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 PDOC00100Protein kinases signatures and profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00100
Eukaryotic protein kinases [1,2,3,4,5] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common to both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. We have selected two of these regions to build signature patterns. The first region, which is located in the N-terminal extremity of the catalytic domain, is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. The second region, which is located in the central part of the catalytic domain, contains a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [6]; we have derived two signature patterns for that region: one specific for serine/ threonine kinases and the other for tyrosine kinases. We also developed a profile which is based on the alignment in [1] and covers the entire catalytic domain.
Note:If a protein analyzed includes the two protein kinase signatures, the probability of it being a protein kinase is close to 100%
Note:Eukaryotic-type protein kinases have also been found in prokaryotes such as Myxococcus xanthus [11] and Yersinia pseudotuberculosis.
Note:The patterns shown above has been updated since their publication in [7].
Expert(s) to contact by email: Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
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| Title | Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. | |
| Source | FASEB J. 9:576-596(1995). | |
| PubMed ID | 7768349 |
| 2 | Authors | Hunter T. |
| Title | Protein kinase classification. | |
| Source | Methods Enzymol. 200:3-37(1991). | |
| PubMed ID | 1835513 |
| 3 | Authors | Hanks S.K. Quinn A.M. |
| Title | Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. | |
| Source | Methods Enzymol. 200:38-62(1991). | |
| PubMed ID | 1956325 |
| 4 | Authors | Hanks S.K. |
| Source | Curr. Opin. Struct. Biol. 1:369-383(1991). |
| 5 | Authors | Hanks S.K. Quinn A.M. Hunter T. |
| Title | The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. | |
| Source | Science 241:42-52(1988). | |
| PubMed ID | 3291115 |
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| Title | Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. | |
| Source | Science 253:407-414(1991). | |
| PubMed ID | 1862342 |
| 7 | Authors | Bairoch A. Claverie J.-M. |
| Title | Sequence patterns in protein kinases. | |
| Source | Nature 331:22-22(1988). | |
| PubMed ID | 3340146 | |
| DOI | 10.1038/331022a0 |
| 8 | Authors | Benner S. |
| Source | Nature 329:21-21(1987). |
| 9 | Authors | Kirby R. |
| Title | Evolutionary origin of aminoglycoside phosphotransferase resistance genes. | |
| Source | J. Mol. Evol. 30:489-492(1990). | |
| PubMed ID | 2165531 |
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| Source | Nature 358:160-162(1992). |
| 11 | Authors | Munoz-Dorado J. Inouye S. Inouye M. |
| Source | Cell 67:995-1006(1991). |
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