Serine/threonine-protein kinase MPS1
InterPro Protein Domain record
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description
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<p>Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [<cite idref="PUB00005115"/>]:</p><p> <ul> <li>Serine/threonine-protein kinases</li><li>Tyrosine-protein kinases</li><li>Dual specific protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)</li> </ul> </p><p>Protein kinase function has been evolutionarily conserved from <taxon tax_id="562">Escherichia coli</taxon> to human [<cite idref="PUB00020114"/>]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [<cite idref="PUB00015362"/>]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [<cite idref="PUB00034898"/>], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [<cite idref="PUB00034899"/>].</p><p>This entry represents serine/threonine-protein kinases (<db_xref db="EC" dbkey="2.7.12.2"/>), such as MPS1, which acts as a dual specificity kinase that can phosphorylate serine, threonine and tyrosine residues. Mps1 protein kinase is required for regulation of the onset of mitosis, for proper assembly of the mitotic spindle, checkpoint signalling, and for coordination of cell proliferation and differentiation. It is also implicated in spindle pole body (SPD) duplication. Mps1 regulation is mediated by cell cycle-dependent changes in transcription and protein level. There is also a strong correlation between hyperphosphorylated mitotic forms of Mps1 and increased kinase activity. It appears that site-specific Mps1 autophosphorylation within the activation loop is required for full activity of the enzyme [<cite idref="PUB00042756"/>]. MAP kinase (MAPK) can phosphorylate and activate Msk1 in Xenopus eggs [<cite idref="PUB00042757"/>]. Msp1 targets include: mortalin (Hsp70 chaperoning protein family) [<cite idref="PUB00042758"/>], Smad2 and Smad3 (mediators of TGF-beta signalling) [<cite idref="PUB00042759"/>], Dam1 (kinetochore component that directly binds to microtubules) [<cite idref="PUB00042760"/>], BLM helicase (interacts with proteins involved in DNA replication, recombination, and repair) [<cite idref="PUB00042761"/>], amongst others.</p>
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Serine/threonine-protein kinase MPS1
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