Curated Information
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Home > Curated Information Page > PubMed Id: 26556865
Gao J, et al. (2015) PPARĪ± 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 UBE2D2 (human)
UBIQUITIN LIGASE UBE2D1 (human)
UBIQUITIN LIGASE PPAR-alpha (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