Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant PTEN in Spodoptera fruiperda Sf9 cells | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C124S | site-directed mutagenesis, inactive mutant | Homo sapiens |
D92A | site-directed mutagenesis, the D92A mutation causes a 250 to 700fold reduction in phospholipid phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN | Homo sapiens |
G129E | naturally occuring mutation, the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN, complete loss of phospholipid phosphatase activity of the G129E PTEN mutant | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analyses of the effects of D92A and G129E mutations on the phospholipid and phosphoprotein phosphatase activities of PTEN | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | PTEN phosphoprotein phosphatase catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys124 transiently phosphorylated to form the phosphoenzyme intermediate | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation, possibly at Ser380, Thr382 and Thr383 at the C-terminal tail suppresses the activity of PTEN and D92A PTEN, dephosphorylation of recombinant wild-type PTEN and D92A PTEN leaads to a 2-5 fold increase in phosphatase activity. PTEN reacts with pY-SOP to form a phospho-PTEN protein. The phosphoPTEN protein is not the cysteinyl phosphoenzyme intermediate formed by transient phosphorylation of Cys124 in the course of phosphopeptide dephosphorylation reaction | Homo sapiens |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant PTEN from Spodoptera fruiperda Sf9 cells by anion exchange chromatography | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | PTEN phosphoprotein phosphatase catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys124 transiently phosphorylated to form the phosphoenzyme intermediate | Homo sapiens | ? | - |
? | |
additional information | Ser380, Thr382 and Thr383 C-terminal tail residues do not affect the recruitment of the WPD-loop into the active site to participate in the phosphoprotein dephosphorylation reaction, catalytic mechanism of PTEN phosphoprotein phosphatase activity, overview. The phosphoPTEN protein is not the cysteinyl phosphoenzyme intermediate formed by transient phosphorylation of Cys124 in the course of phosphopeptide dephosphorylation reaction. PTEN can adopt the closed conformation to allow Asp92 to participate in catalysis when it dephosphorylates the physiological protein substrates such as FAK and Shc in cells | Homo sapiens | ? | - |
? | |
protein FAK + H2O | - |
Homo sapiens | ? | - |
? | |
protein Shc + H2O | - |
Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
protein tyrosine phosphatase | - |
Homo sapiens |
PTEN phosphoprotein phosphatase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN | Homo sapiens |