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Article

Stability of checkpoint kinase 2 is regulated via phosphorylation at serine 456.

The Journal of biological chemistry - 12 Oct 2007

Kass Elizabeth M, Ahn Jinwoo, Tanaka Tomoaki, Freed-Pastor William A, Keezer Susan, Prives Carol

Abstract excerpt

Checkpoint kinase 2 (Chk2), a DNA damage-activated protein kinase, is phosphorylated at Thr-68 by ataxia telangiectasia mutated leading to its activation by phosphorylation at several additional sites. Using mass spectrometry we identified a new Chk2 phosphorylation site at Ser-456. We show that phosphorylation of Ser-456 plays a role in the regulation of Chk2 stability particularly after DNA damage. Mutation of...

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Identifiers

PMID: 17715138
DOI: 10.1074/jbc.M704642200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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