BAIT
ATP6V1E1
ATP6E, ATP6E2, ATP6V1E, P31, Vma4
ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1
GO Process (7)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
ALDOA
ALDA, GSD12, HEL-S-87p
aldolase A, fructose-bisphosphate
GO Process (16)
GO Function (8)
GO Component (9)
Gene Ontology Biological Process
- ATP biosynthetic process [IMP]
- actin filament organization [TAS]
- blood coagulation [TAS]
- carbohydrate metabolic process [TAS]
- fructose 1,6-bisphosphate metabolic process [IDA]
- fructose metabolic process [IMP]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [IMP, TAS]
- muscle cell cellular homeostasis [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- protein homotetramerization [ISS]
- regulation of cell shape [IDA]
- small molecule metabolic process [TAS]
- striated muscle contraction [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump.
Vacuolar H(+)-ATPases (V-ATPases) are essential for acidification of intracellular compartments and for proton secretion from the plasma membrane in kidney epithelial cells and osteoclasts. The cellular proteins that regulate V-ATPases remain largely unknown. A screen for proteins that bind the V-ATPase E subunit using the yeast two-hybrid assay identified the cDNA clone coded for aldolase, an enzyme of the glycolytic ... [more]
J. Biol. Chem. Aug. 10, 2001; 276(32);30407-13 [Pubmed: 11399750]
Throughput
- Low Throughput
Curated By
- BioGRID