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Orthologous residues
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Cdc25A (human): T507‑p, Cdc25A (mouse): T497‑p, Cdc25A (rat): T508‑p
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Characterization
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Methods used to characterize site in vivo:
mutation of modification site, phospho-antibody
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Relevant cell lines - cell types - tissues:
293 (epithelial), COS (fibroblast), HeLa (cervical)
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Cellular systems studied:
cell lines
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Species studied:
human
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Enzymes shown to modify site in vitro:
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Upstream Regulation
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Potential in vivo enzymes for site:
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Type
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Enzyme
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Evidence
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Notes
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KINASE
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Chk1 (human)
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inhibition of upstream enzyme
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Inhibition of Chk1 using siRNA decreased Cdc25A T506 phosphorylation and, to a lesser extent, inhibited S177 phosphorylation.
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Downstream Regulation
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Effect of modification (function):
inhibition, molecular association, regulation
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Modification regulates interactions with:
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Interacting molecule
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Interacting domains
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Effect
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Consequences (function)
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Consequences (process)
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Detection assays
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14-3-3 beta (human)
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Induces
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co-immunoprecipitation
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Comments:
Mutation of T506 to alanine enhanced the activity of Cdc25A, enhancing binding to cyclin B1, activating cyclinB1-Cdk1, and promoting premature entry into mitosis. Binding to 14-3-3 negatively regulates the ability of Cdc25A to dephosphorylate Cdk1.
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