Protein Variants | Comment | Organism |
---|---|---|
additional information | a triple-Ala mutant of the SUMO-interacting motif SIM does not cause a noticeable growth defect. Contrary to wild-type, the mutant motif does not bind to tetra-SUMO or hexa-SUMO protein conjugates. The mutant significantly reduces Ulp2's SUMO protease activity for all of the linear SUMO substrates | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | P40537 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
di-SUMO + H2O | 25% degradation within 60 min | Saccharomyces cerevisiae | 2 SUMO | - |
? | |
hexa-SUMO + H2O | 95% degradation within 60 min | Saccharomyces cerevisiae | SUMO + ? | - |
? | |
tetra-SUMO + H2O | 55% degradation within 60 min | Saccharomyces cerevisiae | SUMO + ? | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | the C-terminal regulatory domain of Ulp2 contains three distinct conserved motifs that control its in vivo substrate specificity and cell growth. Among them, a SUMO-interacting motif (SIM) coordinates with the domain of Ulp2 that binds to the nucleolar protein Csm1 to ensure maximal deSUMOylation of Ulp2's nucleolar substrates. The Csm1-binding domain of Ulp2 recruits this enzyme to the nucleolus, and Ulp2's C-terminal SIM promotes its SUMO protease activity and plays a key role in mediating the in vivo specificity of Ulp2 | Saccharomyces cerevisiae |