Curated Information

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Curated Information Page

PubMed Id: 16885023

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.

Information from this record has been curated, but not yet edited in PhosphoSitePlus^® and may be incomplete.

Wang X, et al. (2006) Rad17 phosphorylation is required for claspin recruitment and Chk1 activation in response to replication stress. Mol Cell 23, 331-41 16885023

Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.

S646-p - Rad17 (human)

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Orthologous residues

Rad17 (human): S646‑p, Rad17 (mouse): S647‑p

Characterization

Methods used to characterize site in vivo: mutation of modification site

Cellular systems studied: cell lines

Species studied: human

Comments: Rad17 flox/- cells

Downstream Regulation

Effect of modification (function): molecular association, regulation, phosphorylation

Effect of modification (process): cell cycle regulation, cell growth, altered

Modification regulates interactions with:

Interacting molecule	Interacting domains	Effect	Consequences (function)	Consequences (process)	Detection assays
claspin (human)		Induces			co-immunoprecipitation, pull-down assay

Comments: regulates genomic stability, phosphorylation of Chk1

S656-p - Rad17 (human)

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