TyrKc

Tyrosine kinase, catalytic domain
TyrKc
SMART accession number:SM00219
Description: Phosphotransferases. Tyrosine-specific kinase subfamily.
Interpro abstract (IPR001245):

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).

Tyrosine phosphorylating activity was originally detected in two viral transforming proteins but many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors, which are activated by ligand binding, and the insulin-related peptide receptor, are also family members.

GO process:protein amino acid phosphorylation (GO:0006468)
GO function:protein tyrosine kinase activity (GO:0004713), ATP binding (GO:0005524)
Family alignment:
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There are 3236 TyrKc domains in 3235 proteins in SMART's nrdb database.

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