Curated Information
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Home > Curated Information Page > PubMed Id: 18570920
Kang ES, et al. (2008) O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic beta cells. Exp Cell Res 314, 2238-48 18570920
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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S473-p - Akt1 (mouse)
Modsite: RPHFPQFsysAsGtA SwissProt Entrez-Gene
Orthologous residues
Akt1 (human): S473‑p, Akt1 iso2 (human): S411‑p, Akt1 (mouse): S473‑p, Akt1 (rat): S473‑p, Akt1 (fruit fly): S586‑p, Akt1 (cow): S473‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, phospho-antibody, western blotting
Disease tissue studied:  pancreatic cancer, pancreatic carcinoma
Relevant cell lines - cell types - tissues:  beta TC3 (pancreatic)
Cellular systems studied:  cell lines
Species studied:  mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
glucosamine decrease
glucose decrease
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced

S473-gl - Akt1 (mouse)
Modsite: RPHFPQFsysAsGtA SwissProt Entrez-Gene
Orthologous residues
Akt1 (human): S473‑gl, Akt1 iso2 (human): S411‑gl, Akt1 (mouse): S473‑gl, Akt1 (rat): S473‑gl, Akt1 (fruit fly): S586‑gl, Akt1 (cow): S473‑gl

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
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
glucosamine decrease

S473-p - Akt1 (rat)
Modsite: RPHFPQFsYSASGTA SwissProt Entrez-Gene
Orthologous residues
Akt1 (human): S473‑p, Akt1 iso2 (human): S411‑p, Akt1 (mouse): S473‑p, Akt1 (rat): S473‑p, Akt1 (fruit fly): S586‑p, Akt1 (cow): S473‑p
Characterization
Methods used to characterize site in vivo 2D analysis, immunoprecipitation, mass spectrometry, phospho-antibody, western blotting
Disease tissue studied:  pancreatic cancer, pancreatic carcinoma
Relevant cell lines - cell types - tissues:  INS-1 (pancreatic)
Cellular systems studied:  cell lines
Species studied:  rat
Enzymes shown to modify site in vitro
Type Enzyme
O-GlcNAc TRANSFERASE OGT (human)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
glucosamine decrease
BADGP glucosamine inhibit treatment-induced decrease
alloxan glucosamine inhibit treatment-induced decrease
BADGP increase
alloxan increase
PUGNAc decrease
PUGNAc glucosamine decrease
OGT (human) decrease

S473-gl - Akt1 (rat)
Modsite: RPHFPQFsYSASGTA SwissProt Entrez-Gene
Orthologous residues
Akt1 (human): S473‑gl, Akt1 iso2 (human): S411‑gl, Akt1 (mouse): S473‑gl, Akt1 (rat): S473‑gl, Akt1 (fruit fly): S586‑gl, Akt1 (cow): S473‑gl
Characterization
Methods used to characterize site in vivo immunoprecipitation, modification-specific antibody, mutation of modification site, western blotting
Disease tissue studied:  pancreatic cancer, pancreatic carcinoma
Relevant cell lines - cell types - tissues:  INS-1 (pancreatic)
Cellular systems studied:  cell lines
Species studied:  rat
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
O-GlcNAc TRANSFERASE OGT (human) co-immunoprecipitation, transfection of wild-type enzyme
Comments:  in cells treated with glucosamine
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
glucosamine increase decreases cells viability
Downstream Regulation
Effect of modification (function):  phosphorylation
Comments:  O-GlcNAc modification at Akt S473 competes with phosphorylation at Akt S473