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Literature summary for 3.4.22.68 extracted from

  • Peek, J.; Harvey, C.; Gray, D.; Rosenberg, D.; Kolla, L.; Levy-Myers, R.; Yin, R.; McMurry, J.; Kerscher, O.
    SUMO targeting of a stress-tolerant Ulp1 SUMO protease (2018), PLoS ONE, 13, e0191391 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.68

Cloned(Commentary)

Cloned (Comment) Organism
expresssion in Escherichia coli Kluyveromyces marxianus

Protein Variants

Protein Variants Comment Organism
C517S catalytically inactive Kluyveromyces marxianus

Organism

Organism UniProt Comment Textmining
Kluyveromyces marxianus
-
-
-
Kluyveromyces marxianus BY28356
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-
-
Saccharomyces cerevisiae
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-
-

General Information

General Information Comment Organism
physiological function the catalytic UD domains of both Saccharomyces cerevisiae ScUlp1 and Kluyveromyces marxianus KmUlp1 show a high degree of sequence conservation, complement a Ulp1 deletion mutant in vivo, and process a SUMO precursor in vitro. Catalytically inactive recombinant fragments of the UD domains are able to efficiently bind a variety of purified SUMO isoforms and bind immobilized SUMO1 with nanomolar affinity Saccharomyces cerevisiae
physiological function the catalytic UD domains of both Saccharomyces cerevisiae ScUlp1 and Kluyveromyces marxianus KmUlp1 show a high degree of sequence conservation, complement a Ulp1 deletion mutant in vivo, and process a SUMO precursor in vitro. Catalytically inactive recombinant fragments of the UD domains are able to efficiently bind a variety of purified SUMO isoforms and bind immobilized SUMO1 with nanomolar affinity Kluyveromyces marxianus