Curated Information
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Curated Information Page
PubMed Id: 12379650 
Kitao H, Yuan ZM (2002) Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation. J Biol Chem 277, 48944-8 12379650
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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Y104-p - Rad52 (human)
Orthologous residues
Rad52 (human): Y104‑p, Rad52 (mouse): Y105‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Abl (human) mutation in upstream enzyme recognition motif, transfection of inactive enzyme
Downstream Regulation
 Effect of modification (function):  activity, induced, intracellular localization


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