The Enzyme Database

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Accepted name: MAST-subfamily protein kinase
Reaction: (1) ATP + [protein]-L-serine = ADP + [protein]-O-phospho-L-serine
(2) ATP + [protein]-L-threonine = ADP + [protein]-O-phospho-L-threonine
Other name(s): microtubule-associated serine/threonine-protein kinase; MAST1; MAST2; MAST3; MAST4; MAST205; SAST; IREH1; dop; kin-4
Comments: Requires Mg2+. MAST (Microtubule Associated Serine/Threonine) kinases are eukaryotic-wide kinases with roles in microtubule function, PTEN regulation and a variety of neuronal functions. They are found in most eukaryotes, though lost from most fungi and ciliates. MAST kinases associate with their substrates via their PDZ domains. Substrates include the PTEN phosphatase (EC in human and nematodes, and Dlic (Dynein light intermediate chain) in Drosophila. The latter is phosphorylated on Ser401.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Valiente, M., Andres-Pons, A., Gomar, B., Torres, J., Gil, A., Tapparel, C., Antonarakis, S.E. and Pulido, R. Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases. J. Biol. Chem. 280 (2005) 28936–28943. [DOI] [PMID: 15951562]
2.  An, S.WA., Choi, E.S., Hwang, W., Son, H.G., Yang, J.S., Seo, K., Nam, H.J., Nguyen, N.TH., Kim, E.JE., Suh, B.K., Kim, Y., Nakano, S., Ryu, Y., Man Ha, C., Mori, I., Park, S.K., Yoo, J.Y., Kim, S. and Lee, S.V. KIN-4/MAST kinase promotes PTEN-mediated longevity of Caenorhabditis elegans via binding through a PDZ domain. Aging Cell 18:e12906 (2019). [DOI] [PMID: 30773781]
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