Literature summary for 3.1.3.4 extracted from

O'Hara, L.; Han, G.S.; Peak-Chew, S.; Grimsey, N.; Carman, G.M.; Siniossoglou, S.
Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase (2006), J. Biol. Chem., 281, 34537-34548.

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Protein Variants

Protein Variants	Comment	Organism
S110A/S114A/S168A/S602A/T723A/S744A/S748A	site-directed mutagenesis, phosphorylation of the mutant is completely abolished	Saccharomyces cerevisiae
S168A/S602A/T723A/S744A/S748A	site-directed mutagenesis, the mutant shows reduce dphosphorylation	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	several strains, overview	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	Pah1p is phosphorylated in vivo, phosphorylation is required for the efficient transcriptional derepression of key enzymes involved in phospholipid biosynthesis, the phosphorylation-deficient Pah1p exhibits higher phosphatidic acid phosphatase-specific activity than the wild-type Pah1p, indicating that phosphorylation of Pah1p at residues S110, S114, S168, S602, T723, S744, and S748 controls phosphatidic production	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
lipin Pah1p/Smp2p	-	Saccharomyces cerevisiae
Mg2+-dependent phosphatidate phosphatase	-	Saccharomyces cerevisiae
PA phosphatase	-	Saccharomyces cerevisiae
Pah1p	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)