The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo.
p36, a major in vivo substrate of protein-tyrosine kinases, is shown to be phosphorylated at serine 25, a site very close to the major site of tyrosine phosphorylation by pp60v-src, tyrosine 23 (J. R. Glenney, Jr., and B. F. Tack, Proc. Natl. Acad. Sci. USA 82:7884-7888, 1985). We present evidence suggesting that protein kinase C mediates phosphorylation of serine 25.
D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins; D002417:Cattle; D008565:Membrane Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000032:analysis; D011493:Protein Kinase C / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D013379:Substrate Specificity
D017302:Annexins; D008565:Membrane Proteins; D010750:Phosphoproteins; D011505:Protein-Tyrosine Kinases; D011493:Protein Kinase C