Activating Compound | Comment | Organism | Structure |
---|---|---|---|
phosphatidylinositol 3,4,5-triphosphate | specifically interacts with the phox homology domain of phospholipase D1 and stimulates activity | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
R179A | mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate | Mus musculus |
R179K | mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
NIH-3T3 cell | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1 | Mus musculus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
phospholipase D1 | - |
Mus musculus |
PLD1 | - |
Mus musculus |