EC Number   |
Natural Substrates |
|---|
   2.7.1.149 | ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate |
- |
| 2.7.1.149 | ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate |
5' phosphorylation |
| 2.7.1.149 | ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate |
- |
| 2.7.1.149 | ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate |
the enzyme may have an important role in synthesis of phosphatidylinositol bisphosphate in the endoplasmic reticulum |
| 2.7.1.149 | ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate |
type II PIP kinases are physiological targets for protein kinase D phosphorylation. This modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases |
| 2.7.1.149 | more |
although PIP4K II generates PI-4,5-P2, a substrate for PI3K, expression of this enzyme reduces rather than increases phosphatidylinositol-3,4,5-trisphosphate (PI-3,4,5-P3) levels in cells stimulated with insulin or cells expressing activated PI3K, this reduction in PI-3,4,5-P3 levels results in decreased activation of the downstream protein kinase Akt/PKB, expression of IpgD, a bacterial phosphatase that converts PI-4,5-P2 to PI-5-P, results in Akt activation, and this effect is partially reversed by PIP4K IIbeta, PIP4K IIbeta expression does not impair insulin-dependent association of PI3K with insulin receptor substrate 1 IRS1 but abbreviates Akt activation, indicating that PIP4K II regulates PI-3,4,5-P3 degradation rather than synthesis |
| 2.7.1.149 | more |
isozyme PIP4Kbeta interacts in vitro and in vivo with the PIP4Kalpha isoform. PIP4Kbeta has 2000fold less activity towards 1-phosphatidyl-1D-myo-inositol 5-phosphate compared with PIP4Kalpha, the majority of enzyme activity associated with PIP4Kbeta comes from its interaction with PIP4Kalpha |
