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Literature summary for 3.4.22.B67 extracted from

  • de Albuquerque, C.P.; Suhandynata, R.T.; Carlson, C.R.; Yuan, W.T.; Zhou, H.
    Binding to small ubiquitin-like modifier and the nucleolar protein Csm1 regulates substrate specificity of the Ulp2 protease (2018), J. Biol. Chem., 293, 12105-12119 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P40537
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
di-SUMO + H2O 25% degradation within 60 min Saccharomyces cerevisiae 2 SUMO
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 ?
hexa-SUMO + H2O 95% degradation within 60 min Saccharomyces cerevisiae SUMO + ?
-
 ?
tetra-SUMO + H2O 55% degradation within 60 min Saccharomyces cerevisiae SUMO + ?
-
 ?

General Information

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