Literature summary for 2.4.1.11 extracted from

Jensen, J.; Jebens, E.; Brennesvik, E.O.; Ruzzin, J.; Soos, M.A.; Engebretsen, E.M.; ORahilly, S.; Whitehead, J.P.
Muscle glycogen inharmoniously regulates glycogen synthase activity, glucose uptake, and proximal insulin signaling (2006), Am. J. Physiol. Endocrinol. Metab., 290, E154-E162.

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Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	in low glycogen, basal and insulin-stimulated glycogen synthesis and glycogen synthase activation is higher and glycogen synthase phosphorylation (Ser645, Ser649, Ser653, Ser657) lower than in normal glycogen. Muscles with high glycogen show lower insulin-stimulated glycogen synthesis and glycogen synthase activation than normal glycogen despite similar dephosphorylation	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	in low glycogen, basal and insulin-stimulated glycogen synthesis and glycogen synthase activation is higher and glycogen synthase phosphorylation (Ser645, Ser649, Ser653, Ser657) lower than in normal glycogen. Muscles with high glycogen show lower insulin-stimulated glycogen synthesis and glycogen synthase activation than normal glycogen despite similar dephosphorylation	Rattus norvegicus	-

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Release 2023.1 (January 2023)