| Primary Identifier | IPR044867 | Type | Domain |
| Short Name | DEUBAD_dom |
| description | Protein ubiquitination is a fundamental mechanism that affects nearly all aspects of cellular life. Deubiquitinating enzymes (DUBs) play important roles in ubiquitin (Ub) signalling by Ub cleavage from adducts. The Ub C-terminal hydrolase (UCH) family of deubiquitinases (DUBs) contains four members including UCH37 (also called ubiquitin carboxy-terminal hydrolase isozyme L5, UCHL-5) and BAP1 which share high similarity in the catalytic domain (UCH) and the C-terminal region, termed the UCH37-like domain (ULD) which is responsible for binding interaction partners and is also involved in the regulation of DUB activity. ULD from BAP1 and UCH-L5 binds the DEUBiquitinase ADaptor (DEUBAD) domain present in their interacting partners, e.g., ASXL1 for BAP1, and RPN13 (ADRM1) and INO80G (NFRKB) for UCH-L5 [, , , , ].This entry represents the DEUBAD domain which consists of eight α-helices that form a helical bundle surrounding a compact hydrophobic core []. It has a modular architecture with the core formed by helices 1-4, primarily responsible for binding to ULD, and accessory elements that lead to full activation, or inhibition, of the UCH activity [, ]. |
