Curated Information

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PubMed Id: 12379650

This page summarizes selected information from the article 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.

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

Y104-p - Rad52 (human)

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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): activation, intracellular localization

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