Seroatlas · Protein domains

Serine/threonine-protein kinase, active site

IPR008271

Definition

Eukaryotic protein kinases [[cite:PMID:7768349], [cite:PMID:1835513], [cite:PMID:1956325], [cite:PMID: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 PMID:1862342. This entry represents a conserved region that surrounds the active site aspartate residue and it is more specific for serine/threonine protein kinases. It also matches several dual-specificity protein kinases and members of WEE kinase family that are bona fide tyrosine protein kinases. 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 PMID:3291115: Serine/threonine-protein kinases Tyrosine-protein kinases Dual specificity protein kinases (e.g. MEK -phosphorylates both Thr and Tyr on target proteins) Protein kinase function is evolutionarily conserved from Escherichia coli to human PMID:12471243. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation PMID: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 PMID:15078142, leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases PMID:15320712.

310 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

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