Threonine and Tyrosine Kinase (None)

Most "protein kinases" are enzymes transferring phosphate groups from ATP to specific amino acids (serine, threonine, tyrosine) on protein substrates, regulating activity in key pathways such as signal transduction, cell division, and differentiation. "Tyrosine kinases" specifically phosphorylate tyrosine residues, while "serine/threonine kinases" act on serine and threonine. Some kinases, known as "dual-specificity kinases" (e.g., MAP kinase kinases/MEKs), can phosphorylate both. Aberrant kinase activity is implicated in multiple diseases, notably cancer and autoimmunity, making them major pharmacological targets. The term "Threonine and Tyrosine Kinase" does not accurately refer to a unique canonical target; relevant canonical targets should be "Tyrosine kinase," "Serine/threonine kinase," or precise dual-specificity kinases such as "Mitogen-activated protein kinase kinase (MEK)".

Other names

Tyrosine kinaseSerine/threonine kinaseDual-specificity kinaseProtein kinase

Competitive inhibition of ATP-binding site (for many TKIs); Allosteric inhibition; Covalent inhibition; Type I–V inhibitor classes based on binding site and mechanism