Curated Information
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Home > Curated Information Page > PubMed Id: 27738106
Hinds TD, et al. (2016) Biliverdin Reductase A Attenuates Hepatic Steatosis by Inhibition of Glycogen Synthase Kinase (GSK) 3β Phosphorylation of Serine 73 of Peroxisome Proliferator-activated Receptor (PPAR) α. J Biol Chem 291, 25179-25191 27738106
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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S9-p - GSK3B (mouse)
Modsite: SGRPRttsFAEsCKP SwissProt Entrez-Gene
Orthologous residues
GSK3B (human): S9‑p, GSK3B iso2 (human): S9‑p, GSK3B (mouse): S9‑p, GSK3B (rat): S9‑p, GSK3B (rabbit): S9‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  liver
Cellular systems studied:  tissue
Species studied:  mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
BVR (mouse) increase BVR KO decrease

S73-p - PPAR-alpha (mouse)
Modsite: SVITDTLsPASSPSS SwissProt Entrez-Gene
Orthologous residues
PPAR‑alpha (human): S73‑p, PPAR‑alpha (mouse): S73‑p, PPAR‑alpha (rat): S73‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  liver
Cellular systems studied:  tissue
Species studied:  mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
BVR (mouse) decrease BVR KO increase (in liver)
Downstream Regulation
Effect of modification (function):  activity, inhibited, protein degradation, ubiquitination