EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.4.1.11 | glycoprotein |
the enzyme has two potential N-glycosylation sites at residues 520 and 577 |
718703 |
| 2.4.1.11 | more |
no covalently attached amino sugars, 2% carbohydrate |
488426 |
| 2.4.1.11 | more |
the enzyme contains no signal peptide, putative cleavage sites, and transmembrane domain |
718703 |
| 2.4.1.11 | phosphoprotein |
- |
488405, 488418, 488422, 488438, 488450, 488452 |
| 2.4.1.11 | phosphoprotein |
0.3 mol per mol enzyme |
488426 |
| 2.4.1.11 | phosphoprotein |
0.7-0.9 mol phosphate per mol protein |
488449 |
| 2.4.1.11 | phosphoprotein |
0.8 phosphates per subunit |
488414 |
| 2.4.1.11 | phosphoprotein |
covalent phosphorylation |
488407 |
| 2.4.1.11 | phosphoprotein |
in healthy subjects, adrenaline infusion increases blood glucose concentration by approximately 50%, but a hyperinsulinemic clamp normalizes blood glucose within 30 minutes. Insulin increases glycogen synthase fractional activity and decreases glycogen synthase Ser641 and Ser645,649,653,657 phosphorylation. In the presence of adrenaline, insulin does neither activate glycogen synthase nor dephosphorylate glycogen synthase Ser641. Glycogen synthase Ser7 phosphorylation is not influenced by adrenaline. Adrenaline increases plasma lactate concentration, and muscle glycogen content is reduced in skeletal muscle the day after adrenaline infusion |
705511 |
| 2.4.1.11 | 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 |
671230 |
