EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.4.11 | lipoprotein |
TcPI-PLC is lipid modified in vivo, TcPI-PLC contains an N-myristoylation consensus sequence at its N-terminal end and is modified by myristate and palmitate, myristoyl group may play an important role in the association of enzyme with the plasma membrane |
652082 |
| 3.1.4.11 | phosphoprotein |
an early increase in PLC-beta1b activity (6 h after partial hepatectomy) in nuclear matrix is associated with serine phosphorylation of the enzyme |
668594 |
| 3.1.4.11 | phosphoprotein |
increased phosphorylation of nuclear PLCbeta1, due to nuclear translocation of MAP kinase, is required for the activation of the nuclear inositol lipid cycle in 3T3 cells treated with insulin-like growth factor 1 |
649261 |
| 3.1.4.11 | phosphoprotein |
phosphorylation of nuclear PLC-beta1b on serine occurs at the G2/M and the late G1 phase and is necessary for the progression of the cells through the cell cycle |
667801 |
| 3.1.4.11 | phosphoprotein |
PLC-gamma1 and 2, tyrosine phosphorylation activates enzyme |
649330 |
| 3.1.4.11 | phosphoprotein |
PLC-gamma1, phosphorylation sites: Tyr-771 and Tyr-783 |
653442 |
| 3.1.4.11 | phosphoprotein |
PLC-gamma2 is phosphorylated on Y753, Y759, and Y1271 in response to engagement of the B-cell receptor in Ramos cells. In Ramos cells stimulated maximally with this receptor, the extent of phosphorylation of Y1217 is three times that of Y753 or of Y759. Stimulation of Jurkat cells or platelets via their immunoreceptors elicites phosphorylation of Y753 and Y759 but not that of Y1217. A basal level of phosphorylation of Y753 is apparent in unstimulated lymphocytes. The extent of phosphorylation of Y753 and Y759, but not that of Y1217 correlates with the lipase activity of PLC-gamma2. Btk is largely, but not completely, responsible for phosphorylation of Y753 and Y759, whereas phosphorylation of Y1217 is independent of Btk. Phosphorylation of Y1217 and that of Y753 and Y759 occurs on different PLC-gamma2 molecules |
670242 |
| 3.1.4.11 | phosphoprotein |
PLC-gamma2 is phosphorylated on Y753, Y759, and Y1271 in response to engagement of the B-cell receptor in spleenic cells. In spleenic cells stimulated maximally with this receptor, the extent of phosphorylation of Y1217 is three times that of Y753 or of Y759 |
670242 |
| 3.1.4.11 | phosphoprotein |
PLCgamma2, phosphorylation in response to B-cell antigen receptor stimulation or H2O2 stress, phosphorylation of Tyr-753 and Tyr-759 activates enzyme |
649762 |
| 3.1.4.11 | phosphoprotein |
stimulation of PLCgamma2 activity by tyrosine phosphorylation, multiple phosphorylation sites, the kinase Btk phosphorylates recombinant PLCgamma2 in vitro, Tyr-753 and Tyr-759 are essential for PLCgamma2 function in B-cells, preferential phosphorylation of Tyr-753 over Tyr-759 |
652208 |
