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Gene Review

RBBP6  -  retinoblastoma binding protein 6

Homo sapiens

Synonyms: E3 ubiquitin-protein ligase RBBP6, MY038, My038, P2P-R, P2PR, ...
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Disease relevance of RBBP6


High impact information on RBBP6


Biological context of RBBP6

  • It forms part of a three-domain form of RBBP6 containing the DWNN domain, a zinc knuckle and a RING finger domain, which is found in all eukaryotic genomes so far examined, in the majority of cases at single copy number [6].
  • Confocal microscopy next established the localization of P2P-R to nucleoli in interphase cells and at the periphery of chromosomes in mitotic cells that lack nucleoli [5].
  • These changes in P2P-R protein occur without a concomitant change in P2P-R mRNA expression suggesting that P2P-R immunoreactivity increases during mitosis [5].
  • The localization of P2P-R also is modulated during the cell cycle [7].
  • Functional potential of P2P-R: a role in the cell cycle and cell differentiation related to its interactions with proteins that bind to matrix associated regions of DNA [7]?

Anatomical context of RBBP6

  • The 250 kDa P2P-R protein is the predominate product expressed in multiple murine cell lines [7].

Associations of RBBP6 with chemical compounds

  • More striking is the > 10-fold enrichment of P2P-R protein in specimens of highly purified mitotic cells prepared by the mitotic shake-select technique, or by synchrony with the mitotic spindle disruption agents nocodazole or vinblastine [5].

Physical interactions of RBBP6

  • This compendium of data supports the possibility that P2P-R may form complexes with the Rb1 and/or p53 tumor suppressors and MARs-related factors, in a cell cycle and cell differentiation-dependent manner, to influence gene transcription/expression and nuclear organization [7].

Analytical, diagnostic and therapeutic context of RBBP6

  • RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease [6].
  • Western blots show that relative to G0 quiescent cells, P2P-R protein levels are higher in populations of G2/M cells prepared by the physiological parasynchronization technique of serum deprivation followed by serum stimulation [5].


  1. cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 (RBBP6), that binds to the retinoblastoma gene product. Sakai, Y., Saijo, M., Coelho, K., Kishino, T., Niikawa, N., Taya, Y. Genomics (1995) [Pubmed]
  2. Proliferation potential-related protein, an ideal esophageal cancer antigen for immunotherapy, identified using complementary DNA microarray analysis. 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. Clin. Cancer Res. (2004) [Pubmed]
  3. Could the Chagas disease elimination programme in Venezuela be compromised by reinvasion of houses by sylvatic Rhodnius prolixus bug populations? Sanchez-Martin, M.J., Feliciangeli, M.D., Campbell-Lendrum, D., Davies, C.R. Trop. Med. Int. Health (2006) [Pubmed]
  4. 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. Scott, R.E., White-Grindley, E., Ruley, H.E., Chesler, E.J., Williams, R.W. J. Cell. Physiol. (2005) [Pubmed]
  5. P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity. Gao, S., Witte, M.M., Scott, R.E. J. Cell. Physiol. (2002) [Pubmed]
  6. DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways. Pugh, D.J., Ab, E., Faro, A., Lutya, P.T., Hoffmann, E., Rees, D.J. BMC Struct. Biol. (2006) [Pubmed]
  7. Functional potential of P2P-R: a role in the cell cycle and cell differentiation related to its interactions with proteins that bind to matrix associated regions of DNA? Scott, R.E., Giannakouros, T., Gao, S., Peidis, P. J. Cell. Biochem. (2003) [Pubmed]
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