Literature summary for 3.1.3.4 extracted from

Su, W.M.; Han, G.S.; Carman, G.M.
Cross-talk phosphorylations by protein kinase C and Pho85p-Pho80p protein kinase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae (2014), J. Biol. Chem., 289, 18818-18830.

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P32567	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	residues Ser677, Ser769, Ser773, and Ser788 are major sites of phosphorylation by protein kinase C. Prephosphorylation with protein kinase C reduces Pah1p subsequent phosphorylation with protein kinase A and vice versa. Prephosphorylation with kinase Pho85p-Pho80p has an inhibitory effect on its subsequent phosphorylation with protein kinase C. Prephosphorylation with protein kinase C has no effect on the subsequent phosphorylation with Pho85p-Pho80p	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
metabolism	isoform Pah1p is a bona fide substrate of protein kinase C. The phosphorylation reaction is time- and dose-dependent and dependent on the concentrations of ATP and Pah1p. The stoichiometry of the reaction is 0.8 mol of phosphate/mol of Pah1p. Unlike its phosphorylations by Pho85p-Pho80p and protein kinase A, which cause a significant reduction in phosphatidate phosphatase activity, the phosphorylation of Pah1p by protein kinase C has a small stimulatory effect on the enzyme activity. Protein kinase C does not have a major effect on Pah1p location or its function in triacylglycerol synthesis	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)