 Elongation Factor 2 Kinase
"Elongation Factor 2 Kinase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A monomeric calcium-calmodulin-dependent protein kinase subtype that specifically phosphorylates PEPTIDE ELONGATION FACTOR 2. The enzyme lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE, however it is regulated by phosphorylation by PROTEIN KINASE A and through intramolecular autophosphorylation.
| Descriptor ID |
D054736
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| MeSH Number(s) |
D08.811.913.696.620.682.700.125.425 D12.644.360.100.425 D12.776.476.100.425
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| Concept/Terms |
Elongation Factor 2 Kinase- Elongation Factor 2 Kinase
- eEF-2-Specific Ca and Calmodulin-Dependent Protein Kinase III
- eEF 2 Specific Ca and Calmodulin Dependent Protein Kinase III
- EF-2 Kinase
- EF 2 Kinase
- Kinase, EF-2
- Eukaryotic Elongation Factor-2 Kinase
- Eukaryotic Elongation Factor 2 Kinase
- Calcium-Calmodulin-Dependent Protein Kinase Type 3
- Calcium Calmodulin Dependent Protein Kinase Type 3
- Calmodulin-Dependent Protein Kinase III
- Calmodulin Dependent Protein Kinase III
- CAM Kinase III
- Cam PK III
- E-2 Kinase
- E 2 Kinase
- Protein Kinase CPK3
- Kinase CPK3, Protein
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Below are MeSH descriptors whose meaning is more general than "Elongation Factor 2 Kinase".
Below are MeSH descriptors whose meaning is more specific than "Elongation Factor 2 Kinase".
This graph shows the total number of publications written about "Elongation Factor 2 Kinase" by people in this website by year, and whether "Elongation Factor 2 Kinase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1987 | 0 | 1 | 1 | | 1990 | 0 | 1 | 1 | | 2012 | 1 | 0 | 1 | | 2013 | 1 | 0 | 1 | | 2021 | 1 | 0 | 1 |
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Below are the most recent publications written about "Elongation Factor 2 Kinase" by people in Profiles.
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Nabais Sá MJ, Olson AN, Yoon G, Nimmo GAM, Gomez CM, Willemsen MA, Millan F, Schneider A, Pfundt R, de Brouwer APM, Dinman JD, de Vries BBA. De Novo variants in EEF2 cause a neurodevelopmental disorder with benign external hydrocephalus. Hum Mol Genet. 2021 02 25; 29(24):3892-3899.
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Leprivier G, Remke M, Rotblat B, Dubuc A, Mateo AR, Kool M, Agnihotri S, El-Naggar A, Yu B, Somasekharan SP, Faubert B, Bridon G, Tognon CE, Mathers J, Thomas R, Li A, Barokas A, Kwok B, Bowden M, Smith S, Wu X, Korshunov A, Hielscher T, Northcott PA, Galpin JD, Ahern CA, Wang Y, McCabe MG, Collins VP, Jones RG, Pollak M, Delattre O, Gleave ME, Jan E, Pfister SM, Proud CG, Derry WB, Taylor MD, Sorensen PH. The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation. Cell. 2013 May 23; 153(5):1064-79.
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Hekman KE, Yu GY, Brown CD, Zhu H, Du X, Gervin K, Undlien DE, Peterson A, Stevanin G, Clark HB, Pulst SM, Bird TD, White KP, Gomez CM. A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult. Hum Mol Genet. 2012 Dec 15; 21(26):5472-83.
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Brady MJ, Nairn AC, Wagner JA, Palfrey HC. Nerve growth factor-induced down-regulation of calmodulin-dependent protein kinase III in PC12 cells involves cyclic AMP-dependent protein kinase. J Neurochem. 1990 Mar; 54(3):1034-9.
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Palfrey HC, Nairn AC, Muldoon LL, Villereal ML. Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients. J Biol Chem. 1987 Jul 15; 262(20):9785-92.
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