EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.1.137 | more |
no glycosylation |
640936 |
| 2.7.1.137 | more |
proteinase K treatment of partially purified Rickettsia typhi results in a dose-dependent degradation of Risk1 on the bacterial membrane |
-, 761792 |
| 2.7.1.137 | phosphoprotein |
for Vps34, phosphorylation sites within the C2 domain are inhibitory (Thr159, Thr163 and Ser165) as is phosphorylation of Thr668 in the kinase domain. Activating phosphorylation sites are in the C2-helical linker (Tyr231) or in the kinase domain (Tyr310 and Thr667). Inhibitory phosphorylation sites in Atg14 (Ser3, Ser223, Ser233, Ser383 and Ser440) are spread throughout the proteins. Ser90 phosphorylation regulates Vps34 activity |
760521 |
| 2.7.1.137 | phosphoprotein |
highly phosphorylated on both p85a and p110 subunits, and dephosphorylation generates a deactivated complex, indicating that phosphorylation is an important covalent modification of the complex and may modulate PtdIns 3-kinase activity |
640856 |
| 2.7.1.137 | phosphoprotein |
IL-2 stimulation triggers tyrosine phosphorylation of the p85 subunit of PI3-kinase in murine T cell line CTLL-2 |
640889 |
| 2.7.1.137 | phosphoprotein |
p85 subunit is rapidly phosphorylated in response to insulin |
640898 |
| 2.7.1.137 | phosphoprotein |
phosphorylation by tyrosine kinases activates the enzyme |
661892 |
| 2.7.1.137 | phosphoprotein |
PI3-K is activated by phosphorylation through serine/threonine protein kinases |
710074 |
| 2.7.1.137 | phosphoprotein |
purified enzyme complex is highly phosphorylated on both subunits, dephosphorylation generates a deactivated complex |
640856 |
| 2.7.1.137 | phosphoprotein |
putative PI 3-kinase 85000 Da subunit is phosphorylated by pp60vscr |
640854 |
