| Primary Identifier | IPR033841 | Type | Domain |
| Short Name | USP48 |
| description | Ubiquitin carboxyl-terminal hydrolases (UCH) () []are thiol proteases that recognise and hydrolyse the peptide bond at the C-terminal glycine of ubiquitin. These enzymes are involved in the processing of poly-ubiquitin precursors as well as that of ubiquinated proteins. The deubiquitinsing proteases can be split into 2 size ranges, 20-30kDa() and 100-200kDa []: the second class consist of large proteins (800 to 2000 residues) that belong to the peptidase family C19, and this group is currently represented by yeast UBP1 []. This entry contains the peptidase domain for ubiquitin-specific peptidase 48 (USP48; MEROPS identifier C19.068). In animals, USP48 is found in the nucleus where it trims long Lys48-linked free and substrate-anchored ubiquitin-chains, rather than completely disassembling them; a catalytic property only shared with ataxin-3 and otubain-1. USP48 ubiquitin-chain-trimming activity is regulated by casein-kinase-2-mediated phosphorylation in response to cytokine-stimulation. USP48 controls the turnover of activated NF-kB/RelA in the nucleus together with the CSN and contributes to a timely control of immune responses [].In plants, the gene name is USP26, which should not be confused with USP26 from mammals. USP26 deubiquitinates histone H2B and is required for heterochromatin silencing []. |
