BAIT

VPH1

H(+)-transporting V0 sector ATPase subunit a, L000002467, YOR270C
Subunit a of vacuolar-ATPase V0 domain; one of two isoforms (Vph1p and Stv1p); Vph1p is located in V-ATPase complexes of the vacuole while Stv1p is located in V-ATPase complexes of the Golgi and endosomes; relative distribution to the vacuolar membrane decreases upon DNA replication stress
Saccharomyces cerevisiae (S288c)
PREY

ATP6V1E2

4930500C14Rik, Atp6e1, E1
ATPase, H+ transporting, lysosomal V1 subunit E2
GO Process (2)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Mus musculus

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

Defective assembly of a hybrid vacuolar H(+)-ATPase containing the mouse testis-specific E1 isoform and yeast subunits.

Hayashi K, Sun-Wada GH, Wada Y, Nakanishi-Matsui M, Futai M

Mammalian vacuolar-type proton pumping ATPases (V-ATPases) are diverse multi-subunit proton pumps. They are formed from membrane V(o) and catalytic V(1) sectors, whose subunits have cell-specific or ubiquitous isoforms. Biochemical study of a unique V-ATPase is difficult because ones with different isoforms are present in the same cell. However, the properties of mouse isoforms can be studied using hybrid V-ATPases formed ... [more]

Biochim. Biophys. Acta Oct. 01, 2008; 1777(10);1370-7 [Pubmed: 18662668]

Throughput

  • Low Throughput

Curated By

  • BioGRID