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O75376 (NCOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor corepressor 1
Short name=N-CoR
Short name=N-CoR1
Gene names
Name:NCOR1
Synonyms:KIAA1047
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length2440 AA.
Sequence statusComplete.
Protein existenceEvidence 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.14

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.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.29

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   LigandDNA-binding
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation

Inferred from electronic annotation. Source: Compara

Notch signaling pathway

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cholesterol homeostasis

Inferred from electronic annotation. Source: Compara

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

circadian regulation of gene expression

Inferred from electronic annotation. Source: Compara

definitive erythrocyte differentiation

Inferred from electronic annotation. Source: Compara

negative regulation of JNK cascade

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of phosphatidylinositol 3-kinase cascade

Inferred from electronic annotation. Source: Compara

positive regulation of histone deacetylation

Inferred from electronic annotation. Source: Compara

regulation of fatty acid transport

Inferred by curator PubMed 19955185. Source: BHF-UCL

regulation of glycolysis by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19955185. Source: BHF-UCL

regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19955185. Source: BHF-UCL

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Compara

small molecule metabolic process

Traceable author statement. Source: Reactome

spindle assembly

Inferred from mutant phenotype PubMed 18326024. Source: UniProtKB

thalamus development

Inferred from electronic annotation. Source: Compara

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Compara

nuclear chromatin

Inferred from direct assay PubMed 17505061. Source: BHF-UCL

spindle microtubule

Inferred from direct assay PubMed 18326024. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Compara

transcriptional repressor complex

Inferred from direct assay PubMed 12628926. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: InterPro

histone deacetylase regulator activity

Inferred from electronic annotation. Source: Compara

sequence-specific DNA binding

Inferred from electronic annotation. Source: Compara

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Compara

transcription corepressor activity

Inferred from mutant phenotype PubMed 12628926. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 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
Isoform 3 (identifier: O75376-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24402440Nuclear receptor corepressor 1
PRO_0000055617

Regions

Domain435 – 48652SANT 1
Domain623 – 67452SANT 2
Region1 – 373373Interaction with ZBTB33 and HEXIM1
Region254 – 31259Interaction with SIN3A/B
Region988 – 1816829Interaction with ETO
Region1501 – 2440940Interaction with C1D By similarity
Region2032 – 211584ID1 By similarity
Region2047 – 20504Required for interaction with RARA in the absence of its ligand By similarity
Region2212 – 227362ID2 By similarity
Coiled coil174 – 21643 Potential
Coiled coil299 – 32830 Potential
Coiled coil501 – 55757 Potential
Motif1933 – 19375CORNR box 1
Motif2055 – 20595CORNR box 2
Motif2263 – 22675CORNR box 3
Compositional bias58 – 647Poly-Gln
Compositional bias593 – 60311Poly-Ala
Compositional bias607 – 61711Pro-rich
Compositional bias1032 – 10354Poly-Pro
Compositional bias1707 – 17126Poly-Ala
Compositional bias1952 – 196312Poly-Ser

Amino acid modifications

Modified residue2241Phosphoserine Ref.16
Modified residue9991Phosphoserine Ref.16
Modified residue11111Phosphoserine Ref.22
Modified residue11951Phosphoserine Ref.27
Modified residue14121N6-acetyllysine Ref.24
Modified residue14721Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27
Modified residue19771Phosphoserine Ref.22 Ref.23
Modified residue19811Phosphoserine Ref.22
Modified residue21021Phosphoserine By similarity
Modified residue21511Phosphoserine Ref.16 Ref.23 Ref.27
Modified residue21841Phosphoserine Ref.17 Ref.22 Ref.23 Ref.25
Modified residue23991Phosphothreonine Ref.22
Modified residue24361Phosphoserine Ref.22 Ref.23 Ref.27
Modified residue24381Phosphoserine Ref.22 Ref.25 Ref.27

