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Gene Review

USP20  -  ubiquitin specific peptidase 20

Homo sapiens

Synonyms: Deubiquitinating enzyme 20, KIAA1003, LSFR3A, Ubiquitin carboxyl-terminal hydrolase 20, Ubiquitin thioesterase 20, ...
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High impact information on USP20

  • D2 interaction with VDU1 and VDU2, a closely related deubiquitinase, was confirmed in mammalian cells [1].
  • VDU1, but not VDU2, is markedly increased in brown adipocytes by norepinephrine or cold exposure, further amplifying the increase in D2 activity that results from catecholamine-stimulated de novo synthesis [1].
  • These findings suggest that ubiquitination of HIF-1alpha is a dynamic process and that ubiquitinated HIF-1alpha might be rescued from degradation by VDU2 through deubiquitination [2].
  • Finally, we demonstrate that VDU2 can also be ubiquitinated and degraded in a pVHL-dependent manner [3].
  • VDU2 contains the signature motifs of the ubiquitin-specific processing protease family and possesses deubiquitinating activity [3].

Other interactions of USP20

  • Based on human and mouse cDNA sequences, VDU1 and VDU2 are identical in approximately 59% of the amino acids with strong homology in the N-terminus and C-terminus and a weaker similarity in the middle region [3].
  • Since deubiquitination, by reversing ubiquitination, has been recognized as an important regulatory step in ubiquitination-related processes, VDU1 and VDU2 could be important substrates of pVHL E3 ligase complex [3].


  1. Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation. Curcio-Morelli, C., Zavacki, A.M., Christofollete, M., Gereben, B., de Freitas, B.C., Harney, J.W., Li, Z., Wu, G., Bianco, A.C. J. Clin. Invest. (2003) [Pubmed]
  2. VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha. Li, Z., Wang, D., Messing, E.M., Wu, G. EMBO Rep. (2005) [Pubmed]
  3. Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor. Li, Z., Wang, D., Na, X., Schoen, S.R., Messing, E.M., Wu, G. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
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