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Tyrosine-specific protein kinases (EC 2.7.10.1 and EC 2.7.10.2) phosphorylate tyrosine amino acid residues, and like serine/threonine-specific kinases are used in signal transduction. They act primarily as growth factor receptors and in downstream signaling from growth factors. [12] Some examples include: Platelet-derived growth factor receptor ...
Many serine/threonine protein kinases do not have their own individual EC numbers and use 2.7.11.1, "non-specific serine/threonine protein kinase". This entry is for any enzyme that phosphorylates proteins while converting ATP to ADP (i.e., ATP:protein phosphotransferases.) [10] 2.7.11.37 "protein kinase" was the former generic placeholder and was split into several entries (including 2.7.11.1 ...
Tyrosine kinases belong to a larger class of enzymes known as protein kinases which also attach phosphates to other amino acids such as serine and threonine. Phosphorylation of proteins by kinases is an important mechanism for communicating signals within a cell (signal transduction) and regulating cellular activity, such as cell division.
Kinases are either phosphorylated on serine and/or threonine residues, or solely on tyrosine residues. [5] This serves as a means to classify them as either Ser/Thr- or Tyr-kinases. Several residues within the primary structure may be autophosphorylated simultaneously.
Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. [3] The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine. [4] [5] These phosphorylations play important and well-characterized roles in signaling pathways and metabolism.
In biochemistry, a dual-specificity kinase (EC 2.7.12.1) is a kinase that can act as both tyrosine kinase and serine/threonine kinase. MEKs, involved in MAP pathways, are principal examples of dual-specificity kinases. Other common examples include: ADK1 (Arabidopsis dual specificity kinase 1)
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 ...
Glycogen synthase kinase 3 (GSK-3) is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. First discovered in 1980 as a regulatory kinase for its namesake, glycogen synthase (GS), [2] GSK-3 has since been identified as a protein kinase for over 100 different proteins in a variety of different pathways.