1.13.99.1 | phosphoprotein |
mutants with substituted phosphorylation sites have a minimal increase in activity. Treatment of cells with PKC, PKA, and PDK1 kinase activators increased activity, whereas inhibitors reduced it. Protein kinases A, C, and PDK1 are capable of phosphorylating mouse in both prokaryotic and eukaryotic systems. Using deletion constructs it is shown that the N-terminus contains the critical phosphorylation sites that are highly relevant to the functionality of the protein |
727881 |