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Protein

Nuclear receptor corepressor 1

Gene

Ncor1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates transcriptional repression by certain nuclear receptors. Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6.

GO - Molecular functioni

  • DNA binding Source: MGI
  • histone deacetylase binding Source: MGI
  • histone deacetylase regulator activity Source: MGI
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • nuclear hormone receptor binding Source: MGI
  • protein domain specific binding Source: BHF-UCL
  • retinoic acid receptor binding Source: MGI
  • retinoid X receptor binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: MGI
  • sequence-specific DNA binding Source: MGI
  • thyroid hormone receptor binding Source: MGI
  • transcription corepressor activity Source: MGI
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  • CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: MGI
  • cellular response to Thyroglobulin triiodothyronine Source: MGI
  • cholesterol homeostasis Source: MGI
  • chromatin modification Source: UniProtKB-KW
  • circadian regulation of gene expression Source: MGI
  • circadian rhythm Source: Reactome
  • definitive erythrocyte differentiation Source: MGI
  • negative regulation of JNK cascade Source: MGI
  • negative regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • negative regulation of production of miRNAs involved in gene silencing by miRNA Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of histone deacetylation Source: MGI
  • regulation of glycolytic process by negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • regulation of thyroid hormone mediated signaling pathway Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • spindle assembly Source: MGI
  • thalamus development Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1368071. NR1D1 (REV-ERBA) represses gene expression.
R-MMU-1368082. RORA activates gene expression.
R-MMU-1368092. Rora activates gene expression.
R-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-400253. Circadian Clock.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-5667092. Nr1d1 (Rev-erba) represses gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor corepressor 1
Short name:
N-CoR
Short name:
N-CoR1
Alternative name(s):
Retinoid X receptor-interacting protein 13
Short name:
RIP13
Gene namesi
Name:Ncor1
Synonyms:Rxrip13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1349717. Ncor1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • membrane Source: MGI
  • nuclear chromatin Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • Sin3 complex Source: GO_Central
  • spindle microtubule Source: MGI
  • transcriptional repressor complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24532453Nuclear receptor corepressor 1PRO_0000055618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei224 – 2241PhosphoserineCombined sources
Modified residuei1011 – 10111PhosphoserineCombined sources
Cross-linki1117 – 1117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1117 – 1117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1122 – 11221PhosphoserineCombined sources
Modified residuei1206 – 12061PhosphoserineBy similarity
Modified residuei1207 – 12071PhosphoserineBy similarity
Modified residuei1274 – 12741PhosphoserineBy similarity
Modified residuei1292 – 12921PhosphoserineBy similarity
Modified residuei1333 – 13331PhosphoserineBy similarity
Modified residuei1347 – 13471N6-acetyllysineCombined sources
Modified residuei1378 – 13781PhosphothreonineCombined sources
Modified residuei1423 – 14231N6-acetyllysineBy similarity
Modified residuei1459 – 14591PhosphoserineCombined sources
Modified residuei1481 – 14811PhosphoserineCombined sources
Modified residuei1598 – 15981PhosphoserineBy similarity
Modified residuei1993 – 19931PhosphoserineCombined sources
Modified residuei1997 – 19971PhosphoserineBy similarity
Modified residuei2116 – 21161PhosphoserineBy similarity
Modified residuei2134 – 21341PhosphoserineBy similarity
Modified residuei2150 – 21501PhosphoserineBy similarity
Modified residuei2165 – 21651PhosphoserineBy similarity
Modified residuei2198 – 21981PhosphoserineCombined sources
Modified residuei2412 – 24121PhosphothreonineBy similarity
Modified residuei2449 – 24491PhosphoserineCombined sources
Modified residuei2451 – 24511PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60974.
MaxQBiQ60974.
PaxDbiQ60974.
PeptideAtlasiQ60974.
PRIDEiQ60974.

PTM databases

iPTMnetiQ60974.
PhosphoSiteiQ60974.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

CleanExiMM_NCOR1.

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.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Creb1Q011475EBI-349004,EBI-2291098
Dach1Q9QYB22EBI-349004,EBI-348961
HDAC9Q9UKV0-32EBI-349004,EBI-765476From a different organism.
HDAC9Q9UKV0-73EBI-349004,EBI-1372717From a different organism.
Sap30O885743EBI-349004,EBI-593511
SIRT1Q96EB62EBI-349004,EBI-1802965From a different organism.
SKIP127555EBI-349004,EBI-347281From a different organism.
SKILP127572EBI-349004,EBI-2902468From a different organism.
SNW1Q135733EBI-349004,EBI-632715From a different organism.

