BAIT

PEP4

PHO9, PRA1, yscA, proteinase A, L000001375, YPL154C
Vacuolar aspartyl protease (proteinase A); required for posttranslational precursor maturation of vacuolar proteinases; important for protein turnover after oxidative damage; plays a protective role in acetic acid induced apoptosis; synthesized as a zymogen, self-activates
GO Process (4)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

CUE1

KIS4, L000003518, YMR264W
Ubiquitin-binding protein; endoplasmic reticulum membrane protein that recruits the ubiquitin-conjugating enzyme Ubc7p to the ER where it functions in protein degradation; contains a CUE domain that binds ubiquitin to facilitate intramolecular monoubiquitination; CUE1 has a paralog, CUE4, that arose from the whole genome duplication
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

Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control.

Wang S, Ng DT

In the endoplasmic reticulum (ER), most newly synthesized proteins are retained by quality control mechanisms until folded. Misfolded molecules are sorted to ER-associated degradation (ERAD) pathways for disposal. Reports of mutant proteins degraded in the vacuole/lysosome suggested an independent Golgi-based mechanism also at work. Although little is understood of the post-ER pathway, the growing number of variants using it suggests ... [more]

Mol. Biol. Cell Apr. 01, 2010; 21(7);1153-65 [Pubmed: 20130083]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: protein/peptide modification (APO:0000131)

Additional Notes

  • double mutants show impaired protein degradation

Curated By

  • BioGRID