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Information on EC 2.7.11.20 - elongation factor 2 kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P15442

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IUBMB Comments
Requires Ca2+ and calmodulin for activity. The enzyme can also be phosphorylated by the catalytic subunit of EC 2.7.11.11, cAMP-dependent protein kinase. Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca2+ [1,2].
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Saccharomyces cerevisiae
UNIPROT: P15442
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
eef2k, eef-2k, eif2alpha kinase, eef-2 kinase, eef2 kinase, eukaryotic elongation factor 2 kinase, gcn2 kinase, eukaryotic elongation factor-2 kinase, elongation factor-2 kinase, elongation factor 2 kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
eukaryotic translation initiation factor 2alpha kinase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[elongation factor 2] phosphotransferase
Requires Ca2+ and calmodulin for activity. The enzyme can also be phosphorylated by the catalytic subunit of EC 2.7.11.11, cAMP-dependent protein kinase. Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca2+ [1,2].
CAS REGISTRY NUMBER
COMMENTARY hide
116283-83-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
show the reaction diagram
-
-
-
?
ATP + [elongation factor 3]
ADP + [elongation factor 3]phosphate
show the reaction diagram
-
-
-
-
?
ATP + [eukaryotic translation initiation factor 2alpha]
ADP + [eukaryotic translation initiation factor 2alpha]phosphate
show the reaction diagram
additional information
?
-
-
translation regulation mechanism
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
show the reaction diagram
-
-
-
?
ATP + [elongation factor 3]
ADP + [elongation factor 3]phosphate
show the reaction diagram
-
-
-
-
?
ATP + [eukaryotic translation initiation factor 2alpha]
ADP + [eukaryotic translation initiation factor 2alpha]phosphate
show the reaction diagram
-
GCN2 mediates translational control of gene expressionin amino acid-starved cells by phosphorylation of the eukaryotic translation initiation factor 2alpha associated to polyribosome and the regulatory GCN1-GCN20 complex, overview
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?
additional information
?
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translation regulation mechanism
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GCN1-GCN20
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positive effectors, uncharged tRNAs activate GCN2 requiring direct interaction with both the GCN1-GCN20 regulatory complex and ribosomes
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uncharged tRNAs
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activate GCN2 requiring direct interaction with both the GCN1-GCN20 regulatory complex and ribosomes
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additional information
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the eEF3-like domain has an effector function in GCN2 activation
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in response to amino acid starvation, GCN2 phosphorylation of eukaryotic initiation factor 2 leads to repression of general translation and initiation of gene reprogramming that facilitates adaptation to nutrient stress
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 5.5) and 21-28% (w/v) polyethylene glycol 2000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of GCN1 and GCN2 mutants with mutations in the domain structures that are involved in interaction between the GCNs, the elongation factors, and the polyribosome, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sattlegger, E.; Hinnebusch, A.G.
Polyribosome binding by GCN1 is required for full activation of eukaryotic translation initiation factor 2{alpha} kinase GCN2 during amino acid starvation
J. Biol. Chem.
280
16514-16521
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
He, H.; Singh, I.; Wek, S.; Dey, S.; Baird, T.; Wek, R.; Georgiadis, M.
Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals
J. Biol. Chem.
289
15023-15034
2014
Saccharomyces cerevisiae (P15442), Mus musculus (Q9QZ05)
Manually annotated by BRENDA team