{PDOC51283} {PS51283; DUSP} {BEGIN} *********************** * DUSP domain profile * *********************** Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins (see ) from ubiquitin-conjugated proteins. All DUBs contain a catalytic domain surrounded by one or more subdomains, some of which contribute to target recognition. The ~120-residue DUSP (domain present in ubiquitin-specific proteases) domain is one of these specific subdomains. Single or tandem DUSP domains are located both N- and C-terminal to the ubiquitin carboxyl-terminal hydrolase catalytic core domain (see ) [1]. The DUSP domain displays a tripod-like AB3 fold with a three-helix bundle and a three-stranded anti-parallel beta-sheet ressembling the legs and seat of the tripod (see ). Conserved residues are predominantly involved in hydrophobic packing interactions within the three alpha-helices. The most conserved DUSP residues, forming the PGPI motif, are flanked by two long loops that vary both in length and sequence. The PGPI motif packs against the three- helix bundle and is highly ordered [1]. Some proteins known to contain a DUSP domain are listed below: - Mammalian ubiquitin carboxyl-terminal hydrolase 4 (USP4) (EC 3.4.19.12). - Mammalian ubiquitin carboxyl-terminal hydrolase 11 (USP11) (EC 3.4.19.12). - Mammalian ubiquitin carboxyl-terminal hydrolase 15 (USP15) (EC 3.4.19.12). - Mammalian ubiquitin carboxyl-terminal hydrolase 20 (USP20) (EC 3.4.19.12). - Mammalian ubiquitin carboxyl-terminal hydrolase 32 (USP32) (EC 3.4.19.12). - Vertebrate ubiquitin carboxyl-terminal hydrolase 33 (USP33) (EC 3.4.19.12). - Vertebrate ubiquitin carboxyl-terminal hydrolase 48 (USP48) (EC 3.4.19.12). The profile we developed covers the entire DUSP domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2006 / First entry. [ 1] de Jong R.N., AB E., Diercks T., Truffault V., Daniels M., Kaptein R., Folkers G.E. "Solution structure of the human ubiquitin-specific protease 15 DUSP domain." J. Biol. Chem. 281:5026-5031(2006). PubMed=16298993; DOI=10.1074/jbc.M510993200 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}