Curated Information
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Curated Information Page
PubMed Id: 23888040 
Bassi C, et al. (2013) Nuclear PTEN controls DNA repair and sensitivity to genotoxic stress. Science 341, 395-9 23888040
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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K254-sm - PTEN (human)
Orthologous residues
PTEN (human): K254‑sm, PTEN iso2 (human): K427‑sm, PTEN (mouse): K254‑sm, PTEN (rat): K254‑sm
 Methods used to characterize site in vivo mass spectrometry (in vitro), mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  nuclear localization retention

T398-p - PTEN (human)
Orthologous residues
PTEN (human): T398‑p, PTEN iso2 (human): T571‑p, PTEN (mouse): S398‑p, PTEN (rat): S398‑p
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ATM (human) co-immunoprecipitation, activation of upstream enzyme, modification site within consensus motif
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation increase

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