3.1.3.4: phosphatidate phosphatase

This is an abbreviated version!
For detailed information about phosphatidate phosphatase, go to the full flat file.

Reaction

Synonyms

3-sn-phosphatidate phosphohydrolase, acid phosphatidyl phosphatase, APP1, DGPP phosphatase, diacylglycerol diphosphate phosphatase, diacylglycerol pyrophosphate phosphatase, DPP1, Dpp1p, DPPL1, DPPL2, Dri-42, Dri42, ecto-PAPase, ecto-phosphatidic acid phosphohydrolase, EtLPP1, EtLPP2, EtLPP3, Germ cell guidance factor, Ippalpha, Ippbeta, Laza, Lazaro phosphatidic acid phosphatase, lipid phosphate phosphatase, lipid phosphate phosphatase 1, lipid phosphate phosphatase 3, lipid phosphate phosphatase-1, lipid phosphate phosphatase-2, lipid phosphate phosphatase-3, lipid phosphate phosphatase-related protein, lipid phosphate phosphatase-related protein type 1, lipid phosphate phosphatase-related protein type 2, lipid phosphate phosphatase-related protein type 3, lipid phosphate phosphatase-related protein type 4, lipid phosphate phosphohydrolase, lipidphosphatase-related protein 1, lipin, lipin 1, lipin 1beta, lipin 2, lipin 3, lipin Pah1p/Smp2p, lipin-1, lipin-1alpha, lipin-1beta, lipin-1gamma, lipin-2, lipin-3, Lipin1, lipin1alpha, lipin1beta, LLP1, LLP2, LPIN1, LPP, LPP-1, LPP1, LPP1-encoded lipid phosphatase, Lpp1p, LPP2, LPP3, LPPR2, LPR, LPR-1, LPR-2, LPR-3, LPR-4, LPR1, Mg2+-dependent PA1 phosphatase, Mg2+-dependent phosphatidate phosphatase, Mg2+-dependent phosphatidic acid phosphatase, More, PA phosphatase, PA-P, PA-PSP, PA2 phosphatase, PAH, pah1, Pah1p, Pah1p/Smp2p, PAH2, PAP, PAP-1, PAP-2, PAP-2b, PAP1, PAP2, PAP2-like protein, PAP2a, PAP2d, PAP2L2, PAP3, PAPase, phosphatidate phosphatase, phosphatidate phosphatase type-1, phosphatidate phosphatase-1, phosphatidate phosphohydrolase, phosphatidic acid phosphatase, phosphatidic acid phosphatase 2a, phosphatidic acid phosphatase type 2, phosphatidic acid phosphatase-1, phosphatidic acid phosphohydrolase, phosphatidic acid phosphohydrolase 1, phosphatidic acid phosphohydrolase-1, plasticity related gene 1, plasticity related gene 3, plasticity related gene 4, presqualene diphosphate phosphatase, PRG-1, PRG-3, PRG3, RHA1_ro00075, SCO1102, SCO1753, SMP2, type 2b phosphatidic acid phosphatase, wun, wun2, WunD, Wunen, Wunen protein, wunen-2, Wunen2

ECTree

     3 Hydrolases

         3.1 Acting on ester bonds

             3.1.3 Phosphoric-monoester hydrolases

                3.1.3.4 phosphatidate phosphatase

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Results	in table
56	Activating Compound
7412	AA Sequence
12	Application
1	CAS Registry Number
80	Cloned(Commentary)
1184	Disease/ Diagnostics
43	Expression
107	General Information
8	IC50 Value
226	Inhibitors
1	Ki Value [mM]
42	KM Value [mM]
252	Localization
100	Metals/Ions
51	Molecular Weight [Da]
135	Natural Substrates/ Products (Substrates)
345	Organism
15	Pathway
1	PDB ID
54	pH Optimum
10	pH Range
43	Posttranslational Modification
130	Protein Variants
27	Purification (Commentary)
4	Reaction
1	Reaction Type
229	Reference
341	Source Tissue
24	Specific Activity [micromol/min/mg]
3	Storage Stability
393	Substrates and Products (Substrate)
47	Subunits
557	Synonyms
1	Systematic Name
22	Temperature Optimum [°C]
7	Temperature Stability [°C]

Posttranslational Modification

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Posttranslational Modification on EC 3.1.3.4 - phosphatidate phosphatase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

11 entries

phosphoprotein

29 entries

proteolytic modification

Saccharomyces cerevisiae

-

the 91-kDa enzyme is a proteolysis product of a 104-kDa enzyme form, the 104-kDa PA phosphatase is not a precursor of the 45-kDa enzyme form

134878

sumoylation

2 entries

glycoprotein

Drosophila melanogaster

-

N-glycosylation

665805

glycoprotein

Eimeria tenella

A0A0A7H6F4, A0A0A7H9C0, A0A0A7H9U0

the enzyme is partially N-glycosylated

751935

glycoprotein

Homo sapiens

-

the two Mg2+-independent isoenzymes, PAP-2a and PAP-2b are glycoproteins

134884

glycoprotein

Homo sapiens

Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1

N-glycosylation

665805

glycoprotein

Homo sapiens

-

the glycosylation is not required for catalytic activity, no glycosylation of PRG-1

666926

glycoprotein

Mus musculus

-

N-glycosylation

665805

glycoprotein

Mus musculus

-

glycosylation is not required for activity

649679

glycoprotein

Mus musculus

-

the glycosylation is not required for catalytic activity, no glycosylation of PRG-1

