Phosphorylation of ras oncogene product by protein kinase C.
The Harvey (H)-ras oncogene product, p21, can be phosphorylated by protein kinase C in vitro at sites distinct from the site of autophosphorylation of p21. Serine was found to be the main phosphate acceptor. Kinetic studies revealed a high apparent affinity but a much lower turnover for the phosphorylation of p21 as compared with that of the phosphorylation of histone by protein kinase C. Indirect association between protein kinase C and p21 was suggested by the co-immunoprecipitation of both proteins with either anti-protein kinase C or anti-p21 antibodies.
D000818:Animals; D007700:Kinetics; D051379:Mice; D015689:Oncogene Protein p21(ras); D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D013379:Substrate Specificity
D009856:Oncogene Proteins, Viral; D011493:Protein Kinase C; D015689:Oncogene Protein p21(ras)