EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.11.31 | lipoprotein |
the subunit beta sequence contains an N-myristoylation site |
740129 |
| 2.7.11.31 | phosphoprotein |
- |
760910 |
| 2.7.11.31 | phosphoprotein |
8-chloro-cAMP and no 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside induce AMPK phosphorylation |
693328 |
| 2.7.11.31 | phosphoprotein |
AAK-2 is phosphorylated at Thr243 in response to paraquat treatment, the phosphorylation depends on PAR-4, the Caenorhabditis elegans LKB1 homologue |
693057 |
| 2.7.11.31 | phosphoprotein |
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C |
692365 |
| 2.7.11.31 | phosphoprotein |
activation of AMPK requires phosphorylation at Thr172 by an AMPK kinases, e.g. LKB1 and Ca2+/calmodulin-dependent kinase kinase, CaMKK |
693032 |
| 2.7.11.31 | phosphoprotein |
activation of the enzyme by phosphorylation of Thr172 of the alpha subunit. Thr172 is the only site phosphorylated by its upstream kinase, liver kinase B1, and the phosphorylation dramatically increases the kinase activity of the catalytic domain/alpha-subunit. Phosphorylation of AMPK alpha1 on Thr172 by LKB1/Ste20-related adaptor (STRAD)/mouse protein 25(MO25) complex. Top-down mass spectrometric analysis, overview. Ser18 and Ser22 in the His-tag region as well as Thr196 (equivalent to Thr172 in the unmodified enzyme) in the sequence of the AMPK catalytic domain are the three phosphorylation sites |
740582 |
| 2.7.11.31 | phosphoprotein |
AMPK alpha1 subunit is phosphorylated at Thr172 |
691621 |
| 2.7.11.31 | phosphoprotein |
AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals |
692209 |
| 2.7.11.31 | phosphoprotein |
AMPK is activated by phosphorylation, induced e.g. by leptin |
692277 |
