EC Number |
Posttranslational Modification |
Reference |
---|
2.7.11.26 | phosphoprotein |
- |
691623, 703016, 703599, 704607, 705282, 705325, 705453, 705898 |
2.7.11.26 | phosphoprotein |
0.001 mg/ml chaperonin 10 stimulates the phosphorylation of GSK-3beta |
704796 |
2.7.11.26 | phosphoprotein |
14-3-3 recognises GSK-3 phosphorylated at Ser9, and indeed GSK-3 in this complex is phosphorylated at Ser9 in brain |
740530 |
2.7.11.26 | phosphoprotein |
activity of GSK3beta is regulated through phosphorylation on serine-9 (inhibitory) and tyrosine-216 residues (stimulatory) |
705251 |
2.7.11.26 | phosphoprotein |
Akt phosphorylates GSK-3beta at serine residue 9 thereby inhibiting the activity of GSK-3beta, furthermore GSK-3beta is controlled by tyrosine phosphorylation, which increases its activity |
703941 |
2.7.11.26 | phosphoprotein |
AMP binding induces a conformational change in the ? -subunit activation loop of the kinase that allows phosphorylation of the activating residue Thr172 by AMPK upstream kinases |
740531 |
2.7.11.26 | phosphoprotein |
autophosphorylation, phosphorylation on a conserved tyrosine residue is required for efficient activity. Phosphorylated at a Ser225 is likely to inhibit its function |
491705 |
2.7.11.26 | phosphoprotein |
GSK-3 is inactivated by phosphorylation of serine 9 in GSK-3beta and serine 21 in GSK-3alpha subunits. Akt appears to be the predominant kinase mediating this phosphorylation of GSK-3 |
741440 |
2.7.11.26 | phosphoprotein |
GSK-3beta is activated by phosphorylation of the tyrosine 216 residue located in the kinase domain and inactivated by phosphorylation of the amino-terminal serine 9 residue |
706424 |
2.7.11.26 | phosphoprotein |
GSK-3beta is activated via phosphorylation at Ser9 |
706016 |