666926

glycoprotein

Rattus norvegicus

-

the anionic and the cationic enzyme form are glycoproteins

134885

glycoprotein

Rattus norvegicus

-

N-glycosylation

665805

glycoprotein

Rattus norvegicus

-

the glycosylation is not required for catalytic activity, no glycosylation of PRG-1

666926

phosphoprotein

Bos taurus

-

-

694357

phosphoprotein

Homo sapiens

-

reversible phosphorylation might play a role in enzyme regulation

666926

phosphoprotein

Homo sapiens

Q14693

mitotic phosphorylation of lipin 1 inhibits its phosphatidic acid phosphatase activity

693153

phosphoprotein

Homo sapiens

-

phosphorylation play an important role in modulation of enzyme activity, phosphorylation of lipin-1 influences its subcellular localization, dephosphorylation of lipin-1 in response to oleic acid and epinephrine

693521

phosphoprotein

Homo sapiens

-

insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720

714316

phosphoprotein

Mus musculus

-

reversible phosphorylation might play a role in enzyme regulation

666926

phosphoprotein

Mus musculus

Q91ZP3

identification of fifteen phosphorylation sites by mass spectrometric analysis

680814

phosphoprotein

Mus musculus

-

mitotic phosphorylation of lipin 2 inhibits its phosphatidic acid phosphatase activity

693153

phosphoprotein

Mus musculus

-

phosphorylation plays an important role in modulation of enzyme activity, phosphorylation of lipin-1 and lipin-2 is associated with reduced PAP1 activity druing mitosis, phosphorylation of lipin-1, mainly at Ser106, influences its subcellular localization, dephosphorylation of lipin-1 in response to oleic acid and epinephrine

693521

phosphoprotein

Mus musculus

-

serine 106 residue of lipin-1 and lipin-2 is a major site of phosphorylation

693251

phosphoprotein

Mus musculus

-

insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720

714316

phosphoprotein

Rattus norvegicus

-

reversible phosphorylation might play a role in enzyme regulation

666926

phosphoprotein

Rattus norvegicus

-

phosphorylation plays an important role in modulation of enzyme activity, phosphorylation of lipin-1 influences its subcellular localization, dephosphorylation of lipin-1 in response to oleic acid and epinephrine

693521

phosphoprotein

Saccharomyces cerevisiae

-

-

749525

phosphoprotein

Saccharomyces cerevisiae

P32567

-

751097

phosphoprotein

Saccharomyces cerevisiae

-

lipin is phosphorylated by human Dullard, a protein that participates in a unique phosphatase cascade regulating nuclear membrane biogenesis, and this cascade is conserved from yeast to mammals

682573

phosphoprotein

Saccharomyces cerevisiae

-

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

680711

phosphoprotein

Saccharomyces cerevisiae

-

the 45-kDa PA phosphatase is phosphorylated by protein kinase A, while the purified 104-kDa PA phosphatase is not a substrate, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction

134878

phosphoprotein

Saccharomyces cerevisiae

-

PAP PAH1 is a target for multiplec protein kinases, including cyclin-dependent kinase Cdk1, Pho85, and Dbf2-Mob1. PAP is phosphorylated by Cdk1 in a cell cycle-dependent manner, a purified phosphorylation-deficient Ser/Thr 3 Ala septuple mutant enzyme exhibits elevated PAP activity

693238

phosphoprotein

Saccharomyces cerevisiae

-

phosphorylation, e.g. by Nem1p, plays an important role in modulation of enzyme activity, overview

693521

phosphoprotein

Saccharomyces cerevisiae

P32567

phosphorylation at sites Ser110, Ser114, Ser168, Ser602, Thr723, Ser744, and Ser748 is managed by protein kinase-cyclin complex Pho85p-Pho80p. The phosphorylation of recombinant isoform Pah1p is time- and dose-dependent and dependent on the concentrations of ATP and Pah1p. Phosphorylation reduces the catalytic efficiency 6fold and reduces 3fold its interaction with liposomes. Alanine mutations of the seven sites ablates the inhibitory effect of phosphorylation. Loss of Pho85p-Pho80p phosphorylation reduces Pah1p abundance. Lack of Nem1p-Spo7p, the phosphatase complex that dephosphorylates Pah1p at the nuclear/endoplasmic reticulum membrane, stabilizes Pah1p abundance

729976

phosphoprotein

Saccharomyces cerevisiae

P32567

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

730045

phosphoprotein

Saccharomyces cerevisiae

-

target of rapamycin complex TORC1 inhibits the function of phosphatidate phosphatase Pah1, to prevent the accumulation of triacylglycerol. TORC1 regulates Pah1 in part indirectly by controlling the phosphorylation status of Nem1 within the Pah1-activating, heterodimeric Nem1-Spo7 protein phosphatase module

730766

phosphoprotein

Saccharomyces cerevisiae

-

the enzyme is phosphorylated by cyclin-dependent kinase 1

751022

phosphoprotein

Saccharomyces cerevisiae

-

the enzyme translocates from the cytosol to the nuclear/endoplasmic reticulum membrane through phosphorylation and dephosphorylation

751277

phosphoprotein

Saccharomyces cerevisiae W303-1A

-

-

-

phosphoprotein

Tetrahymena thermophila

-

-

751135

phosphoprotein

Tetrahymena thermophila B2086

-

-

-

phosphoprotein

Tetrahymena thermophila CU428

-

-

-

sumoylation

Homo sapiens

-

isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites

714316

sumoylation

Mus musculus

-

isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites

714316