BAIT

SSM4

DOA10, KIS3, E3 ubiquitin-protein ligase SSM4, L000002087, YIL030C
Ubiquitin-protein ligase involved in ER-associated protein degradation; located in the ER/nuclear envelope; ssm4 mutation suppresses mRNA instability caused by an rna14 mutation
Saccharomyces cerevisiae (S288c)
PREY

PDR5

LEM1, STS1, YDR1, ATP-binding cassette multidrug transporter PDR5, L000001365, L000002136, L000002504, YOR153W
Plasma membrane ATP-binding cassette (ABC) transporter; multidrug transporter actively regulated by Pdr1p; also involved in steroid transport, cation resistance, and cellular detoxification during exponential growth; PDR5 has a paralog, PDR15, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (3)

Gene Ontology Molecular Function

Saccharomyces cerevisiae (S288c)

Phenotypic Enhancement

A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Publication

Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.

Stolz A, Besser S, Hottmann H, Wolf DH

Quality control and degradation of misfolded proteins are essential processes of all cells. The endoplasmic reticulum (ER) is the entry site of proteins into the secretory pathway in which protein folding occurs and terminally misfolded proteins are recognized and retrotranslocated across the ER membrane into the cytosol. Here, proteins undergo polyubiquitination by one of the membrane-embedded ubiquitin ligases, in yeast ... [more]

Proc. Natl. Acad. Sci. U.S.A. Sep. 17, 2013; 110(38);15271-6 [Pubmed: 23988329]

Throughput

  • Low Throughput

Ontology Terms

  • protein/peptide accumulation (APO:0000149) [increased (APO:0000004)]

Additional Notes

  • hrd1 doa10 pdr5 triple mutant, in the presence of protease inhibitor MG132, exhibits decreased degradation of a misfolded Ste6 substrate

Curated By

  • BioGRID