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O75376

- NCOR1_HUMAN

UniProt

O75376 - NCOR1_HUMAN

Protein

Nuclear receptor corepressor 1

Gene

NCOR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    6. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    7. sequence-specific DNA binding Source: Ensembl
    8. sequence-specific DNA binding transcription factor activity Source: Ensembl
    9. transcription corepressor activity Source: UniProtKB
    10. 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

    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

    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

    ArrayExpressiO75376.
    BgeeiO75376.
    CleanExiHS_NCOR1.
    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. 142 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.
    HOGENOMiHOG000113746.
    HOVERGENiHBG052587.
    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

    MSSSGYPPNQ GAFSTEQSRY PPHSVQYTFP NTRHQQEFAV PDYRSSHLEV     50
    SQASQLLQQQ QQQQLRRRPS LLSEFHPGSD RPQERRTSYE PFHPGPSPVD 100
    HDSLESKRPR LEQVSDSHFQ RVSAAVLPLV HPLPEGLRAS ADAKKDPAFG 150
    GKHEAPSSPI SGQPCGDDQN ASPSKLSKEE LIQSMDRVDR EIAKVEQQIL 200
    KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY DENRKKAEEA 250
    HKIFEGLGPK VELPLYNQPS DTKVYHENIK TNQVMRKKLI LFFKRRNHAR 300
    KQREQKICQR YDQLMEAWEK KVDRIENNPR RKAKESKTRE YYEKQFPEIR 350
    KQREQQERFQ RVGQRGAGLS ATIARSEHEI SEIIDGLSEQ ENNEKQMRQL 400
    SVIPPMMFDA EQRRVKFINM NGLMEDPMKV YKDRQFMNVW TDHEKEIFKD 450
    KFIQHPKNFG LIASYLERKS VPDCVLYYYL TKKNENYKAL VRRNYGKRRG 500
    RNQQIARPSQ EEKVEEKEED KAEKTEKKEE EKKDEEEKDE KEDSKENTKE 550
    KDKIDGTAEE TEEREQATPR GRKTANSQGR RKGRITRSMT NEAAAASAAA 600
    AAATEEPPPP LPPPPEPIST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI 650
    AKMVGTKSEA QCKNFYFNYK RRHNLDNLLQ QHKQKTSRKP REERDVSQCE 700
    SVASTVSAQE DEDIEASNEE ENPEDSEVEA VKPSEDSPEN ATSRGNTEPA 750
    VELEPTTETA PSTSPSLAVP STKPAEDESV ETQVNDSISA ETAEQMDVDQ 800
    QEHSAEEGSV CDPPPATKAD SVDVEVRVPE NHASKVEGDN TKERDLDRAS 850
    EKVEPRDEDL VVAQQINAQR PEPQSDNDSS ATCSADEDVD GEPERQRMFP 900
    MDSKPSLLNP TGSILVSSPL KPNPLDLPQL QHRAAVIPPM VSCTPCNIPI 950
    GTPVSGYALY QRHIKAMHES ALLEEQRQRQ EQIDLECRSS TSPCGTSKSP 1000
    NREWEVLQPA PHQVITNLPE GVRLPTTRPT RPPPPLIPSS KTTVASEKPS 1050
    FIMGGSISQG TPGTYLTSHN QASYTQETPK PSVGSISLGL PRQQESAKSA 1100
    TLPYIKQEEF SPRSQNSQPE GLLVRAQHEG VVRGTAGAIQ EGSITRGTPT 1150
    SKISVESIPS LRGSITQGTP ALPQTGIPTE ALVKGSISRM PIEDSSPEKG 1200
    REEAASKGHV IYEGKSGHIL SYDNIKNARE GTRSPRTAHE ISLKRSYESV 1250
    EGNIKQGMSM RESPVSAPLE GLICRALPRG SPHSDLKERT VLSGSIMQGT 1300
    PRATTESFED GLKYPKQIKR ESPPIRAFEG AITKGKPYDG ITTIKEMGRS 1350
    IHEIPRQDIL TQESRKTPEV VQSTRPIIEG SISQGTPIKF DNNSGQSAIK 1400
    HNVKSLITGP SKLSRGMPPL EIVPENIKVV ERGKYEDVKA GETVRSRHTS 1450
    VVSSGPSVLR STLHEAPKAQ LSPGIYDDTS ARRTPVSYQN TMSRGSPMMN 1500
    RTSDVTISSN KSTNHERKST LTPTQRESIP AKSPVPGVDP VVSHSPFDPH 1550
    HRGSTAGEVY RSHLPTHLDP AMPFHRALDP AAAAYLFQRQ LSPTPGYPSQ 1600
    YQLYAMENTR QTILNDYITS QQMQVNLRPD VARGLSPREQ PLGLPYPATR 1650
    GIIDLTNMPP TILVPHPGGT STPPMDRITY IPGTQITFPP RPYNSASMSP 1700
    GHPTHLAAAA SAERERERER EKERERERIA AASSDLYLRP GSEQPGRPGS 1750
    HGYVRSPSPS VRTQETMLQQ RPSVFQGTNG TSVITPLDPT AQLRIMPLPA 1800
    GGPSISQGLP ASRYNTAADA LAALVDAAAS APQMDVSKTK ESKHEAARLE 1850
    ENLRSRSAAV SEQQQLEQKT LEVEKRSVQC LYTSSAFPSG KPQPHSSVVY 1900
    SEAGKDKGPP PKSRYEEELR TRGKTTITAA NFIDVIITRQ IASDKDARER 1950
    GSQSSDSSSS LSSHRYETPS DAIEVISPAS SPAPPQEKLQ TYQPEVVKAN 2000
    QAENDPTRQY EGPLHHYRPQ QESPSPQQQL PPSSQAEGMG QVPRTHRLIT 2050
    LADHICQIIT QDFARNQVSS QTPQQPPTST FQNSPSALVS TPVRTKTSNR 2100
    YSPESQAQSV HHQRPGSRVS PENLVDKSRG SRPGKSPERS HVSSEPYEPI 2150
    SPPQVPVVHE KQDSLLLLSQ RGAEPAEQRN DARSPGSISY LPSFFTKLEN 2200
    TSPMVKSKKQ EIFRKLNSSG GGDSDMAAAQ PGTEIFNLPA VTTSGSVSSR 2250
    GHSFADPASN LGLEDIIRKA LMGSFDDKVE DHGVVMSQPM GVVPGTANTS 2300
    VVTSGETRRE EGDPSPHSGG VCKPKLISKS NSRKSKSPIP GQGYLGTERP 2350
    SSVSSVHSEG DYHRQTPGWA WEDRPSSTGS TQFPYNPLTM RMLSSTPPTP 2400
    IACAPSAVNQ AAPHQQNRIW EREPAPLLSA QYETLSDSDD 2440
    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. 142 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.
    HOGENOMi HOG000113746.
    HOVERGENi HBG052587.
    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

    ArrayExpressi O75376.
    Bgeei O75376.
    CleanExi HS_NCOR1.
    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

    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 1, 2014
    This is version 156 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