Curated Information
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Curated Information Page
PubMed Id: 12556884 
Bakkenist CJ, Kastan MB (2003) DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature 421, 499-506 12556884
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S1981-p - ATM (human)
Orthologous residues
ATM (human): S1981‑p, ATM (mouse): S1987‑p, ATM (rat): S1988‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phospho-antibody, phosphoamino acid analysis, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial), fibroblast-foreskin, HeLa (cervical)
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ATM (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation increase
wortmannin ionizing radiation inhibit treatment-induced increase
UV increase
chloroquine increase
trichostatin A increase
hypotonic buffer increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Effect of modification (process):  cell cycle regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
p53 (human) Induces phosphorylation functional assay, in vitro


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