Literature summary for 2.7.11.20 extracted from

Huber-Keener, K.J.; Evans, B.R.; Ren, X.; Cheng, Y.; Zhang, Y.; Hait, W.N.; Yang, J.M.
Phosphorylation of elongation factor-2 kinase differentially regulates the enzymes stability under stress conditions (2012), Biochem. Biophys. Res. Commun., 424, 308-314.

Search for more literature for 2.7.11.20

Protein Variants

Protein Variants	Comment	Organism
S398A	phosphorylation-defective mutant, mutation results in an increased stability under normal culture conditions, t1/2 is above 24 h	Homo sapiens
S78A/S366A	phosphorylation-defective mutant, mutation results in an increased stability under normal culture conditions, t1/2 is above 24 h	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	Ca2+/calmodulin-dependent enzyme	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + [elongation factor 2]	Homo sapiens	-	ADP + [elongation factor 2] phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	phosphorylation of the enzyme differentially affects the turnover of the enzyme under both normal and stress conditions. Phosphorylation control of the enzyme is a complex process, with a variety of signaling pathways converging on eEF-2K. The mTOR pathway deactivates the enzyme by phosphorylating the enzyme at Ser78 and Ser366, while the AMPK pathway activates eEF-2K through phosphorylation at Ser398 during cellular stress	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
glioma cell line	T98G and LN299	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [elongation factor 2]	-	Homo sapiens	ADP + [elongation factor 2] phosphate	-	?

Synonyms

Synonyms	Comment	Organism
EEF-2K	-	Homo sapiens
elongation factor-2 kinase	-	Homo sapiens

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Release 2023.1 (January 2023)