Wu X, Chen J (2003) Autophosphorylation of checkpoint kinase 2 at serine 516 is required for radiation-induced apoptosis. J Biol Chem 278, 36163-8 12855706

This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.

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T68-p - Chk2 (human) ▲

Modsite: SsLEtVstQELYsIP SwissProt Entrez-Gene Orthologous residues Chk2 (human): T68‑p, Chk2 iso9 (human): T68‑p, Chk2 iso11 (human): T68‑p, Chk2 iso12 (human): T68‑p, Chk2 (mouse): T77‑p, Chk2 (rat): T76‑p Characterization Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phospho-antibody Relevant cell lines - cell types - tissues:  293 (epithelial), HCT15 (intestinal), SF9 Cellular systems studied:  cell lines Species studied:  human, insect

S516-p - Chk2 (human) ▲

Modsite: PQVLAQPstSRkRPR SwissProt Entrez-Gene Orthologous residues Chk2 (human): S516‑p, Chk2 iso9 (human): S559‑p, Chk2 iso11 (human): S198‑p, Chk2 iso12 (human): S487‑p, Chk2 (mouse): S520‑p, Chk2 (rat): S519‑p Characterization Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phospho-antibody Relevant cell lines - cell types - tissues:  293 (epithelial), HCT15 (intestinal), SF9 Cellular systems studied:  cell lines Species studied:  human, insect Enzymes shown to modify site in vitro:  Type Enzyme KINASE Chk2 (human) Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes KINASE Chk2 (human) transfection of wild-type enzyme, transfection of inactive enzyme Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes ionizing_radiation increase Downstream Regulation Effect of modification (function):  enzymatic activity, induced