RBBP6

RBBP6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRBBP6, MY038, P2P-R, PACT, RBQ-1, SNAMA, retinoblastoma binding protein 6, RB binding protein 6, ubiquitin ligase
External IDsMGI: 894835 HomoloGene: 136812 GeneCards: RBBP6
Gene location (Human)
Chr.Chromosome 16 (human)[1]
BandNo data availableStart24,537,693 bp[1]
End24,572,863 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5930

19647

Ensembl

ENSG00000122257

ENSMUSG00000030779

UniProt

Q7Z6E9

P97868

RefSeq (mRNA)

NM_006910
NM_018703
NM_032626

NM_011247
NM_175023

RefSeq (protein)

NP_008841
NP_061173
NP_116015

NP_035377
NP_778188

Location (UCSC)Chr 16: 24.54 – 24.57 MbChr 16: 122.97 – 123 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Retinoblastoma-binding protein 6 is a protein that in humans is encoded by the RBBP6 gene.[5][6][7]

Function

The retinoblastoma tumor suppressor (pRB) protein binds with many other proteins. In various human cancers, pRB suppresses cellular proliferation and is inactivated. Cell cycle-dependent phosphorylation regulates the activity of pRB. This gene encodes a protein which binds to underphosphorylated but not phosphorylated pRB. Multiple alternatively spliced transcript variants that encode different isoforms have been found for this gene.[7]

Interactions

RBBP6 has been shown to interact with Y box binding protein 1.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000122257 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030779 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Sakai Y, Saijo M, Coelho K, Kishino T, Niikawa N, Taya Y (Nov 1995). "cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 (RBBP6), that binds to the retinoblastoma gene product". Genomics. 30 (1): 98–101. PMID 8595913. doi:10.1006/geno.1995.0017.
  6. ↑ Pugh DJ, Ab E, Faro A, Lutya PT, Hoffmann E, Rees DJ (Feb 2006). "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways". BMC Structural Biology. 6: 1. PMC 1360078 Freely accessible. PMID 16396680. doi:10.1186/1472-6807-6-1.
  7. 1 2 "Entrez Gene: RBBP6 retinoblastoma binding protein 6".
  8. ↑ Chibi M, Meyer M, Skepu A, G Rees DJ, Moolman-Smook JC, Pugh DJ (Dec 2008). "RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1". Journal of Molecular Biology. 384 (4): 908–16. PMID 18851979. doi:10.1016/j.jmb.2008.09.060.

Further reading

  • Simons A, Melamed-Bessudo C, Wolkowicz R, Sperling J, Sperling R, Eisenbach L, Rotter V (Jan 1997). "PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb". Oncogene. 14 (2): 145–55. PMID 9010216. doi:10.1038/sj.onc.1200825. 
  • Gao S, Witte MM, Scott RE (May 2002). "P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity". Journal of Cellular Physiology. 191 (2): 145–54. PMID 12064457. doi:10.1002/jcp.10084. 
  • Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. PMC 442148 Freely accessible. PMID 15231748. doi:10.1101/gr.2334104. 
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. PMC 514446 Freely accessible. PMID 15302935. doi:10.1073/pnas.0404720101. 
  • Yoshitake Y, Nakatsura T, Monji M, Senju S, Matsuyoshi H, Tsukamoto H, Hosaka S, Komori H, Fukuma D, Ikuta Y, Katagiri T, Furukawa Y, Ito H, Shinohara M, Nakamura Y, Nishimura Y (Oct 2004). "Proliferation potential-related protein, an ideal esophageal cancer antigen for immunotherapy, identified using complementary DNA microarray analysis". Clinical Cancer Research. 10 (19): 6437–48. PMID 15475430. doi:10.1158/1078-0432.CCR-04-0841. 
  • Scott RE, White-Grindley E, Ruley HE, Chesler EJ, Williams RW (Jul 2005). "P2P-R expression is genetically coregulated with components of the translation machinery and with PUM2, a translational repressor that associates with the P2P-R mRNA". Journal of Cellular Physiology. 204 (1): 99–105. PMID 15617101. doi:10.1002/jcp.20263. 
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. PMID 16964243. doi:10.1038/nbt1240. 
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. PMID 17081983. doi:10.1016/j.cell.2006.09.026. 
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