| Primary Identifier | IPR059996 | Type | Domain |
| Short Name | USP28_C |
| description | This entry represents the C-terminal domain of ubiquitin-specific protease USP28, a deubiquitinase (DUB), which shares high similarity with USP25 but varies in cellular function [, ]. USP28 is known for its tumor-promoting role while USP25 is a regulator of the innate immune system and may play a role in tumorigenesis [, , , ]. USP28 stabilises c-MYC and other nuclear proteins, and USP25 regulates inflammatory TRAF signalling. These two closely related DUBs contain an N-terminal domain harbouring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID) [, ].This C-terminal region has been implicated in substrate binding for USP28 and harbours the splicing site for isoform-specific sequences. Structure studies suggest that the C-terminal domain forms an independent entity. |
