A genomic and functional inventory of deubiquitinating enzymes.
Open accessAbstract
Posttranslational modification of proteins by the small molecule ubiquitin is a key regulatory event, and the enzymes catalyzing these modifications have been the focus of many studies. Deubiquitinating enzymes, which mediate the removal and processing of ubiquitin, may be functionally as important but are less well understood. Here, we present an inventory of the deubiquitinating enzymes encoded in the human genome. In addition, we review the literature concerning these enzymes, with particular emphasis on their function, specificity, and the regulation of their activity.
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The USP7 TRAF-like domain endows USP7 with unique substrate recognition and specificity that sets it apart from other USPs.
“This endows USP7 with unique substrate recognition and specificity that sets it apart from other USPs (Nijman et al., 2005).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Nijman et al., 2005
USP7 is the sole member of the USP family with a TRAF-like domain.
“Of the USP family of enzymes, USP7 is the sole member with a TRAF-like domain.”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Nijman et al., 2005
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Novel Predicted Peptidases with a Potential Role in the Ubiquitin Signaling Pathway
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- Authors
- Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R.
- Affiliations
- The Netherlands Cancer Institute (NL)
- Whitehead Institute for Biomedical Research (US)
- Corresponding author
- Nijman, Sebastian M.B.
- Bernards, René
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2005-12
- Volume
- 123
- Issue
- 5
- Pages
- 773-786
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2088724822
- Cited by
- 1,854
- References
- 119
- Citations by year
- 2026: 43 · 2025: 61 · 2024: 89 · 2023: 70 · 2022: 94 · 2021: 115 · 2020: 109 · 2019: 112 · 2018: 90 · 2017: 91 · 2016: 71 · 2015: 84 · 2014: 87 · 2013: 106 · 2012: 105
- FWCI
- 5.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- deubiquitinase, ubiquitin, ubiquitination, post-translational modification, human genome, enzyme specificity, enzyme regulation, proteasome
- MeSH terms
- Animals, Chromatin, Endocytosis, Humans, Hydrolases, Models, Molecular, Endopeptidases, Phylogeny, Protein Conformation, Protein Processing, Post-Translational, Substrate Specificity, Genome, Human, Amino Acid Motifs, Ubiquitin, Proteasome Endopeptidase Complex
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