S_TK_X

Extension to Ser/Thr-type protein kinases
S_TK_X
SMART accession number:SM00133
Description:
Interpro abstract (IPR000961):

Protein kinases are a group of enzymes that possess a catalytic subunit which transfers 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. The enzymes fall into two broad classes, characterised with respect to substrate specificity: serine/threonine specific and tyrosine specific (PUBMED:3291115).

Protein kinase function has been evolutionarily conserved from Escherichia coli to Homo sapiens. Protein kinases play a role in a mulititude 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).

This domain is found in a large variety of protein kinases with different functions and dependencies. Protein kinase C, for example, is a calcium-activated, phospholipid-dependent serine- and threonine-specific enzyme. It is activated by diacylglycerol which, in turn, phosphorylates a range of cellular proteins. This domain is most often found associated with IPR000719.
GO process:protein amino acid phosphorylation (GO:0006468)
GO function:protein serine/threonine kinase activity (GO:0004674), ATP binding (GO:0005524)
Family alignment:
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There are 2719 S_TK_X domains in 2713 proteins in SMART's nrdb database.

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