Gao J, et al. (2015) PPARα induces cell apoptosis by destructing Bcl2. Oncotarget 6, 44635-42 26556865

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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K22-ub - Bcl-2 (human) ▲

Modsite: VMkYIHYkLSQRGYE SwissProt Entrez-Gene Orthologous residues Bcl‑2 (human): K22‑ub, Bcl‑2 (mouse): K22‑ub, Bcl‑2 (rat): K22‑ub Characterization Methods used to characterize site in vivo:  mutation of modification site, western blotting Relevant cell lines - cell types - tissues:  HEK293T (epithelial) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme UBIQUITIN LIGASE UBE2D3 (human) UBIQUITIN LIGASE PPAR-alpha (human) UBIQUITIN LIGASE UBE2D1 (human) UBIQUITIN LIGASE UBE2D2 (human) Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes PPAR-alpha (human) increase E3-ubiquitin ligase Downstream Regulation Effect of modification (function):  protein degradation Effect of modification (process):  apoptosis, induced Comments:  increased cancer cell chemotherapy sensitivity