EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.22.68 | His6-Smt3-hemagglutinin fusion protein + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.68 | His6-Smt3-Leu-beta-galactosidase + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.68 | His6-Smt3-Met-beta-galactosidase + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.68 | more |
the NH2-terminal regulatory domain of Ulp1 restricts Ulp1 activity towards certain sumoylated proteins while enabling the cleavage of others, the COOH-terminal catalytic domain of Ulp1 is both necessary and sufficient for the essential function of the protein in cell cycle progression and for Smt3 precursor cleavage |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.68 | more |
the enzyme is specifically required for cell cycle progression |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.68 | more |
ELS1, but not ELS1C461S, is capable of cleaving the extension oV the carboxyl terminus of SUMO1 |
Arabidopsis thaliana |
? |
- |
? |
| 3.4.22.68 | more |
PfSENP1 has unique substrate sequence specificity, comparison to human SENPs, mutational analysis, overview |
Plasmodium falciparum |
? |
- |
? |
| 3.4.22.68 | more |
substrate specificities of different SENPS with different SUMOs, wild-types and mutants, very detailed overview. the SENP6 and SENP7 subclass displays a clear proteolytic cleavage preference for SUMO2/3 isoformsm structural determinants, overview. Identification of a unique sequence insertion in the SENP6 and SENP7 subclass that is essential for their proteolytic activity and that forms a more extensive interface with SUMO during the proteolytic reaction. Structure-based comparisons combined with biochemical and mutagenesis analysis reveal Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family. Loop 1 SENP7 interacts with SUMO2. Deconjugation of diSUMO2(D71K) with SENP7 loop 1 mutant constructs, although proteolytic cleavage of diSUMO2(D71K) substrate shows a decrease in the proteolytic activity for all SENP7 constructs tested, including the wild type form. Mutation D71K, on the surface of SUMO2 distant from the cleavage site, can produce marked defects in the proteolytic activity of SENP7, with an approximately loss of 20fold with respect to the diSUMO2 wild type reaction |
Homo sapiens |
? |
- |
? |
| 3.4.22.68 | more |
Ulp1 is responsible for both removing SUMO/Smt3 from specific target proteins and for processing precursor SUMO into its conjugation-competent form. Multiple features in the catalytic domain of Ulp1 affect SUMO interactions, analysis of features of Ulp1 required for substrate targeting, structure-function analysis, overview. D451 is required for targeting of sumoylated proteins and the C580S mutation is required for retention of Ulp1 at the septin ring. Kap121-independent SUMO-targeting information resides in the catalytic domain of Ulp1. The Ulp1 Kap121-interacting domain (region 1), the Ulp1 Kap60/Kap95-interacting domain (region 2) and the catalytic domain (region 3) fail to interact with the Smt3-binding domain |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.68 | more |
Ulp1 liberates poly-Smt3 from a substrate chain. In vitro, Ulp1 is highly active even in very low concentrations. Substrate specificity analysis of immobilized recombinant enzyme, overview |
Saccharomyces cerevisiae |
? |
- |
? |
