Due to maintenance work, this service will not be available Thursday August 21st between 7am and 8am CEST.
PROSITE documentation PDOC00100

Protein kinases signatures and profile




Description

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:

Hunter T.
Quinn A.M.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PROTEIN_KINASE_DOM, PS50011; Protein kinase domain profile  (MATRIX)

PROTEIN_KINASE_ATP, PS00107; Protein kinases ATP-binding region signature  (PATTERN)

PROTEIN_KINASE_ST, PS00108; Serine/Threonine protein kinases active-site signature  (PATTERN)

PROTEIN_KINASE_TYR, PS00109; Tyrosine protein kinases specific active-site signature  (PATTERN)


References

1AuthorsHanks S.K., Hunter T.
TitleProtein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.
SourceFASEB J. 9:576-596(1995).
PubMed ID7768349

2AuthorsHunter T.
TitleProtein kinase classification.
SourceMethods Enzymol. 200:3-37(1991).
PubMed ID1835513

3AuthorsHanks S.K., Quinn A.M.
TitleProtein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members.
SourceMethods Enzymol. 200:38-62(1991).
PubMed ID1956325

4AuthorsHanks S.K.
SourceCurr. Opin. Struct. Biol. 1:369-383(1991).

5AuthorsHanks S.K., Quinn A.M., Hunter T.
TitleThe protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
SourceScience 241:42-52(1988).
PubMed ID3291115

6AuthorsKnighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.-H., Taylor S.S., Sowadski J.M.
TitleCrystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
SourceScience 253:407-414(1991).
PubMed ID1862342

7AuthorsBairoch A., Claverie J.-M.
TitleSequence patterns in protein kinases.
SourceNature 331:22-22(1988).
PubMed ID3340146
DOI10.1038/331022a0

8AuthorsBenner S.
SourceNature 329:21-21(1987).

9AuthorsKirby R.
TitleEvolutionary origin of aminoglycoside phosphotransferase resistance genes.
SourceJ. Mol. Evol. 30:489-492(1990).
PubMed ID2165531

10AuthorsLittler E., Stuart A.D., Chee M.S.
SourceNature 358:160-162(1992).

11AuthorsMunoz-Dorado J., Inouye S., Inouye M.
SourceCell 67:995-1006(1991).



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)