Q9WU42 (NCOR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 119.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nuclear receptor corepressor 2 Short name=N-CoR2 Alternative name(s): Silencing mediator of retinoic acid and thyroid hormone receptor Short name=SMRT Short name=SMRTe T3 receptor-associating factor Short name=TRAC Thyroid-, retinoic-acid-receptor-associated corepressor | ||||
| Gene names |
| ||||
| 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 | 2472 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transcriptional corepressor of NR4A2/NURR1 and acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Ref.9 |
| Subunit structure | 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, and may stabilize their interaction with TFIIB. Interacts directly with RARA in the absence of ligand; the interaction represses RARA activity. Interacts with HDAC10, BCL6 and MINT. Interacts with ATXN1L. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Interacts with RARB; the interaction is weak and does not repress RARB transactivational activity By similarity. Interacts with CBFA2T3, C1D and HDAC7. Interacts with NR4A2; the interaction increases in the absence of PITX3. Ref.4 Ref.5 Ref.6 Ref.9 |
| Subcellular location | |
| Tissue specificity | Ubiquitous. Also widely expressed in early embryos. |
| Domain | The N-terminal region contains repression functions that are divided into three independent repression domains (RD1, RD2 and RD3). The C-terminal region contains the nuclear receptor-interacting domains that are divided in two separate interaction domains (ID1 and ID2). The two interaction domains (ID) contain a conserved sequence referred to as the CORNR box. This motif is required and sufficient to permit binding to unligated TR and RARS. Sequences flanking the CORNR box determine nuclear hormone receptor specificity. |
| Sequence similarities | Belongs to the N-CoR nuclear receptor corepressors family. Contains 2 SANT domains. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Alpha (identifier: Q9WU42-1) 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 Beta (identifier: Q9WU42-2) The sequence of this isoform differs from the canonical sequence as follows: 36-254: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2472 | 2472 | Nuclear receptor corepressor 2 | PRO_0000055623 | |||||
Regions | |||||||||
| Domain | 427 – 478 | 52 | SANT 1 | ||||||
| Domain | 606 – 657 | 52 | SANT 2 | ||||||
| Region | 254 – 312 | 59 | Interaction with SIN3A/B By similarity | ||||||
| Region | 2086 – 2090 | 5 | Required for interaction with RARA in the absence of its ligand By similarity | ||||||
| Coiled coil | 165 – 207 | 43 | Potential | ||||||
| Coiled coil | 492 – 560 | 69 | Potential | ||||||
| Coiled coil | 658 – 682 | 25 | Potential | ||||||
| Motif | 2094 – 2098 | 5 | CORNR box of ID1 | ||||||
| Motif | 2296 – 2300 | 5 | CORNR box of ID2 | ||||||
| Compositional bias | 494 – 507 | 14 | Poly-Gln | ||||||
| Compositional bias | 775 – 804 | 30 | Pro-rich | ||||||
| Compositional bias | 989 – 999 | 11 | Pro-rich | ||||||
| Compositional bias | 1351 – 1357 | 7 | Pro-rich | ||||||
| Compositional bias | 1615 – 1619 | 5 | Poly-Ala | ||||||
| Compositional bias | 2434 – 2437 | 4 | Poly-Pro | ||||||
Amino acid modifications | |||||||||
| Modified residue | 54 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 67 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 149 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 152 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 215 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 549 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 550 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 747 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 750 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 863 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 878 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 938 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 955 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 958 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1181 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1209 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1220 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1350 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1406 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 1449 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1749 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1819 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1920 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1963 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1983 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 2004 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2012 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2015 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2016 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2020 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2161 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2181 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2215 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2410 | 1 | Phosphoserine Ref.7 | ||||||
Natural variations | |||||||||
| Alternative sequence | 36 – 254 | 219 | Missing in isoform Beta. | VSP_003414 | |||||
Experimental info | |||||||||
| Sequence conflict | 176 | 1 | M → RL in AAD22972. Ref.2 | ||||||
| Sequence conflict | 396 – 402 | 7 | PPMLYDA → RHVVRR in AAD22972. Ref.2 | ||||||
