PROSITE documentation PDOC00005Protein kinase C phosphorylation site
Description
In vivo, protein kinase C exhibits a preference for the phosphorylation of serine or threonine residues found close to a C-terminal basic residue [1,2]. The presence of additional basic residues at the N- or C-terminal of the target amino acid enhances the Vmax and Km of the phosphorylation reaction.
Last update:June 1988 / First entry.
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Technical section
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References
| 1 | Authors | Woodget J.R. Gould K.L. Hunter T. |
| Source | Eur. J. Biochem. 161:177-184(1986). |
| 2 | Authors | Kishimoto A. Nishiyama K. Nakanishi H. Uratsuji Y. Nomura H. Takeyama Y. Nishizuka Y. |
| Title | Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3':5'-monophosphate-dependent protein kinase. | |
| Source | J. Biol. Chem. 260:12492-12499(1985). | |
| PubMed ID | 2413024 |
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