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Literature summary for 2.7.11.22 extracted from

  • Abreu, C.M.; Kumar, R.; Hamilton, D.; Dawdy, A.W.; Creavin, K.; Eivers, S.; Finn, K.; Balsbaugh, J.L.; OConnor, R.; Kiely, P.A.; Shabanowitz, J.; Hunt, D.F.; Grenon, M.; Lowndes, N.F.
    Site-specific phosphorylation of the DNA damage response mediator rad9 by cyclin-dependent kinases regulates activation of checkpoint kinase 1 (2013), PLoS Genet., 9, e1003310.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + Rad9 protein Saccharomyces cerevisiae a DNA damage response mediator ADP + Rad9 phosphoprotein
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 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Rad9 protein a DNA damage response mediator Saccharomyces cerevisiae ADP + Rad9 phosphoprotein
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 ?
ATP + Rad9 protein a DNA damage response mediator, phosphorylaation at Thr125 and Thr143 Saccharomyces cerevisiae ADP + Rad9 phosphoprotein
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 ?

Synonyms

Synonyms Comment Organism
Cdc28
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 Saccharomyces cerevisiae
CDK
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 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function a specific G2/M form of Cdc28 can phosphorylate in vitro the N-terminal region of Rad9 on nine consensus CDK phosphorylation sites, N-terminal CDK consensus sites are phosphorylated by Cdc28/Clb2 and are required for activation of Chk1. The integrity of CDK consensus sites and the activity of Cdc28 are required for both the activation of the Chk1 checkpoint kinase and its interaction with Rad9. Phosphorylation of T143 is the most important feature promoting Rad9/Chk1 interaction, while the much more abundant phosphorylation of the neighbouring T125 residue impedes the Rad9/Chk1 interaction. CDK-dependent activation of Chk1 controls Rad9/Chk1 interaction Saccharomyces cerevisiae