Deubiquitylating Enzymes [chapter]

Xin Li, Q. Ping Dou
2020 Encyclopedia of Molecular Pharmacology  
Synonyms Deubiquitinases Definition Deubiquitylating enzymes (DUBs) are the peptidases that can remove ubiquitin from substrate proteins, edit ubiquitin chains, or cleave ubiquitin precursors. Human genome encodes about 100 DUBs that can be classified into six families based on similar sequence and conserved domains. These DUB families include ubiquitin-specific proteases (USPs), ubiquitin carboxyl-terminal hydrolases (UCHs), Machado-Josephin domain-containing proteases (MJDs), ovarian tumor
more » ... ), ovarian tumor proteases (OTUs), motif interacting with ubiquitin-containing novel DUB family (MINDYs), and JAB1/MPN/MOV34 metalloenzyme family (JAMMs). The first five DUB families are cysteine peptidases with the catalytic triad of cysteine, histidine, and asparagine/asparagine residue, whereas JAMMs are zinc metallopeptidases. DUBs exhibit strong substrate selectivity in targeting individual proteins and structural motifs. This specificity is imparted via the key domain of DUBs, i.e., a zinc finger ubiquitin-specific protease domain (ZnF-UBP domain) (Dou and Zonder 2014; Farshi et al. 2015; Harrigan et al. 2018) .
doi:10.1007/978-3-030-21573-6_10018-1 fatcat:5waoqmabq5gu3a2qmdjmbsrcfa