Serine/threonine-specific protein kinase
Class of protein kinase enzymes / From Wikipedia, the free encyclopedia
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A serine/threonine protein kinase (EC 2.7.11.-) is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).[2]
Protein-serine/threonine kinases | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.11.- | ||||||||
CAS no. | 9026-43-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, the term serine/threonine protein kinase describes a class of enzymes in the family of transferases, that transfer phosphates to the oxygen atom of a serine or threonine side chain in proteins. This process is called phosphorylation. Protein phosphorylation in particular plays a significant role in a wide range of cellular processes and is a very important post-translational modification.[3][4][5][6][7][8][9]
The chemical reaction performed by these enzymes can be written as
- ATP + a protein ADP + a phosphoprotein
Thus, the two substrates of this enzyme are ATP and a protein, whereas its two products are ADP and phosphoprotein.
The systematic name of this enzyme class is ATP:protein phosphotransferase (non-specific).