Curated Information
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Home > Curated Information Page > PubMed Id: 20363734
Antony R, Lukiw WJ, Bazan NG (2010) Neuroprotectin D1 induces dephosphorylation of Bcl-xL in a PP2A-dependent manner during oxidative stress and promotes retinal pigment epithelial cell survival. J Biol Chem 285, 18301-8 20363734
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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S62-p - Bcl-xL (human)
Modsite: PSWHLADsPAVNGAT SwissProt Entrez-Gene
Orthologous residues
Bcl‑xL (human): S62‑p, Bcl‑xL (mouse): S62‑p, Bcl‑xL (rat): S62‑p
Methods used to characterize site in vivo phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  ARPE19 (retinal)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
PHOSPHATASE PPP2CA (human) pharmacological inhibitor of upstream enzyme, siRNA inhibition of enzyme, co-immunoprecipitation, microscopy-colocalization
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF, H2O2 increase
NPD1 H2O2, TNF inhibit treatment-induced increase
okadaic_acid H2O2, TNF augment treatment-induced increase
H2O2, TNF PPP2CA (human) inhibit treatment-induced increase PPP2CA siRNA augments increase
Downstream Regulation
Effect of modification (function):  intracellular localization
Comments:  in cytosol