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Research → Protein kinase superfamily

This superfamily includes the Serine/Threonine- and Tyrosine- protein kinases as well as related kinases that act on non-protein substrates.

This clan contains 17 families and the total number of domains in the clan is 115925. The clan was built by DJ Studholme.

Literature references

  1. Hanks SK, Quinn AM; Methods Enzymol 1991; 200:38-62. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. 1956325
  2. Hanks SK, Hunter T; FASEB J 1995; 9:576-596. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. 7768349
  3. Hunter T, Plowman GD; Trends Biochem Sci 1997; 22:18-22. The protein kinases of budding yeast: six score and more. 9020587

Members

This clan contains the following 17 member families:

ABC1 APH APH_6_hur Choline_kinase DUF1679 DUF2252 EcKinase Fructosamin_kin Kdo Pkinase Pkinase_Tyr Pox_ser-thr_kin RIO1 Seadorna_VP7 UL97 WaaY YrbL-PhoP_reg

InterPro entry IPR017442

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [PUBMED:3291115]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specific protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function has been evolutionarily conserved from Escherichia coli to human [PUBMED:12471243]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [PUBMED:12368087]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [PUBMED:15078142], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [PUBMED:15320712].

Eukaryotic protein kinases [PUBMED:12734000, PUBMED:7768349, PUBMED:1835513, PUBMED:1956325, PUBMED:3291115] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [PUBMED:1862342]. This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.

Gene Ontology

Molecular function

ATP binding (GO:0005524)

protein kinase activity (GO:0004672)

Biological process

protein phosphorylation (GO:0006468)

PDB structures for Pfam kinase member families

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Pfam Run Query at RCBS PDB / PDBsum / PDB europe / Pfam
Pfam link: PF04655 RCBS PDB Run Query Now (3 structures hits)
PDBsum Run Query Now (0 structures hits)
PDBeurope Run Query Now (0 structures hits)
Pfam Run Query Now (0 structures hits)
Pfam link: PF01633 RCBS PDB Run Query Now (24 structures hits)
PDBsum Run Query Now (16 structures hits)
PDBeurope Run Query Now (15 structures hits)
Pfam Run Query Now (9 structures hits)
Pfam link: PF02958 RCBS PDB Run Query Now (18 structures hits)
PDBsum Run Query Now (0 structures hits)
PDBeurope Run Query Now (0 structures hits)
Pfam Run Query Now (0 structures hits)
Pfam link: PF03881 RCBS PDB Run Query Now (2 structures hits)
PDBsum Run Query Now (3 structures hits)
PDBeurope Run Query Now (2 structures hits)
Pfam Run Query Now (2 structures hits)
Pfam link: PF06293 RCBS PDB Run Query Now (456 structures hits)
PDBsum Run Query Now (3 structures hits)
PDBeurope Run Query Now (0 structures hits)
Pfam Run Query Now (0 structures hits)
Pfam link: PF00069 RCBS PDB Run Query Now (2472 structures hits)
PDBsum Run Query Now (2301 structures hits)
PDBeurope Run Query Now (1898 structures hits)
Pfam Run Query Now (1061 structures hits)
Pfam link: PF07714 RCBS PDB Run Query Now (2345 structures hits)
PDBsum Run Query Now (1069 structures hits)
PDBeurope Run Query Now (652 structures hits)
Pfam Run Query Now (348 structures hits)
Pfam link: PF01163 RCBS PDB Run Query Now (62 structures hits)
PDBsum Run Query Now (10 structures hits)
PDBeurope Run Query Now (9 structures hits)
Pfam Run Query Now (14 structures hits)
Pfam link: PF07387 RCBS PDB Run Query Now (3 structures hits)
PDBsum Run Query Now (0 structures hits)
PDBeurope Run Query Now (0 structures hits)
Pfam Run Query Now (0 structures hits)
Pfam link: PF06176 RCBS PDB Run Query Now (5 structures hits)
PDBsum Run Query Now (0 structures hits)
PDBeurope Run Query Now (0 structures hits)
Pfam Run Query Now (0 structures hits)


RCBS PDB Query for Pfam kinase member families

Pfam Accession Number: PF00069 and ENZYMECLASSIFICATION is 2: Transferases

Pfam Accession Number: PF07714 and ENZYMECLASSIFICATION is 2: Transferases