BAIT

VMA11

CLS9, TFP3, H(+)-transporting V0 sector ATPase subunit c', L000002290, L000002464, YPL234C
Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen
GO Process (1)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

VMA16

PPA1, H(+)-transporting V0 sector ATPase subunit c'', L000001468, YHR026W
Subunit c'' of the vacuolar ATPase; v-ATPase functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain
GO Process (1)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)

Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Publication

VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase.

Hirata R, Graham LA, Takatsuki A, Stevens TH, Anraku Y

The vacuolar membrane H+-ATPase (V-ATPase) of the yeast Saccharomyces cerevisiae is composed of peripheral catalytic (V1) and integral membrane (V0) domains. The 17-kDa proteolipid subunit (VMA3 gene product; Vma3p) is predicted to constitute at least part of the proton translocating pore of V0. Recently, two VMA3 homologues, VMA11 and VMA16 (PPA1), have been identified in yeast, and VMA11 has been ... [more]

J. Biol. Chem. Feb. 21, 1997; 272(8);4795-803 [Pubmed: 9030535]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
VMA11 VMA16
Synthetic Lethality
Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Low-BioGRID
643019

Curated By

  • BioGRID