EC Number   |
Activating Compound |
Reference |
|---|
   2.7.1.137 | activated PDGFRbeta |
PI3K binding to the cytoplasmic domain of activated PDGFRbeta receptors requires phosphorylation at residues 739 and 750 and this interaction in turn activates the kinase |
710354 |
| 2.7.1.137 | adenosine |
adenosine activates PI3K and induces Akt phosphorylation leading to induction of hemeoxygenase-1, HO-1, expression in microglia. Adenosine acts as an endogenous regulator of brain inflammation via modulation of microglial reactive oxygen species production, mechanism, overview |
708595 |
| 2.7.1.137 | Atg14 |
PAS localization, along with that of the other components of PI3K complex I, requires Atg14 |
707343 |
| 2.7.1.137 | Atg6 |
in the absence of PpAtg6, PpUvrag-GFP as well as PpAtg8 fully mislocalized to the cytosol |
707343 |
| 2.7.1.137 | beta-catenin |
tyrosine-phopshorylated |
708568 |
| 2.7.1.137 | betagamma subunit of heterotrimeric G-proteins |
direct activation, acts synergistically with Ras |
661892 |
| 2.7.1.137 | bone morphogenetic protein-2 |
activates Akt phopshorylation by PI3K. Cell treatment with BMP-2 exhibits dramatic changes in cell morphology, from a cuboid, epithelial-like shape to a spindle, fibroblastic-like appearance, consistent with epithelial-mesenchymal transition, EMT, overview |
708417 |
| 2.7.1.137 | c-Src |
- |
708568 |
| 2.7.1.137 | cAMP |
PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 |
708336 |
| 2.7.1.137 | Dlg |
tyrosine-phopshorylated |
708568 |
