EEF2K is a highly conserved calmodulin-dependent protein kinase that links activation of cell surface receptors to cell division. EEF2K is involved in the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2), an abundant cytoplasmic protein that catalyzes the movement of the ribosome along mRNA during translation in eukaryotic cells, and inhibits the EEF2 function. EEF2K is highly expressed in heart and skeletal muscle, suggesting that EEF2 phosphorylation may be particularly important in muscle. EEF2K is highly expressed in patients with systemic lupus erythematosus as well as in many cancers.
Proceedings of the National Academy of Sciences of the United States of America, 94(10), 4884-4889 (1997-05-13)
The several hundred members of the eukaryotic protein kinase superfamily characterized to date share a similar catalytic domain structure, consisting of 12 conserved subdomains. Here we report the existence and wide occurrence in eukaryotes of a protein kinase with a
Biochemical and biophysical research communications, 293(3), 1073-1076 (2002-06-08)
Elongation factor 2 kinase (eEF-2K), also known as calmodulin-dependent protein kinase III, is a member of the calmodulin-mediated signaling pathway that links activation of cell surface receptors to cell division. The activity of eEF-2K is increased in many human cancers
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