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Gene Review

UBP6  -  Ubp6p

Saccharomyces cerevisiae S288c

Synonyms: Deubiquitinating enzyme 6, Ubiquitin carboxyl-terminal hydrolase 6, Ubiquitin thioesterase 6, Ubiquitin-specific-processing protease 6, YFR010W
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Disease relevance of UBP6


High impact information on UBP6

  • Proteasome binding activates Ubp6 300-fold and is mediated by the ubiquitin-like domain of Ubp6, which is required for function in vivo [2].
  • Surprisingly, Rad23 and Ubp6 do not compete with each other for proteasome binding [3].
  • To study their relative contributions, we purified proteasomes from a mutant in the putative metalloprotease domain of Rpn11 and from a ubp6 null [4].
  • Here we show that deletion of the UBP6 gene in Saccharomyces cerevisiae causes sensitivity to a broad range of toxic compounds and antagonizes phenotypic expression and de novo induction of the yeast prion [PSI+], a functionally defective self-perpetuating isoform of the translation termination factor Sup35 [5].
  • An N-terminal deletion mutant of Ubp6 that lacks SUb is still capable of cleaving alpha-linked ubiquitin fusions, suggesting that SUb forms a separate domain to the catalytic core of Ubp6 and demonstrating that it is not required for in vitro cleavage activity [6].

Associations of UBP6 with chemical compounds


Other interactions of UBP6

  • These results also show that ubiquitin wasting in ubp6 mutants is proteasome mediated [7].
  • PDR2 Gain-of-function mutations eliminate the need for Pdr1 and require the UBP6 product for resistance to translational inhibitors [8].


  1. Purification and characterization of UBP6, a new ubiquitin-specific protease in Saccharomyces cerevisiae. Park, K.C., Woo, S.K., Yoo, Y.J., Wyndham, A.M., Baker, R.T., Chung, C.H. Arch. Biochem. Biophys. (1997) [Pubmed]
  2. Multiple associated proteins regulate proteasome structure and function. Leggett, D.S., Hanna, J., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R.T., Walz, T., Ploegh, H., Finley, D. Mol. Cell (2002) [Pubmed]
  3. Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. Elsasser, S., Chandler-Militello, D., Müller, B., Hanna, J., Finley, D. J. Biol. Chem. (2004) [Pubmed]
  4. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. Guterman, A., Glickman, M.H. J. Biol. Chem. (2004) [Pubmed]
  5. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. Chernova, T.A., Allen, K.D., Wesoloski, L.M., Shanks, J.R., Chernoff, Y.O., Wilkinson, K.D. J. Biol. Chem. (2003) [Pubmed]
  6. The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: SUb. Wyndham, A.M., Baker, R.T., Chelvanayagam, G. Protein Sci. (1999) [Pubmed]
  7. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Hanna, J., Leggett, D.S., Finley, D. Mol. Cell. Biol. (2003) [Pubmed]
  8. PDR2 Gain-of-function mutations eliminate the need for Pdr1 and require the UBP6 product for resistance to translational inhibitors. Keeven, J., Ko, D., Shallom, J., Uccelini, B., Golin, J. Curr. Genet. (2002) [Pubmed]
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