|PROSITE documentation PDOC50600 [for PROSITE entry PS50600]|
Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins from ubiquitin-conjugated proteins. They can be classified in 3 families according to sequence homology [1,2]: ubiquitin carboxyl-terminal hydrolases (UCH) (see <PDOC00127>), ubiquitin-specific processing proteases (UBP) (see <PDOC00750>), and ubiquitin-like proteases (ULP) (EC 184.108.40.206) specific for deconjugating ubiquitin-like proteins. In contrast to the UBP pathway, which is very redundant (16 UBP enzymes in yeast), there is few ubiquitin-like protease (only one in yeast, ULP1).
ULP1 catalyses two critical functions in the SUMO/Smt3 pathway via its cysteine protease activity. ULP1 processes the Smt3 C-terminal sequence (-GGATY) to its mature form (-GG), and it deconjugates Smt3 from the lysine epsilon-amino group of the target protein .
Crystal structure of yeast ULP1 bound to Smt3  revealed that the catalytic and interaction interface is situated in a shallow and narrow cleft where conserved residues recognize the Gly-Gly motif at the C-terminal extremity of Smt3 protein. Ulp1 adopts a novel architecture despite some structural similarity with other cysteine protease. The secondary structure is composed of seven α helices and seven β strands. The catalytic domain includes the central α helix, β-strands 4 to 6, and the catalytic triad (Cys-His-Asp) (see <PDB:1EUV>).
We developed a profile directed against the C-terminal part of ULP proteins that displays full proteolytic activity .Note:
These proteins belong to family C48 in the classification of peptidases [E1].Last update:
May 2008 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Chung C.H. Baek S.H.|
|Title||Deubiquitinating enzymes: their diversity and emerging roles.|
|Source||Biochem. Biophys. Res. Commun. 266:633-640(1999).|
|Title||Ubiquitin-dependent protein degradation.|
|Source||Annu. Rev. Genet. 30:405-439(1996).|
|3||Authors||Li S.J. Hochstrasser M.|
|Title||A new protease required for cell-cycle progression in yeast.|
|4||Authors||Mossessova E. Lima C.D.|
|Title||Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.|
|Source||Mol. Cell 5:865-876(2000).|