GO - Molecular functioni

  • histone deacetylase binding Source: MGI
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • nuclear hormone receptor binding Source: MGI
  • protein domain specific binding Source: BHF-UCL
  • retinoic acid receptor binding Source: MGI
  • retinoid X receptor binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: MGI
  • thyroid hormone receptor binding Source: MGI

Protein-protein interaction databases

DIPiDIP-32548N.
IntActiQ60974. 15 interactions.
MINTiMINT-2981744.
STRINGi10090.ENSMUSP00000018645.

Structurei

3D structure databases

ProteinModelPortaliQ60974.
SMRiQ60974. Positions 176-216, 433-486, 627-693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini435 – 48652SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini622 – 67352SANT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 373373Interaction with ZBTB33 and HEXIM1By similarityAdd
BLAST
Regioni254 – 31259Interaction with SIN3A/BAdd
BLAST
Regioni1510 – 2453944Interaction with C1DAdd
BLAST
Regioni2050 – 212980ID1Add
BLAST
Regioni2065 – 20684Required for interaction with RARA in the absence of its ligandBy similarity
Regioni2226 – 228762ID2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili174 – 21643Sequence analysisAdd
BLAST
Coiled coili299 – 32830Sequence analysisAdd
BLAST
Coiled coili501 – 55050Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1949 – 19535CORNR box 1
Motifi2073 – 20775CORNR box 2
Motifi2277 – 22815CORNR box 3

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 647Poly-Gln
Compositional biasi593 – 60210Poly-Ala
Compositional biasi606 – 61611Pro-richAdd
BLAST
Compositional biasi1044 – 10474Poly-Pro
Compositional biasi1713 – 17186Poly-Ala
Compositional biasi1968 – 197912Poly-SerAdd
BLAST

Domaini

The N-terminal region contains three independent domains that are capable of mediating transcriptional repression (RD1, RD2 and RD3).1 Publication
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.1 Publication

