We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00005Protein kinase C phosphorylation site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00005
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
PROSITE method (with tools and information) covered by this documentation:
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 |
Copyright
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