RBBP7

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Retinoblastoma binding protein 7
Protein RBBP7 PDB 3CFS.png
Rendering based on PDB 3CFS.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RBBP7 ; RbAp46
External IDs OMIM300825 MGI1194910 HomoloGene55702 GeneCards: RBBP7 Gene
RNA expression pattern
PBB GE RBBP7 201092 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5931 245688
Ensembl ENSG00000102054 ENSMUSG00000031353
UniProt Q16576 Q60973
RefSeq (mRNA) NM_001198719 NM_009031
RefSeq (protein) NP_001185648 NP_033057
Location (UCSC) Chr X:
16.86 – 16.89 Mb
Chr X:
162.76 – 162.78 Mb
PubMed search [1] [2]

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

Function[edit]

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]

Model organisms[edit]

Model organisms have been used in the study of RBBP7 function. A conditional knockout mouse line, called Rbbp7tm1a(EUCOMM)Wtsi[6][7] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[8][9][10]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty one tests were carried out on mutant mice and one significant abnormality was observed: hemizygous mutant males had decreased CD4-positive and CD8-positive T cell numbers.[4]

Interactions[edit]

RBBP7 has been shown to interact with:

References[edit]

  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". 
  3. ^ "Peripheral blood lymphocytes data for Rbbp7". Wellcome Trust Sanger Institute. 
  4. ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  5. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  6. ^ "International Knockout Mouse Consortium". 
  7. ^ "Mouse Genome Informatics". 
  8. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V et al. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750. 
  9. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  10. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  11. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 
  12. ^ a b Yarden RI, Brody LC (April 1999). "BRCA1 interacts with components of the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–8. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405. 
  13. ^ Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY (June 2001). "Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1". Biochem. Biophys. Res. Commun. 284 (2): 507–14. doi:10.1006/bbrc.2001.5003. PMID 11394910. 
  14. ^ Yarden RI, Brody LC. "Identification of proteins that interact with BRCA1 by Far-Western library screening". J. Cell. Biochem. 83 (4): 521–31. doi:10.1002/jcb.1257. PMID 11746496. 
  15. ^ Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (January 2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/mcb.22.2.536-546.2002. PMC 139742. PMID 11756549. 
  16. ^ a b Yao YL, Yang WM (October 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". J. Biol. Chem. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132. 
  17. ^ Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H et al. (September 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nat. Genet. 23 (1): 58–61. doi:10.1038/12659. PMID 10471499. 
  18. ^ a b c Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591. 
  19. ^ 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 89 (3): 357–64. doi:10.1016/s0092-8674(00)80216-0. PMID 9150135. 
  20. ^ a b Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M et al. (June 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell 1 (7): 1021–31. doi:10.1016/s1097-2765(00)80102-1. PMID 9651585. 
  21. ^ a b Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (February 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. 22 (3): 835–48. doi:10.1128/mcb.22.3.835-848.2002. PMC 133546. PMID 11784859. 

Further reading[edit]