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. Author manuscript; available in PMC: 2010 Jan 1.
Published in final edited form as: Annu Rev Biochem. 2009;78:363–397. doi: 10.1146/annurev.biochem.78.082307.091526

Figure 1.

Figure 1

Domain structure of yeast UBP deubiquitinating enzymes. The catalytic core is indicated by the blue boxes. Other common domains are indicated with differently colored boxes: MATH, meparin and TRAF homology; Rhodanese, rhodanese-like; ZnF-UBP, zinc finger common in UBP DUBs, UBL, ubiquitin-like, and UBA, ubiquitin-associated. Three sites of common insertions within the catalytic core are indicated by arrows. These insertions and the N- and C-terminal extensions are thought to provide specific sequences that define substrate specificity and provide interaction surfaces for binding to adapters and scaffolds.