EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.11.20 | more |
the enzyme is ubiquitinated in vivo, ubiquitination and turnover is increased by inhibition of heat shock protein 90, enzyme degradation involves the proteasome |
664505 |
| 2.7.11.20 | phosphoprotein |
- |
723025 |
| 2.7.11.20 | phosphoprotein |
AMPK activates eEF2K via phosphorylation. Inhibition of proline hydroxylases, e.g. by DMOG, induces the phosphorylation of eEF2 independently of altered mTORC1 or AMPK signaling |
740996 |
| 2.7.11.20 | phosphoprotein |
autophosphorylation site is Thr348 in eEF2K |
740015 |
| 2.7.11.20 | phosphoprotein |
eEF2K activity is also regulated by phosphorylation. Ser366 is phosphorylated by S6 kinases, enzymes which are phosphorylated and activated by mTORC1, phosphorylation at this site desensitizes eEF2K to activation by Ca2+/CaM. Phosphorylation of Ser359, a site whose modification strongly inhibits eEF2K, and Ser78, immediately next to the CaM-binding motif, are also promoted by mTORC1. The latter strongly impairs the interaction of eEF2K with CaM thereby impairing its activation. For eEF2K stimulation, cAMP, a catabolic signal which inhibits protein synthesis, stimulates cAMP-dependent protein kinase, PKA, which phosphorylates eEF2K at Ser500. Degradation of eEF2K requires the autophosphorylation site at Ser445, which forms part of a typical bTrCP-binding motif or phosphodegron. eEF2K is also phosphorylated at several sites in response to activation of stress-stimulated MAP kinase cascades, either directly by MAPKs or by their downstream effectors. Phosphorylation of eEF2 at Thr56 impairs its binding to the ribosome. The enzyme is regulated by its phosphorylation status, overview |
739828 |
| 2.7.11.20 | phosphoprotein |
inactivating Ser366 phosphorylation of eEF2 kinase |
684318 |
| 2.7.11.20 | phosphoprotein |
phosphorylated GCN2 is the active form of the enzyme |
723079 |
| 2.7.11.20 | phosphoprotein |
phosphorylation at Ser366 inhibits the enzyme, mediated by cholecystokinin |
663836 |
| 2.7.11.20 | phosphoprotein |
phosphorylation by p70-S6 kinase inhibits EF2K, Ca2+ decreases the phosphorylation of the enzyme |
684831, 685402 |
| 2.7.11.20 | phosphoprotein |
phosphorylation of eEF2K can either inhibit or enhance the activity of its downstream substrate, depending on the site of phosphorylation and the type of stimul, lopinavir increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview |
687926 |
