Curated Information

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Curated Information Page

PubMed Id: 9543386

This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus^®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus^®, click here.

Peng CY, et al. (1998) C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and promotes 14-3-3 protein binding. Cell Growth Differ 9, 197-208 9543386

S216-p - Cdc25C (human)

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Orthologous residues

Cdc25C (human): S216‑p, Cdc25C iso3 (human): S173‑p, Cdc25C (mouse): ‑, Cdc25C (frog): S287‑p

Characterization

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	MARK3 (human)

Comments: MARK3 ubiquitously expressed in human tissues and cell lines.

Downstream Regulation

Effect of modification (function): intracellular localization, molecular association, regulation

Modification regulates interactions with:

Interacting molecule	Interacting domains	Effect	Consequences (function)	Consequences (process)	Detection assays
14-3-3 beta (human)		Induces

Comments: It is likely that multiple isoforms of 14-3-3 bound pS216 in the experiments described here.

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