Sequence similaritiesi

Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1878. Eukaryota.
ENOG410YDXP. LUCA.
HOVERGENiHBG052587.
InParanoidiQ60974.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q60974-1) [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 PSHSVQYTFP SARHQQEFAV PDYRSSHLEV
60 70 80 90 100
SQASQLLQQQ QQQQLRRRPS LLSEFHPGSD RPQERRSGYE QFHPGPSPVD
110 120 130 140 150
HDSLESKRPR LEQVSDSHFQ RISAAVLPLV HTLPEGLRSS ANAKKDPAFG
160 170 180 190 200
VKHEAPSSPL 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 EKKDDEEKDD KEDSKETTKE
560 570 580 590 600
KDRTEATAEE PEEREQVTPR GRKTANSQGR GKGRVTRSMT SEAAAANAAA
610 620 630 640 650
AATEEPPPPL PPPPEPISTE PVETSRWTEE EMEVAKKGLV EHGRNWAAIA
660 670 680 690 700
KMVGTKSEAQ CKNFYFNYKR RHNLDNLLQQ HKQKASRKPR EERDVSQCES
710 720 730 740 750
VASTVSAQED EDIEASNEEE NPEDSEGAEN SSDTESAPSP SPVEAAKSSE
760 770 780 790 800
DSSENAASRG NTEPVAELEA TTDPAPCASP SSAVPTTKPA ERESVEAQVT
810 820 830 840 850
DSASAETAEP MDVDHEECGA EGSSVLDPPA PTKADSVDPE MQVPENTASK
860 870 880 890 900
GEGDAKERDL ESTSEKTEAR DEDVVVAEQI ERPEPQSDDD SSATCSADEG
910 920 930 940 950
VDGEPERQRV FPMDAKPSLL TPPGSILISS PIKPNLLDLP QLQHRAAVIP
960 970 980 990 1000
PMVSCTPCNI PIGTPVSGYA LYQRHIKAMH ESALLEEQRQ RQEQVDLECR
1010 1020 1030 1040 1050
SSTSPCSTSK SPNREWEVLQ PAPHQVITNL PEGVRLPTTR PTRPPPPLIP
1060 1070 1080 1090 1100
SSKTTVASEK PSFIMGGSIS QGTPGTYLSS HNQAYPQEAP KPSVGSISLG
1110 1120 1130 1140 1150
LPRQQESTKA APLTYIKQEE FSPRSQNSQP EGLLVRAQHE GVVRGTAGAV
1160 1170 1180 1190 1200
QEGSITRGTP ASKISVETIS SLRGSITQGT PALPQAGIPT EALVKGPVSR
1210 1220 1230 1240 1250
MPIEESSPEK VREEAASKGH VIYEGKSGHI LSYDNIKNAR EGTRSPRTAH
1260 1270 1280 1290 1300
EMSLKRSYEA VEGSIKQGMS MRESPVSAPL EGLICRALPR GSPHSDLKER
1310 1320 1330 1340 1350
TVLSGSIMQG TPRATAESFE DGLKYPKQIK RESPPIRAFE GAITKGKPYD
1360 1370 1380 1390 1400
GITTIKEMGR SIHEIPRQDI LTQESRKTPE VVQSTRPIIE GSISQGTPIK
1410 1420 1430 1440 1450
FDNNSGQSAI KHNVKSLITG PSKLPRGMLE IVPENIKVVE RGKYEDVKAG
1460 1470 1480 1490 1500
EPVRARHTSV VSSGPSVLRS TLHEAPKAQL SPGLYDDSSA RRTPVSYQNT
1510 1520 1530 1540 1550
ISRGSPMMNR TSDVSSSKSA SHERKSTLTP TQRESIPAKS PVPGVDPIVS
1560 1570 1580 1590 1600
HSPFDPHHRS SAAGEVYRSH LPTHLDPAMP FHRALDPAAA YLLQRQLSPT
1610 1620 1630 1640 1650
PGYPSQYQLY AMENTRQTIL NDYITSQQMQ VNLRPDVTRG LSPREQPLGL
1660 1670 1680 1690 1700
PYPATRGIID LTNMPPTILV PHAGGTSTPP MDRITYIPGT QVTFPPRPYN
1710 1720 1730 1740 1750
AASLSPGHPT HLAAAASAER EREREREKER ERERERERER ERERIAAAPA
1760 1770 1780 1790 1800
DLYLRPGSEQ PGRPGSHGYV RSPSPSVRTQ ETILQQRPSV FQGTNGTSVI
1810 1820 1830 1840 1850
TPLDPTAQLR IMPLPSGGPS ISQGLPASRY NTAADALAAL VDAAASAPQM
1860 1870 1880 1890 1900
DVSKTKESKH EAARLEENLR SRSAAVSEQQ QLEQKNLEVE KRSVQCVCTS
1910 1920 1930 1940 1950
SALPSGKAQP HASVVYSEAG KDKGPPPKSR YEEELRTRGK TTITAANFID
1960 1970 1980 1990 2000
VIITRQIASD KDARERGSQS SDSSSSLSSH RYETASDAIE VISPASSPAP
2010 2020 2030 2040 2050
PQEKPQAYQP DMVKANQAEN ESTRQYEGPL HHYRSQQESP SPQQQPPLPP
2060 2070 2080 2090 2100
SSQSEGMGQV PRTHRLITLA DHICQIITQD FARNQVPSQA STSTFQTSPS
2110 2120 2130 2140 2150
ALSSTPVRTK TSSRYSPESQ SQTVLHPRPG PRVSPENLVD KSRGSRPGKS
2160 2170 2180 2190 2200
PERSHIPSEP YEPISPPQGP AVHEKQDSML LLSQRGVDPA EQRSDSRSPG
2210 2220 2230 2240 2250
SISYLPSFFT KLESTSPMVK SKKQEIFRKL NSSGGGDSDM AAAQPGTEIF
2260 2270 2280 2290 2300
NLPAVTTSGA VSSRSHSFAD PASNLGLEDI IRKALMGSFD DKVEDHGVVM
2310 2320 2330 2340 2350
SHPVGIMPGS ASTSVVTSSE ARRDEGEPSP HAGVCKPKLI NKSNSRKSKS
2360 2370 2380 2390 2400
PIPGQSYLGT ERPSSVSSVH SEGDYHRQTP GWAWEDRPSS TGSTQFPYNP
2410 2420 2430 2440 2450
LTIRMLSSTP PTQIACAPSA ITQAAPHQQN RIWEREPAPL LSAQYETLSD

SDD
Length:2,453
Mass (Da):270,642
Last modified:November 1, 1996 - v1
Checksum:i52208B40382F7E6A
GO
Isoform 2 (identifier: Q60974-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2333-2371: Missing.

