Global InformationProtein kinase domain information
| Protein kinase domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the catalytic subunit of cAMP-dependent protein kinase.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Pkinase | ||||||||
| Pfam | PF00069 | ||||||||
| InterPro | IPR000719 | ||||||||
| SMART | TyrKc | ||||||||
| PROSITE | PDOC00100 | ||||||||
| SCOP2 | 1apm / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 186 | ||||||||
| CDD | cd00180 | ||||||||
| Membranome | 3 | ||||||||
| |||||||||
The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases.[2][3][4] Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. This functions as an on/off switch for many cellular processes, including metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. They also function in embryonic development, physiological responses, and in the nervous and immune system. Abnormal phosphorylation causes many human diseases, including cancer, and drugs that affect phosphorylation can treat those diseases.[5]
Protein kinases possess a catalytic subunit which transfers the gamma phosphate from nucleoside triphosphates (almost always ATP) to the side chain of an amino acid in a protein, resulting in a conformational and/or dynamic changes affecting protein function. These enzymes fall into two broad classes, characterised with respect to substrate specificity: serine/threonine specific and tyrosine specific.[6]
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