{PDOC00127} {PS00140; UCH_1} {BEGIN} ************************************************************************ * Ubiquitin carboxyl-terminal hydrolases family 1 cysteine active site * ************************************************************************ Ubiquitin carboxyl-terminal hydrolases (EC 3.4.19.12) (UCH) (deubiquitinating enzymes) [1,2] are thiol proteases that recognize and hydrolyze 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. There are two distinct families of UCH. The first class consist of enzymes of about 25 Kd and is currently represented by: - Mammalian isozymes L1, L3 and L5. - Yeast YUH1. - Drosophila Uch. One of the active site residues of class-I UCH [3] is a cysteine. We derived a signature pattern from the region around that residue. -Consensus pattern: Q-x(3)-N-[SA]-C-G-x(3)-[LIVM](2)-H-[SA]-[LIVM]-[SA] [C is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: These proteins belong to family C12 in the classification of peptidases [4,E1]. -Last update: December 2001 / Text revised. [ 1] Jentsch S., Seufert W., Hauser H.-P. "Genetic analysis of the ubiquitin system." Biochim. Biophys. Acta 1089:127-139(1991). PubMed=1647207 [ 2] D'andrea A., Pellman D. Crit. Rev. Biochem. Mol. Biol. 33:337-352(1998). [ 3] Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P. "Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution." EMBO J. 16:3787-3796(1997). PubMed=9233788; DOI=10.1093/emboj/16.13.3787 [ 4] Rawlings N.D., Barrett A.J. "Families of cysteine peptidases." Methods Enzymol. 244:461-486(1994). PubMed=7845226 [E1] https://www.uniprot.org/docs/peptidas -------------------------------------------------------------------------------- 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}