Show »
Length:2,414
Mass (Da):266,519
Checksum:i73D7A3799340A5F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1952 – 19521I → T in AAC52168 (PubMed:7760852).Curated
Sequence conflicti2090 – 20901A → P in AAC52168 (PubMed:7760852).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2333 – 237139Missing in isoform 2. 1 PublicationVSP_003411Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35312 mRNA. Translation: AAB17125.1.
U22016 mRNA. Translation: AAC52168.1.
PIRiS60254.
UniGeneiMm.271814.
Mm.460227.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35312 mRNA. Translation: AAB17125.1.
U22016 mRNA. Translation: AAC52168.1.
PIRiS60254.
UniGeneiMm.271814.
Mm.460227.

3D structure databases

ProteinModelPortaliQ60974.
SMRiQ60974. Positions 176-216, 433-486, 627-693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-32548N.
IntActiQ60974. 15 interactions.
MINTiMINT-2981744.
STRINGi10090.ENSMUSP00000018645.

PTM databases

iPTMnetiQ60974.
PhosphoSiteiQ60974.

Proteomic databases

EPDiQ60974.
MaxQBiQ60974.
PaxDbiQ60974.
PeptideAtlasiQ60974.
PRIDEiQ60974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1349717. Ncor1.

Phylogenomic databases

eggNOGiKOG1878. Eukaryota.
ENOG410YDXP. LUCA.
HOVERGENiHBG052587.
InParanoidiQ60974.

Enzyme and pathway databases

ReactomeiR-MMU-1368071. NR1D1 (REV-ERBA) represses gene expression.
R-MMU-1368082. RORA activates gene expression.
R-MMU-1368092. Rora activates gene expression.
R-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-400253. Circadian Clock.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-5667092. Nr1d1 (Rev-erba) represses gene expression.

Miscellaneous databases

ChiTaRSiNcor1. mouse.
PROiQ60974.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NCOR1.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor."
    Hoerlein A.J., Naeaer A.M., Heinzel T., Torchia J., Gloss B., Kurokawa R., Ryan A., Kamei Y., Soederstroem M., Glass C.K., Rosenfeld M.G.
    Nature 377:397-404(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Pituitary.
  2. "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors."
    Seol W., Choi H.S., Moore D.D.
    Mol. Endocrinol. 9:72-85(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1792-2453 (ISOFORM 1).
    Tissue: Liver.
  3. "Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR."
    Seol W., Mahon M.J., Lee Y.-K., Moore D.D.
    Mol. Endocrinol. 10:1646-1655(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RARB; RXRA AND THRB, DOMAINS ID1 AND ID2.
  4. Cited for: INTERACTION WITH SIN3A AND SIN3B.
  5. "Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex."
    Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1D.
  6. "Proteasomal regulation of nuclear receptor corepressor-mediated repression."
    Zhang J., Guenther M.G., Carthew R.W., Lazar M.A.
    Genes Dev. 12:1775-1780(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH2, DEGRADATION.
  7. "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors."
    Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N.
    Mol. Cell 2:33-42(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAP30 AND SIN3A.
  8. Cited for: INTERACTION WITH HDAC7.
  9. "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.
  10. "Tissue-specific regulation of retinal and pituitary precursor cell proliferation."
    Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.
    Science 297:1180-1183(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DACH1.
  11. "Lysine trimethylation of retinoic acid receptor-alpha: a novel means to regulate receptor function."
    Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.
    Mol. Cell. Proteomics 6:677-688(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RARA.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1481; SER-2449 AND SER-2451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters."
    Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H., Rochette-Egly C.
    EMBO J. 28:34-47(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RARA.
  14. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-1481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  16. "The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
    Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
    Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RXRA.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011; SER-1122; THR-1378; SER-1459; SER-1481; SER-1993 AND SER-2198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  18. Cited for: INTERACTION WITH RORA AND RORC.
  19. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNCOR1_MOUSE
AccessioniPrimary (citable) accession number: Q60974
Secondary accession number(s): Q60812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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