Curated Information
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Home > Curated Information Page > PubMed Id: 16505231
Hutchinson DS, Bengtsson T (2006) AMP-activated protein kinase activation by adrenoceptors in L6 skeletal muscle cells: mediation by alpha1-adrenoceptors causing glucose uptake. Diabetes 55, 682-90 16505231
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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S218-p - ACC2 (rat)
Modsite: PTMRPSMsGLHLVKR SwissProt Entrez-Gene
Orthologous residues
ACC2 (human): S222‑p, ACC2 (mouse): S212‑p, ACC2 (rat): S218‑p
Methods used to characterize site in vivo phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  'muscle, skeletal', CHO (fibroblast)
Cellular systems studied:  primary cultured cells
Species studied:  rat
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
compound_C, insulin, acadesine increase In L6 cells, AICAR and cirazoline but not isoprenaline or insulin phosphorylated ACC2 at S218, and this was inhibited by Compound C.