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Literature summary for extracted from

  • Cohen, I.; Wiener, R.; Reiss, Y.; Ravid, T.
    Distinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases (2015), Proc. Natl. Acad. Sci. USA, 112, E625-E632.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K118R residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates Saccharomyces cerevisiae


Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q02159


Synonyms Comment Organism
Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function residues within helix alpha2 of Ubc7 that interact with donor ubiquitin are essential for polyubiquitin conjugation by Ubc7 and its cognate E3 enzymes. Mutagenesis of these residues inhibits the in vitro activity of Ubc7 by preventing the conjugation of donor ubiquitin to the acceptor. Ubiquitin chain formation by mutant Ubc7 is restored selectively by the E3 enzyme Hrd1 RING domain but not by the E3 enzyme Doa10 RING domain. alpha2 Helix mutations selectively impair the in vivo degradation of Doa10 substrates but have no apparent effect on the degradation of Hrd1 substrates Saccharomyces cerevisiae