PROSITE documentation PDOC00100Protein kinases signatures and profile
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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PURL: https://purl.expasy.org/prosite/documentation/PDOC00100
PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Hanks S.K. Hunter T. |
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 |
6 | Authors | Knighton D.R. Zheng J.H. Ten Eyck L.F. Ashford V.A. Xuong N.-H. Taylor S.S. Sowadski J.M. |
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 |
10 | Authors | Littler E. Stuart A.D. Chee M.S. |
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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