EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.6.5.1 | lipoprotein |
alpha subunits alphao, alphai and alphaz are myristoylated at the N-terminal Gly, alphas and alphaq are not myristoylated. Myristoylation is necessary for membrane attachment and facilitates binding of betagamma. It is an irreversible covalent modification and does not serve a regulatory role. Some alpha subunits are palmitoylated at Cys2. Palmitoylation is reversible. Activation of the beta-adrenergic receptor leads to rapid depalmitoylation of alphas, and depalmitoylated alphas does not activate adenylyl cyclase. Depalmitoylation might be a mechanism to turn off alphas and to sensitize the cell to beta-adrenergic stimulation |
644110 |
| 3.6.5.1 | lipoprotein |
both Galpha12 and 13 are subjected to palmitoylation at cysteine residues near their N-terminus, palmitoylation of Galpha13 is required for its association with the plasma membrane and its ability to activate RhoA through p115RhoGEF. Palmitoylated Galpha12 but not Galpha13 localizes in lipid rafts |
719765 |
| 3.6.5.1 | lipoprotein |
most Galpha subunits, excluding alphat, are S-palmitoylated at one or more Cys near the amino terminus, others, alphao, alphaz, alphai and alphat are N-myristoylated at Gly2 as well. Lipid modifications help bind alpha subunits to the plasma membrane, juxtaposing them to their cognate receptors and effector targets |
644102 |
| 3.6.5.1 | lipoprotein |
N-terminal palmitoylation and myristoylation of GmGa proteins |
720561 |
| 3.6.5.1 | more |
Galpha12 and Galpha13 are not myristoylated because they lack a glycine residue as the second amino acid residue |
719765 |
| 3.6.5.1 | phosphoprotein |
phosphorylation of Galpha subunits is an important modification that regulates their function. Galpha12 is a substrate for phosphorylation by protein kinase C. Endogenous Ga12 in human platelets is phosphorylated within the first 50 N-terminal amino acid residues in response to PMA, thrombin and the TXA2 receptor agonist U46619. Phosphorylated Galpha12 loses its affinity for Gbetagamma, and the association with Gbetagamma reciprocally inhibits the phosphorylation of Ga12 by protein kinase C. Endogenous Galpha13 in platelets is phosphorylated in response to PMA, although not in vitro. PKC-mediated phosphorylation of Ga13 in cell might require additional factors |
719765 |
| 3.6.5.1 | phosphoprotein |
role of Nod factor receptor 1 (NFR1)-mediated phosphorylation in regulation of the G-protein cycle during nodulation in soybean |
757967 |
| 3.6.5.1 | side-chain modification |
betagamma subunit can be phosphorylated on His residues |
644110 |
| 3.6.5.1 | side-chain modification |
protein kinase K-like kinase phosphorylates G36 protein. The phosphorylation of G36 increases its Km for GTP by about 8fold without modification of Vmax. No significant modification after phosphorylation of G50 by protein kinase C or cAMP kinase |
644107 |
| 3.6.5.1 | side-chain modification |
subunits alphai-2 and alphaz can be phosphorylated on Ser or Thr in vivo and in vitro. Several types of subunits can be phosphorylated in vitro on Tyr residues by pp60c-src or by insulin receptor, changes in activity upon phosphorylation are modest at best |
644110 |
