 – 7271E → EGAENSSDTESAPSPSP in isoform 2 and isoform 3. 3 PublicationsVSP_010207
Alternative sequencei1006 – 10072VL → GR in isoform 3. 1 PublicationVSP_046469
Alternative sequencei1008 – 24401433Missing in isoform 3. 1 PublicationVSP_046470Add
BLAST
Alternative sequencei1842 – 1961120SKHEA…SSSSL → I in isoform 2. 2 PublicationsVSP_010208Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.462323.

Genome annotation databases

EnsembliENST00000268712; ENSP00000268712; ENSG00000141027. [O75376-1]
ENST00000395848; ENSP00000379189; ENSG00000141027. [O75376-3]
ENST00000395851; ENSP00000379192; ENSG00000141027. [O75376-2]
GeneIDi9611.
KEGGihsa:9611.
UCSCiuc002gpn.3. human. [O75376-2]
uc002gpo.3. human. [O75376-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11175.1. [O75376-1 ]
CCDS54094.1. [O75376-3 ]
CCDS54095.1. [O75376-2 ]
RefSeqi NP_001177367.1. NM_001190438.1. [O75376-3 ]
NP_001177369.1. NM_001190440.1. [O75376-2 ]
NP_006302.2. NM_006311.3. [O75376-1 ]
UniGenei Hs.462323.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4II6 X-ray 2.90 C/D 2259-2275 [» ]
ProteinModelPortali O75376.
SMRi O75376. Positions 176-216, 433-486, 628-694.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114973. 145 interactions.
DIPi DIP-29402N.
IntActi O75376. 48 interactions.
MINTi MINT-205170.
STRINGi 9606.ENSP00000268712.

Chemistry

ChEMBLi CHEMBL3038484.

PTM databases

PhosphoSitei O75376.

Proteomic databases

MaxQBi O75376.
PaxDbi O75376.
PRIDEi O75376.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268712 ; ENSP00000268712 ; ENSG00000141027 . [O75376-1 ]
ENST00000395848 ; ENSP00000379189 ; ENSG00000141027 . [O75376-3 ]
ENST00000395851 ; ENSP00000379192 ; ENSG00000141027 . [O75376-2 ]
GeneIDi 9611.
KEGGi hsa:9611.
UCSCi uc002gpn.3. human. [O75376-2 ]
uc002gpo.3. human. [O75376-1 ]

Organism-specific databases

CTDi 9611.
GeneCardsi GC17M015933.
HGNCi HGNC:7672. NCOR1.
HPAi HPA050288.
HPA051168.
MIMi 600849. gene.
neXtProti NX_O75376.
PharmGKBi PA31477.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000110846.
HOGENOMi HOG000113746.
HOVERGENi HBG052587.
InParanoidi O75376.
KOi K04650.
OMAi PIRAFEG.
OrthoDBi EOG75TMB0.
PhylomeDBi O75376.
TreeFami TF106423.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116022. Nuclear signaling by ERBB4.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSi NCOR1. human.
EvolutionaryTracei O75376.
GeneWikii Nuclear_receptor_co-repressor_1.
GenomeRNAii 9611.
NextBioi 36055.
PROi O75376.
SOURCEi Search...

Gene expression databases

Bgeei O75376.
CleanExi HS_NCOR1.
ExpressionAtlasi O75376. baseline and differential.
Genevestigatori O75376.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
InterProi IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view ]
Pfami PF00249. Myb_DNA-binding. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 2 hits.
PROSITEi PS51293. SANT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. Yu L.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. Ohara O., Nagase T., Kikuno R.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    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.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  8. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 974-2440 (ISOFORM 1).
  9. "Transcriptional activation and repression by RORalpha, an orphan nuclear receptor required for cerebellar development."
    Harding H.P., Atkins G.B., Jaffe A.B., Seo W.J., Lazar M.A.
    Mol. Endocrinol. 11:1737-1746(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RORA.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM28.
  11. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.
  12. "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] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1X; TBL1R; NCOR2; GPS2 AND HDAC3.
  13. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC9.
  14. Cited for: INTERACTION WITH DACH1.
  15. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CORO2A; GPS2; HDAC3; TBL1R; TBL1X AND ZBTB33.
  16. "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
    Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
    Cell 119:75-86(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL6.
  17. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDM3A.
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-999 AND SER-2151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEXIM1.
  21. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAZ1A.
  22. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; SER-1472; SER-1977; SER-1981; SER-2184; THR-2399; SER-2436 AND SER-2438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-1977; SER-2151; SER-2184 AND SER-2436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1472; SER-2184 AND SER-2438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195; SER-1472; SER-2151; SER-2436 AND SER-2438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. Cited for: INTERACTION WITH BCL6.
  32. Cited for: INTERACTION WITH DEAF1.
  33. "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.
  34. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2047-2065 IN COMPLEX WITH RARA AND RARA AGONIST BMS493, INTERACTION WITH RARA.

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: October 29, 2014
This is version 157 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

External Data

Dasty 3