DEUBAD domain
IPR044867
Definition
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 [[cite:PMID:22645167], [cite:PMID:24752541], [cite:PMID:26739236], [cite:PMID:30349006], [cite:PMID:30258054]]. This entry represents the DEUBAD domain which consists of eight α-helices that form a helical bundle surrounding a compact hydrophobic core PMID:20471946. 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 [[cite:PMID:25702870], [cite:PMID:30639226]].
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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