Natural variations

Alternative sequence37 – 145109Missing in isoform 3.
VSP_046468
Alternative sequence7271E → EGAENSSDTESAPSPSP in isoform 2 and isoform 3.
VSP_010207
Alternative sequence1006 – 10072VL → GR in isoform 3.
VSP_046469
Alternative sequence1008 – 24401433Missing in isoform 3.
VSP_046470
Alternative sequence1842 – 1961120SKHEA…SSSSL → I in isoform 2.
VSP_010208

Experimental info

Sequence conflict51G → V in AAO32942. Ref.2
Sequence conflict201Y → S in AAO32942. Ref.2
Sequence conflict261Q → K in AAO32942. Ref.2
Sequence conflict311N → S in AAO32942. Ref.2
Sequence conflict331R → H in AAO32942. Ref.2
Sequence conflict3921N → S in AAO32942. Ref.2
Sequence conflict10141V → L in AAC33550. Ref.1
Sequence conflict1508 – 15092SS → PP in AAC33550. Ref.1
Sequence conflict15611R → W in AAC33550. Ref.1
Sequence conflict15671H → Q in AAC33550. Ref.1

Secondary structure

1 ............ 2440
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 1647FE060373A125

FASTA2,440270,210
        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

« Hide

Isoform 2 [UniParc].

Checksum: 6837EA3886E1E03C
Show »

FASTA2,337258,602
Isoform 3 (b) [UniParc].

Checksum: 8210E2A279ACD8A8
Show »

FASTA914103,919

References

« Hide '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] [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. expand/collapse author list , 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]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. expand/collapse author list , 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].
[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]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DACH1.
[14]"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.
[15]"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.
[16]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[18]"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.
[19]"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.
[20]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[21]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[22]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; SER-1472; SER-1977; SER-1981; SER-2184; THR-2399; SER-2436 AND SER-2438, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[23]"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, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[24]"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, MASS SPECTROMETRY.
[25]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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, MASS SPECTROMETRY.
[28]"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.
[29]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00410351.
IPI00793060.
IPI00939364.
IPI00978018.
RefSeqNP_001177369.1. NM_001190440.1.
NP_006302.2. NM_006311.3.
UniGeneHs.462323.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQRNMR-A433-486[»]
3H52X-ray2.80M/N2258-2276[»]
3KMZX-ray2.10C/D2047-2065[»]
3N00X-ray2.60B2045-2065[»]
ProteinModelPortalO75376.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29402N.
IntActO75376. 31 interactions.
MINTMINT-205170.
STRING9606.ENSP00000268712.

PTM databases

PhosphoSiteO75376.

Proteomic databases

PaxDbO75376.
PRIDEO75376.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268712; ENSP00000268712; ENSG00000141027.
ENST00000395848; ENSP00000379189; ENSG00000141027.
ENST00000395851; ENSP00000379192; ENSG00000141027.
GeneID9611.
KEGGhsa:9611.
UCSCuc002gpn.3. human.
uc002gpo.3. human.

Organism-specific databases

CTD9611.
GeneCardsGC17M015933.
HGNCHGNC:7672. NCOR1.
HPAHPA050288.
HPA051168.
MIM600849. gene.
neXtProtNX_O75376.
PharmGKBPA31477.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000113746.
HOVERGENHBG052587.
KOK04650.
OMAPPMDRIT.
OrthoDBEOG4J6RQ2.
PhylomeDBO75376.

Enzyme and pathway databases

Pathway_Interaction_DBsmad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_24941. Circadian Clock.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO75376.
BgeeO75376.
CleanExHS_NCOR1.
GenevestigatorO75376.
GermOnlineENSG00000141027. Homo sapiens.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF46689. Homeodomain_like. 2 hits.
PROSITEPS51293. SANT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCOR1. human.
EvolutionaryTraceO75376.
GenomeRNAi9611.
NextBio36055.
SOURCESearch...

Entry information

Entry nameNCOR1_HUMAN
AccessionPrimary (citable) accession number: O75376
Secondary accession number(s): B3DLF8 expand/collapse secondary AC list , E9PGV6, Q86YY0, Q9UPV5, Q9UQ18
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2004
Last modified: May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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