EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.1.67 | lipoprotein |
isozyme PI4KIIalpha exists almost exclusively as a constitutively active integral membrane protein because of its palmitoylation |
722700 |
| 2.7.1.67 | lipoprotein |
PI4KIIbeta and PI4KIIalpha are palmitoylated |
723790 |
| 2.7.1.67 | more |
PI4KIIalpha undergoes multi-ubiquitination via ubiquitin ligase Itch |
722121 |
| 2.7.1.67 | phosphoprotein |
14-3-3 proteins bind isoform PI4KB upon its phosphorylation by protein kinase D. 14-3-3 proteins protect isoform PI4KB from proteolytic degradation in vitro |
759678 |
| 2.7.1.67 | phosphoprotein |
enzyme exhibits autophosphorylation that is enhanced by Mn2+ ions. Isolated C-terminal catalytic domain still displays autophosphorylation. Phosphorylation of endogenous or overexpressed PI4Kbeta is also observed in COS-7 cells |
641810 |
| 2.7.1.67 | phosphoprotein |
isozyme PI4KIIIbeta can be activated by protein kinase D phosphorylation |
721967 |
| 2.7.1.67 | phosphoprotein |
phosphoprotein, additionally phosphate is incorporated by incubation with ATP/Mg or ATP/Mn. Phosphorylation sites are mapped by MALDI-MS and LC-MS/MS at the following positions: S258, T263, S266, S277, S294, T423, S496, T504 |
641808 |
| 2.7.1.67 | phosphoprotein |
the enzyme is an integral component of the early signal transduction machinery during T-cell activation by concanavalin A and is actively regulated by protein tyrosine phosphorylation-dephosphorylation |
641807 |
| 2.7.1.67 | phosphoprotein |
the enzyme is phosphorylated at S294 in order to interact with 14-3-3 protein |
760185 |
| 2.7.1.67 | phosphoprotein |
yeast Pik1 is phosphorylated by a protein kinase, phosphorylation promotes dissociation of Pik1 from Golgi membranes and association with the 14-3-3 proteins Bmh1 and Bmh2 in the cytosol |
723791 |
