9026-43-1
Chemical Structure
Protein serine/threonine kinase
Synonym(s): Ser/Thr protein kinase
- CAS No.: 9026-43-1
- Formula:N/A
- Molecular Weight:N/A
SMILES: [Protein serine/threonine kinase]
Biological Activity: Protein serine/threonine kinase (Ser/Thr protein kinase) is a signal transduction molecule. Protein serine/threonine kinase phosphorylates specific residues on target substrates, regulates phosphorylation-dependent signal cascades, modulates cellular processes of mycobacteria, blocks phagosome-lysosome fusion, promotes meiotic maturation of Xenopus laevis (African clawed frog) oocytes, rescues the phenotype of Saccharomyces cerevisiae (budding yeast) CDC5 mutants, and exhibits cell cycle phase-specific kinase activity. Protein serine/threonine kinase maintains a tightly regulated cell cycle expression pattern, and sustains the growth and survival of mycobacteria. Protein serine/threonine kinase can be used in studies related to tuberculosis[1][2].
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Protein serine/threonine kinase | Protein serine/threonine kinase (Ser/Thr protein kinase) is a signal transduction molecule. Protein serine/threonine kinase phosphorylates specific residues on target substrates, regulates phosphorylation-dependent signal cascades, modulates cellular processes of mycobacteria, blocks phagosome-lysosome fusion, promotes meiotic maturation of Xenopus laevis (African clawed frog) oocytes, rescues the phenotype of Saccharomyces cerevisiae (budding yeast) CDC5 mutants, and exhibits cell cycle phase-specific kinase activity. Protein serine/threonine kinase maintains a tightly regulated cell cycle expression pattern, and sustains the growth and survival of mycobacteria. Protein serine/threonine kinase can be used in studies related to tuberculosis. | |||||||||||||||||||||
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- [1]. Baros SS, et al. Phosphoproteomic Approaches to Discover Novel Substrates of Mycobacterial Ser/Thr Protein Kinases. Mol Cell Proteomics. 2020;19(2):233-244. [Content Brief]
- [2]. Ouyang B, et al. Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions. J Biol Chem. 1997 Nov 7;272(45):28646-51. [Content Brief]
Keywords
