RBBP7

Retinoblastoma binding protein 7

Rendering based on PDB 3CFS.
Identifiers
Symbols RBBP7; MGC138867; MGC138868; RbAp46
External IDs OMIM300825 MGI1194910 HomoloGene55702 GeneCards: RBBP7 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 5931 245688
Ensembl ENSG00000102054 ENSMUSG00000031353
UniProt Q16576 Q3UJI2
RefSeq (mRNA) NM_001198719.1 NM_009031.3
RefSeq (protein) NP_001185648.1 NP_033057.3
Location (UCSC) Chr X:
16.86 – 16.89 Mb
Chr X:
159.2 – 159.22 Mb
PubMed search [1] [2]

Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.[1]

This protein is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that binds directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein is found in many histone deacetylase complexes, including mSin3 co-repressor complex. It is also present in protein complexes involved in chromatin assembly. This protein can interact with BRCA1 tumor-suppressor gene and may have a role in the regulation of cell proliferation and differentiation.[2]

Interactions

RBBP7 has been shown to interact with HDAC1,[3][4][5][6] MTA2,[3][5] SIN3A,[7][8] Retinoblastoma protein,[1][9] SAP30,[5][7][8] GATAD2B[10] and BRCA1.[9][11][12]

References

  1. ^ a b Qian YW, Lee EY (Dec 1995). "Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast". J Biol Chem 270 (43): 25507–25513. doi:10.1074/jbc.270.43.25507. PMID 7503932. 
  2. ^ "Entrez Gene: RBBP7 retinoblastoma binding protein 7". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5931. 
  3. ^ a b Yao, Ya-Li; Yang Wen-Ming (Oct. 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". J. Biol. Chem. (United States) 278 (43): 42560–42568. doi:10.1074/jbc.M302955200. ISSN 0021-9258. PMID 12920132. 
  4. ^ Ng, H H; Zhang Y, Hendrich B, Johnson C A, Turner B M, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (Sep. 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nat. Genet. (UNITED STATES) 23 (1): 58–61. doi:10.1038/12659. ISSN 1061-4036. PMID 10471499. 
  5. ^ a b c Zhang, Y; Ng H H, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (Aug. 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. (UNITED STATES) 13 (15): 1924–1935. doi:10.1101/gad.13.15.1924. ISSN 0890-9369. PMC 316920. PMID 10444591. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316920. 
  6. ^ Zhang, Y; Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May. 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell (UNITED STATES) 89 (3): 357–364. doi:10.1016/S0092-8674(00)80216-0. ISSN 0092-8674. PMID 9150135. 
  7. ^ a b Zhang, Y; Sun Z W, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (Jun. 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell (UNITED STATES) 1 (7): 1021–1031. doi:10.1016/S1097-2765(00)80102-1. ISSN 1097-2765. PMID 9651585. 
  8. ^ a b Kuzmichev, A; Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (Feb. 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. (United States) 22 (3): 835–848. doi:10.1128/MCB.22.3.835-848.2002. ISSN 0270-7306. PMC 133546. PMID 11784859. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133546. 
  9. ^ a b Yarden, R I; Brody L C (Apr. 1999). "BRCA1 interacts with components of the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (9): 4983–4988. doi:10.1073/pnas.96.9.4983. ISSN 0027-8424. PMC 21803. PMID 10220405. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21803. 
  10. ^ Feng, Qin; Cao Ru, Xia Li, Erdjument-Bromage Hediye, Tempst Paul, Zhang Yi (Jan. 2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. (United States) 22 (2): 536–546. doi:10.1128/MCB.22.2.536-546.2002. ISSN 0270-7306. PMC 139742. PMID 11756549. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139742. 
  11. ^ Chen, G C; Guan L S, Yu J H, Li G C, Choi Kim H R, Wang Z Y (Jun. 2001). "Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1". Biochem. Biophys. Res. Commun. (United States) 284 (2): 507–514. doi:10.1006/bbrc.2001.5003. ISSN 0006-291X. PMID 11394910. 
  12. ^ Yarden RI, Brody LC (2001). "Identification of proteins that interact with BRCA1 by Far-Western library screening". J Cell Biochem 83 (4): 521–531. doi:10.1002/jcb.1257. PMID 11746496. 

Further reading