BAIT

VMA1

CLS8, TFP1, H(+)-transporting V1 sector ATPase subunit A, L000002289, YDL185W
Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner
Saccharomyces cerevisiae (S288c)
PREY

YND1

APY1, YEJ5, S000007428, YER005W
Apyrase with wide substrate specificity; helps prevent inhibition of glycosylation by hydrolyzing nucleoside tri- and diphosphates that inhibit glycotransferases; partially redundant with Gda1p; mediates adenovirus E4orf4-induced toxicity
GO Process (1)
GO Function (2)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Dosage Lethality

A genetic interaction is inferred when over expression or increased dosage of one gene causes lethality in a strain that is mutated or deleted for another gene.

Publication

Regulation of yeast ectoapyrase ynd1p activity by activator subunit Vma13p of vacuolar H+-ATPase.

Zhong X, Malhotra R, Guidotti G

CD39-like ectoapyrases are involved in protein and lipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae. By using a two-hybrid screen, we found that an activator subunit (Vma13p) of yeast vacuolar H(+)-ATPase (V-ATPase) binds to the cytoplasmic domain of Ynd1p, a yeast ectoapyrase. Interaction of Ynd1p with Vma13p was demonstrated by direct binding and co-immunoprecipitation. Surprisingly, the membrane-bound ADPase activity ... [more]

J. Biol. Chem. Nov. 10, 2000; 275(45);35592-9 [Pubmed: 10954728]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID