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Gene Review

RPN1  -  proteasome regulatory particle base...

Saccharomyces cerevisiae S288c

Synonyms: 26S proteasome regulatory subunit RPN1, HMG-CoA reductase degradation protein 2, HRD2, NAS1, Proteasome non-ATPase subunit 1, ...
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High impact information on RPN1

  • A component of the base, Rpn1, specifically recognizes the UBL domain of Rad23 through its leucine-rich-repeat-like (LRR-like) domain [1].
  • Proteasome subunit Rpn1 binds ubiquitin-like protein domains [1].
  • In addition, a screen for high-copy suppressors of the mating defect of one of the ER-retained ste6 mutants has identified a proteasome subunit, Hrd2p/p97, previously implicated in the regulated degradation of wild-type hydroxymethylglutaryl-CoA reductase in the ER membrane [2].
  • By cross-linking experiments, Rpn1 and Rpn2 were identified as Ubl-binding subunits [3].
  • Disruption of NAS1 resulted in several phenotypes, including lethality and temperature-sensitive growth, depending on the genetic background of the cells used [4].

Other interactions of RPN1

  • Taken together, the results suggest that the Rpn1 and Rpn2 in the base subcomplex form the receptor for the ubiquitin-like protein [3].


  1. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Elsasser, S., Gali, R.R., Schwickart, M., Larsen, C.N., Leggett, D.S., Müller, B., Feng, M.T., Tübing, F., Dittmar, G.A., Finley, D. Nat. Cell Biol. (2002) [Pubmed]
  2. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Loayza, D., Tam, A., Schmidt, W.K., Michaelis, S. Mol. Biol. Cell (1998) [Pubmed]
  3. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Saeki, Y., Sone, T., Toh-e, A., Yokosawa, H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  4. cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11. Tsurumi, C., Shimizu, Y., Saeki, M., Kato, S., Demartino, G.N., Slaughter, C.A., Fujimuro, M., Yokosawa, H., Yamasaki, M., Hendil, K.B., Toh-e, A., Tanahashi, N., Tanaka, K. Eur. J. Biochem. (1996) [Pubmed]
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