BAIT

PRKACA

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

PNPLA2

0610039C21Rik, 1110001C14Rik, Atgl, TTS-2.2
patatin-like phospholipase domain containing 2
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

Identification and functional characterization of protein kinase A phosphorylation sites in the major lipolytic protein, adipose triglyceride lipase.

Pagnon J, Matzaris M, Stark R, Meex RC, Macaulay SL, Brown W, O'Brien PE, Tiganis T, Watt MJ

Catecholamine-stimulated lipolysis occurs by activating adenylate cyclase and raising cAMP levels, thereby increasing protein kinase A (PKA) activity. This results in phosphorylation and modulated activity of several key lipolytic proteins. Adipose triglyceride lipase (ATGL) is the primary lipase for the initial step in triacylglycerol hydrolysis, and ATGL activity is increased during stimulated lipolysis. Here, we demonstrate that murine ATGL is ... [more]

Endocrinology Sep. 01, 2012; 153(9);4278-89 [Pubmed: 22733971]

Throughput

  • Low Throughput

Curated By

  • BioGRID