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 PDOC00006Casein kinase II phosphorylation site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00006
Description
Casein kinase II (CK-2) is a protein serine/threonine kinase whose activity is independent of cyclic nucleotides and calcium. CK-2 phosphorylates many different proteins. The substrate specificity [1] of this enzyme can be summarized as follows:
(1) Under comparable conditions Ser is favored over Thr.
(2) An acidic residue (either Asp or Glu) must be present three residues from
the C-terminal of the phosphate acceptor site.
(3) Additional acidic residues in positions +1, +2, +4, and +5 increase the
phosphorylation rate. Most physiological substrates have at least one
acidic residue in these positions.
(4) Asp is preferred to Glu as the provider of acidic determinants.
(5) A basic residue at the N-terminal of the acceptor site decreases the
phosphorylation rate, while an acidic one will increase it.
Note:
This pattern is found in most of the known physiological substrates.
Last update:May 1991 / Text revised.
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Technical section
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Reference
| 1 | Authors | Pinna L.A. |
| Title | Casein kinase 2: an 'eminence grise' in cellular regulation? | |
| Source | Biochim. Biophys. Acta 1054:267-284(1990). | |
| PubMed ID | 2207178 |
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