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Gene Review

UBP1  -  Ubp1p

Saccharomyces cerevisiae S288c

Synonyms: D2250, Deubiquitinating enzyme 1, Ubiquitin carboxyl-terminal hydrolase 1, Ubiquitin thioesterase 1, Ubiquitin-specific-processing protease 1, ...
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Disease relevance of UBP1


High impact information on UBP1


Biological context of UBP1

  • Ubp2 (1,264 residues), Ubp3 (912 residues), and the previously cloned Ubp1 (809 residues) are largely dissimilar except for two short regions containing Cys and His which encompass their putative active sites [6].
  • The amino acid sequence of the 809-residue UBP1 lacks significant similarities to other known proteins, including the 236-residue YUH1 protease [1].
  • On Ubp1 overexpression, Ste6 accumulates at the cell surface, which is consistent with a role of Ubp1 at the internalization step of endocytosis or with enhanced recycling to the cell surface from an internal compartment [5].
  • Additional PIPs include the heat shock proteins Hsp70 and Hsp82, the deubiquitinating enzyme Ubp6, and proteins involved in transcriptional control, mitosis, tubulin assembly, RNA metabolism, and signal transduction [7].
  • UBP10 codes for a deubiquitinating enzyme of Saccharomyces cerevisiae whose loss of function determines slow growth rate and partial impairment of silencing at telomeres and HM loci [8].

Anatomical context of UBP1


Associations of UBP1 with chemical compounds


Physical interactions of UBP1


Enzymatic interactions of UBP1

  • With the exception of polyubiquitin, the UBP1 protease cleaves at the carboxyl terminus of the ubiquitin moiety in natural and engineered fusions irrespective of their size or the presence of an amino-terminal ubiquitin extension [1].

Other interactions of UBP1

  • YUH1 and UBP1, the genes for two ubiquitin-specific proteases of the yeast Saccharomyces cerevisiae, have been cloned previously and shown to encode nonhomologous proteins [6].
  • Ste6 stabilization was not the result of a general increase in deubiquitination activity, because overexpression of Ubp1 had no effect on the degradation of the ER-associated degradation substrate carboxypeptidase Y* and most importantly on Ste6 ubiquitination itself [5].
  • Another yeast deubiquitinating enzyme, Ubp5, which is related in sequence to Doa4 but cannot substitute for it even when overproduced, does not associate with the proteasome [14].
  • The deubiquitinating enzyme Doa4p protects cells from DNA topoisomerase I poisons [15].
  • The influence of Ubp14p, a deubiquitinating enzyme, on proteasome-dependent catabolite degradation was further uncovered [16].


  1. Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. Tobias, J.W., Varshavsky, A. J. Biol. Chem. (1991) [Pubmed]
  2. A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Moazed, D., Johnson, D. Cell (1996) [Pubmed]
  3. The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. Kee, Y., Lyon, N., Huibregtse, J.M. EMBO J. (2005) [Pubmed]
  4. The Deubiquitinating Enzyme Ubp2 Modulates Rsp5-dependent Lys63-linked Polyubiquitin Conjugates in Saccharomyces cerevisiae. Kee, Y., Mu??oz, W., Lyon, N., Huibregtse, J.M. J. Biol. Chem. (2006) [Pubmed]
  5. The deubiquitinating enzyme Ubp1 affects sorting of the ATP-binding cassette-transporter Ste6 in the endocytic pathway. Schmitz, C., Kinner, A., Kölling, R. Mol. Biol. Cell (2005) [Pubmed]
  6. Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. Baker, R.T., Tobias, J.W., Varshavsky, A. J. Biol. Chem. (1992) [Pubmed]
  7. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Verma, R., Chen, S., Feldman, R., Schieltz, D., Yates, J., Dohmen, J., Deshaies, R.J. Mol. Biol. Cell (2000) [Pubmed]
  8. Transcriptional profiling of ubp10 null mutant reveals altered subtelomeric gene expression and insurgence of oxidative stress response. Orlandi, I., Bettiga, M., Alberghina, L., Vai, M. J. Biol. Chem. (2004) [Pubmed]
  9. RBP45 and RBP47, two oligouridylate-specific hnRNP-like proteins interacting with poly(A)+ RNA in nuclei of plant cells. Lorković, Z.J., Wieczorek Kirk, D.A., Klahre, U., Hemmings-Mieszczak, M., Filipowicz, W. RNA (2000) [Pubmed]
  10. The yeast deubiquitinating enzyme Ubp16 is anchored to the outer mitochondrial membrane. Kinner, A., Kölling, R. FEBS Lett. (2003) [Pubmed]
  11. Genetic analysis of the role of the drosophila fat facets gene in the ubiquitin pathway. Wu, Z., Li, Q., Fortini, M.E., Fischer, J.A. Dev. Genet. (1999) [Pubmed]
  12. The Histone Deubiquitinating Enzyme Ubp10 Is Involved in rDNA Locus Control in Saccharomyces cerevisiae by Affecting Sir2p Association. Calzari, L., Orlandi, I., Alberghina, L., Vai, M. Genetics (2006) [Pubmed]
  13. Atg19p ubiquitination and the cytoplasm to vacuole trafficking pathway in yeast. Baxter, B.K., Abeliovich, H., Zhang, X., Stirling, A.G., Burlingame, A.L., Goldfarb, D.S. J. Biol. Chem. (2005) [Pubmed]
  14. Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Papa, F.R., Amerik, A.Y., Hochstrasser, M. Mol. Biol. Cell (1999) [Pubmed]
  15. The deubiquitinating enzyme Doa4p protects cells from DNA topoisomerase I poisons. Fiorani, P., Reid, R.J., Schepis, A., Jacquiau, H.R., Guo, H., Thimmaiah, P., Benedetti, P., Bjornsti, M.A. J. Biol. Chem. (2004) [Pubmed]
  16. Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Regelmann, J., Schüle, T., Josupeit, F.S., Horak, J., Rose, M., Entian, K.D., Thumm, M., Wolf, D.H. Mol. Biol. Cell (2003) [Pubmed]
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