Literature summary for 2.3.2.27 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.

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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

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	-	Saccharomyces cerevisiae	5783	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P40318	-	-
Saccharomyces cerevisiae	Q08109	-	-

Synonyms

Synonyms	Comment	Organism
Der3	-	Saccharomyces cerevisiae
ERAD-associated E3 ubiquitin-protein ligase DOA10	-	Saccharomyces cerevisiae
ERAD-associated E3 ubiquitin-protein ligase HRD1	-	Saccharomyces cerevisiae
SSM4	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
physiological function	in vivo degradation of substrates for integral endoplasmic reticulum membrane E3 ubiquitin ligase Doa10 is inhibitied by mutations in the alpha2 helix of E2 enzyme Ubc7 by preventing the conjugation of donor ubiquitin to the acceptor. Ubiquitin chain formation by mutant Ubc7 is not restored by the E3 enzyme Doa10 RING domain. alpha2 Helix mutations selectively impair the in vivo degradation of Doa10 substrates	Saccharomyces cerevisiae
physiological function	in vivo degradation of substrates for integral endoplasmic reticulum membrane E3 ubiquitin ligase Hrd1 is not impaired by mutations within helix alpha2 of ubiquitin-conjugating enzyme Ubc7. Ubiquitin-chain formation by mutant Ubc7 is restored selectively by the E3 enzyme Hrd1 RING domain	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)