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CHEK2 phosphorylates TP53 on S366. 7 / 7
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"The cell cycle checkpoint kinases CHK1 and CHK2 have been shown to phosphorylate multiple sites in the N-terminal domain of p53, consequently leading to p53 stabilization and activation. Phosphorylation of at least three of these sites, Ser366, Ser378, and Thr387, was induced by DNA damage."

"Chk1/chk2 and atm/atr also phosphorylate the effector p53, increasing its stability.We Have demonstrated that the human homologs of the checkpoint kinases, chk1 and chk2/hcds1, phosphorylate at least three dna damage-inducible phosphorylation sites in p53."

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"ATM dependent dephosphorylation of p53 at S376 and Chk1 and Chk2 dependent phosphorylation of p53 at S378, S366 and T387 generate 14-3-3 binding sites in vivo."

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"Chk2 is known to mediate phosphorylation of p53 at Ser 366 and Ser 378 in response to genotoxic stresses XREF_BIBR."

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"However, during the later stages, CHK2 may contribute to p53 phosphorylation at Ser366 and Ser378, resulting in p53 degradation through the ubiquitin-proteasome pathway and blocking of p53 mediated apoptosis [XREF_BIBR] and the EBV protein kinase BGLF4 contributes to p27 phosphorylation and its ubiquitin-proteasome dependent degradation [XREF_BIBR]."

No evidence text available

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"The Chk1 and Chk2 kinases phosphorylate p53 at S366, S378 and T387."