Q60974 (NCOR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 134.
History...
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Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 2453 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. |
| Subunit structure | 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 HEXIM1 By similarity. Interacts with C1D, SIAH2, HDAC7, SAP30, SIN3A and SIN3B. 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. Interacts with DACH1. Component of the N-Cor repressor complex, at least composed of CBFA2T3, HEXIM1, NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 |
| Subcellular location | |
| Tissue specificity | Ubiquitous. |
| Domain | The N-terminal region contains three independent domains that are capable of mediating transcriptional repression (RD1, RD2 and RD3). Ref.3 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. Ref.3 |
| Post-translational modification | Ubiquitinated; mediated by SIAH2 and leading to its subsequent proteasomal degradation Probable. Ref.6 |
| Sequence similarities | Belongs to the N-CoR nuclear receptor corepressors family. Contains 2 SANT domains. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Dach1 | Q9QYB2 | 2 | EBI-349004,EBI-348961 | |
| HDAC9 | Q9UKV0-3 | 2 | EBI-349004,EBI-765476 | From a different organism. |
| HDAC9 | Q9UKV0-7 | 3 | EBI-349004,EBI-1372717 | From a different organism. |
| Sap30 | O88574 | 3 | EBI-349004,EBI-593511 | |
| SIRT1 | Q96EB6 | 2 | EBI-349004,EBI-1802965 | From a different organism. |
| SKI | P12755 | 5 | EBI-349004,EBI-347281 | From a different organism. |
| SKIL | P12757 | 2 | EBI-349004,EBI-2902468 | From a different organism. |
| SNW1 | Q13573 | 3 | EBI-349004,EBI-632715 | From a different organism. |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q60974-1) 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: Q60974-2) The sequence of this isoform differs from the canonical sequence as follows: 2333-2371: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2453 | 2453 | Nuclear receptor corepressor 1 | PRO_0000055618 | |||||
Regions | |||||||||
| Domain | 435 – 486 | 52 | SANT 1 | ||||||
| Domain | 622 – 673 | 52 | SANT 2 | ||||||
| Region | 1 – 373 | 373 | Interaction with ZBTB33 and HEXIM1 By similarity | ||||||
| Region | 254 – 312 | 59 | Interaction with SIN3A/B | ||||||
| Region | 1510 – 2453 | 944 | Interaction with C1D | ||||||
| Region | 2050 – 2129 | 80 | ID1 | ||||||
| Region | 2065 – 2068 | 4 | Required for interaction with RARA in the absence of its ligand By similarity | ||||||
| Region | 2226 – 2287 | 62 | ID2 | ||||||
| Coiled coil | 174 – 216 | 43 | Potential | ||||||
| Coiled coil | 299 – 328 | 30 | Potential | ||||||
| Coiled coil | 501 – 550 | 50 | Potential | ||||||
| Motif | 1949 – 1953 | 5 | CORNR box 1 | ||||||
| Motif | 2073 – 2077 | 5 | CORNR box 2 | ||||||
| Motif | 2277 – 2281 | 5 | CORNR box 3 | ||||||
| Compositional bias | 58 – 64 | 7 | Poly-Gln | ||||||
| Compositional bias | 593 – 602 | 10 | Poly-Ala | ||||||
| Compositional bias | 606 – 616 | 11 | Pro-rich | ||||||
| Compositional bias | 1044 – 1047 | 4 | Poly-Pro | ||||||
| Compositional bias | 1713 – 1718 | 6 | Poly-Ala | ||||||
| Compositional bias | 1968 – 1979 | 12 | Poly-Ser | ||||||
Amino acid modifications | |||||||||
| Modified residue | 224 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1011 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1122 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1206 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1423 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1481 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1993 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1997 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2116 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2165 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2198 | 1 | Phosphoserine Ref.12 Ref.16 | ||||||
| Modified residue | 2412 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2449 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 2451 | 1 | Phosphoserine Ref.12 | ||||||
Natural variations | |||||||||
| Alternative sequence | 2333 – 2371 | 39 | Missing in isoform 2. | VSP_003411 | |||||
Experimental info | |||||||||
| Sequence conflict | 1952 | 1 | I → T in AAC52168. Ref.2 | ||||||
| Sequence conflict | 2090 | 1 | A → P in AAC52168. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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] | "A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression." Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M., Laherty C.D., Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E., Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G. Nature 387:43-48(1997) [PubMed] [Europe PMC] [Abstract] 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] | "Identification of a nuclear domain with deacetylase activity." Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M. Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000) [PubMed] [Europe PMC] [Abstract] 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] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198; SER-2449 AND SER-2451, MASS SPECTROMETRY. Tissue: Liver. |
| [13] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011; SER-2116 AND SER-2165, MASS SPECTROMETRY. Tissue: Melanoma. |
| [14] | "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. |
| [15] | "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, MASS SPECTROMETRY. Tissue: Macrophage. |
| [16] | "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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U35312 mRNA. Translation: AAB17125.1. U22016 mRNA. Translation: AAC52168.1. |
| IPI | IPI00274795. IPI00620682. |
| PIR | S60254. |
| UniGene | Mm.271814. Mm.460227. |
3D structure databases | |
| ProteinModelPortal | Q60974. |
| SMR | Q60974. Positions 176-216, 433-486, 627-693. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-32548N. |
| IntAct | Q60974. 10 interactions. |
| MINT | MINT-2981744. |
PTM databases | |
| PhosphoSite | Q60974. |
Proteomic databases | |
| PaxDb | Q60974. |
| PRIDE | Q60974. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| MGI | MGI:1349717. Ncor1. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOVERGEN | HBG052587. |
| InParanoid | Q60974. |
| OrthoDB | EOG4J6RQ2. |
Enzyme and pathway databases | |
| Reactome | REACT_127416. Developmental Biology. REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes. |
Gene expression databases | |
| CleanEx | MM_NCOR1. |
| Genevestigator | Q60974. |
| GermOnline | ENSMUSG00000018501. Mus musculus. |
Family and domain databases | |
| Gene3D | 1.10.10.60. 1 hit. |
| InterPro | IPR009057. Homeodomain-like. IPR001005. SANT/Myb. IPR017884. SANT_dom. [Graphical view] |
| Pfam | PF00249. Myb_DNA-binding. 1 hit. [Graphical view] |
| SMART | SM00717. SANT. 2 hits. [Graphical view] |
| SUPFAM | SSF46689. Homeodomain_like. 2 hits. |
| PROSITE | PS51293. SANT. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | NCOR1. mouse. |
| SOURCE | Search... |
Entry information
| Entry name | NCOR1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q60974 Secondary accession number(s): Q60812 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |