a member of the GTP-binding translation elongation factor family. An essential factor for protein synthesis. Promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. This protein is completely inactivated by eEF2 kinase phosphorylation. eEF2 kinase is normally dependent on Ca2+ ions and calmodulin. eEF2 kinase can also be activated by PKA in response to elevated cAMP levels, which are generally increased in stress- or starvation-related conditions. A variety of treatments known to raise intracellular Ca2+ or cAMP levels have been shown to result in increased phosphorylation of eEF2, and thus to inhibit peptide-chain elongation. Note: This description may include information from UniProtKB.
Molecular Function: cadherin binding; protein binding; protein kinase binding; RNA binding
Biological Process: neutrophil degranulation; peptidyl-diphthamide biosynthetic process from peptidyl-histidine; positive regulation of translation; protein amino acid methylation; translational elongation