BAIT

PRKACA

PKCD, Pkaca
protein kinase, cAMP dependent, catalytic, alpha
GO Process (20)
GO Function (10)
GO Component (16)
Mus musculus
PREY

ATP6V1A

AI647066, Atp6a1, Atp6a2, Atp6v1a1, VA68, VPP2
ATPase, H+ transporting, lysosomal V1 subunit A
Mus musculus

Biochemical Activity (Phosphorylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

PKA regulates vacuolar H+-ATPase localization and activity via direct phosphorylation of the a subunit in kidney cells.

Alzamora R, Thali RF, Gong F, Smolak C, Li H, Baty CJ, Bertrand CA, Auchli Y, Brunisholz RA, Neumann D, Hallows KR, Pastor-Soler NM

The vacuolar H(+)-ATPase (V-ATPase) is a major contributor to luminal acidification in epithelia of Wolffian duct origin. In both kidney-intercalated cells and epididymal clear cells, cAMP induces V-ATPase apical membrane accumulation, which is linked to proton secretion. We have shown previously that the A subunit in the cytoplasmic V(1) sector of the V-ATPase is phosphorylated by protein kinase A (PKA). ... [more]

J. Biol. Chem. Aug. 06, 2010; 285(32);24676-85 [Pubmed: 20525692]

Throughput

  • Low Throughput

Additional Notes

  • Bait species unknown.

Curated By

  • BioGRID