| Sequence conflict | 555 | 1 | D → H in AAD20944. Ref.1 | ||||||
| Sequence conflict | 756 | 1 | T → M in AAD20944. Ref.1 | ||||||
| Sequence conflict | 785 | 1 | V → A in AAD22972. Ref.2 | ||||||
| Sequence conflict | 806 – 846 | 41 | PSPAA…EIDVG → HHLPHPRLLWTRMNKKPRLL QLPRQRMPRSRSLRPRRSMW E in AAD20944. Ref.1 | ||||||
| Sequence conflict | 806 – 846 | 41 | PSPAA…EIDVG → HHLPHPRLLWTRMNKKPRLL QLPRQRMPRSRSLRPRRSMW E in AAD20945. Ref.1 | ||||||
| Sequence conflict | 856 | 1 | E → K in AAD20945. Ref.1 | ||||||
| Sequence conflict | 859 | 1 | E → K in AAD20945. Ref.1 | ||||||
| Sequence conflict | 867 | 1 | E → K in AAD20945. Ref.1 | ||||||
| Sequence conflict | 895 | 1 | E → K in AAD20945. Ref.1 | ||||||
| Sequence conflict | 916 | 1 | S → F in AAD20944. Ref.1 | ||||||
| Sequence conflict | 975 | 1 | I → IQ in AAD20944. Ref.1 | ||||||
| Sequence conflict | 1046 – 1063 | 18 | PKLPT…LPFPI → QSYRLSPHAGHRLPSH in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1073 – 1080 | 8 | PHAADPSA → TRADPL in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1133 | 1 | Missing in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1149 | 1 | Missing in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1157 | 1 | G → E in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1172 – 1201 | 30 | GSATS…SITHG → APPPVEASPRASQYPGCRRP QLQRLYHPR in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1696 | 1 | A → S in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1855 – 1857 | 3 | Missing in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1909 | 1 | P → A in AAD20944. Ref.1 | ||||||
| Sequence conflict | 1909 | 1 | P → A in AAD20945. Ref.1 | ||||||
| Sequence conflict | 1913 | 1 | A → G in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1923 | 1 | A → G in AAD20944. Ref.1 | ||||||
| Sequence conflict | 1923 | 1 | A → G in AAD20945. Ref.1 | ||||||
| Sequence conflict | 1956 | 1 | N → S in AAD22972. Ref.2 | ||||||
| Sequence conflict | 1968 | 1 | A → G in AAD22972. Ref.2 | ||||||
| Sequence conflict | 2195 – 2196 | 2 | TA → AV in AAD22972. Ref.2 | ||||||
| Sequence conflict | 2213 – 2214 | 2 | SK → LE in AAD20944. Ref.1 | ||||||
| Sequence conflict | 2224 | 1 | A → T in AAD20944. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Unique forms of human and mouse nuclear receptor corepressor SMRT." Ordentlich P., Downes M., Xie W., Genin A., Spinner N.B., Evans R.M. Proc. Natl. Acad. Sci. U.S.A. 96:2639-2644(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). Tissue: Brain and Spleen. |
| [2] | "SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor." Park E.J., Schroen D.J., Yang M., Li H., Li L., Chen J.D. Proc. Natl. Acad. Sci. U.S.A. 96:3519-3524(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). Tissue: Embryo. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.  Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [4] | "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. |
| [5] | "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression." Kao H.-Y., Downes M., Ordentlich P., Evans R.M. Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC7. |
| [6] | "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. |
| [7] | "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 THR-549; SER-550; SER-938 AND SER-2410, MASS SPECTROMETRY. Tissue: Liver. |
| [8] | "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-149; SER-152; SER-863; THR-1406 AND SER-1749, MASS SPECTROMETRY. Tissue: Melanoma. |
| [9] | "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression." Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P., Smidt M.P. Development 136:531-540(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NR4A2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF113001 mRNA. Translation: AAD20944.1. AF113002 mRNA. Translation: AAD20945.1. AF125671 mRNA. Translation: AAD22972.1. AC132118 Genomic DNA. No translation available. AC139377 Genomic DNA. No translation available. |
| IPI | IPI00123871. IPI00222492. |
| RefSeq | NP_001240833.1. NM_001253904.1. NP_001240834.1. NM_001253905.1. |
| UniGene | Mm.278646. Mm.472258. |
3D structure databases | |
| ProteinModelPortal | Q9WU42. |
| SMR | Q9WU42. Positions 167-207, 408-476, 611-681. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-3154743. |
| STRING | 10090.ENSMUSP00000107033. |
PTM databases | |
| PhosphoSite | Q9WU42. |
Proteomic databases | |
| PaxDb | Q9WU42. |
| PRIDE | Q9WU42. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000111394; ENSMUSP00000107025; ENSMUSG00000029478. ENSMUST00000111398; ENSMUSP00000107029; ENSMUSG00000029478. |
| GeneID | 20602. |
| KEGG | mmu:20602. |
| UCSC | uc008zqv.1. mouse. uc008zqx.1. mouse. |
Organism-specific databases | |
| CTD | 9612. |
| MGI | MGI:1337080. Ncor2. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| GeneTree | ENSGT00550000074554. |
| HOGENOM | HOG000113746. |
| HOVERGEN | HBG052587. |
| KO | K06065. |
Enzyme and pathway databases | |
| Reactome | REACT_127416. Developmental Biology. REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes. |
Gene expression databases | |
| ArrayExpress | Q9WU42. |
| Bgee | Q9WU42. |
| CleanEx | MM_NCOR2. |
| Genevestigator | Q9WU42. |
| GermOnline | ENSMUSG00000029478. 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 | NCOR2. mouse. |
| NextBio | 298933. |
| SOURCE | Search... |
Entry information
| Entry name | NCOR2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9WU42 Secondary accession number(s): E9Q9V0, Q9WU43, Q9WUC1 | ||||||||
| 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 |