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ATP + a protein
ADP + a phosphoprotein
ATP + acetyl-RKKYKFNEDTERRRFL-amide
ADP + acetyl-RKKYKFNED(phospho)TERRRFL-amide
-
-
-
?
ATP + cortactin
ADP + phosphorylated cortactin
i.e. SRC8, an Src substrate, phosphorylation peptide sequence is EYQGK-T-EKHAS
-
-
?
ATP + heat shock protein 60
ADP + phosphorylated heat shock protein 60
i.e. HSPD1, phosphorylation peptide sequence is TKDGV-T-VAKSI
-
-
?
ATP + hematological and neurological expressed 1-like protein
ADP + phosphorylated hematological and neurological expressed 1-like protein
i.e. HN1L, phosphorylation peptide sequence is FGSPV-T-ATSRL
-
-
?
ATP + heterogeneous nuclear ribonucleoprotein A1
ADP + phosphorylated heterogeneous nuclear ribonucleoprotein A1
i.e. HNRNPA1, phosphorylation peptide sequence is VSRED-S-QRPGA
-
-
?
ATP + immunoglobulin-binding protein 1
ADP + phosphorylated immunoglobulin-binding protein 1
i.e. IGBP1, phosphorylation peptide sequence is EDDEQ-T-LHRAR
-
-
?
ATP + MH-1 peptide
ADP + phosphorylated MH-1 peptide
ATP + microtubule-associated protein 4
ADP + phosphorylated microtubule-associated protein 4
i.e. MAP4, phosphorylation peptide sequence is TEAAA-T-TRKPE
-
-
?
ATP + N-myc downstream-regulated gene 1 protein
ADP + phosphorylated N-myc downstream-regulated gene 1 protein
i.e. NDRG1, phosphorylation peptide sequence is TSLDG-T-RSRSH
-
-
?
ATP + PEST proteolytic signal-containing nuclear protein
ADP + phosphorylated PEST proteolytic signal-containing nuclear protein
i.e. PCNP, phosphorylation peptide sequence is AIGSQ-T-TKKAS
-
-
?
ATP + prothymosin alpha
ADP + phosphorylated prothymosin alpha
i.e. PTMA, phosphorylation peptide sequence is TSSEI-T-TKDLK
-
-
?
ATP + RKKFGESEKTKTKEFL
ADP + ?
-
-
-
-
?
ATP + SAP domain-containing ribonucleoprotein
ADP + phosphorylated SAP domain-containing ribonucleoprotein
i.e. SARNP, phosphorylation peptide sequence is GTTED-T-EAKKR
-
-
?
ATP + scaffold attachment factor B2
ADP + phosphorylated scaffold attachment factor B2
i.e. SAFB2, phosphorylation peptide sequence is VISVK-T-TSRSK
-
-
?
ATP + U4/U6 small nuclear ribonucleoprotein Prp31
ADP + phosphorylated U4/U6 small nuclear ribonucleoprotein Prp31
i.e. PRP31, phosphorylation peptide sequence is ERLGL-T-EIRKQ
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
ATP + [elongation factor 3]
ADP + [elongation factor 3]phosphate
-
-
-
-
?
ATP + [elongation translation factor 2]
ADP + [elongation translation factor 2]phosphate
-
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
ATP + [eukaryotic translation initiation factor 2alpha]
ADP + [eukaryotic translation initiation factor 2alpha]phosphate
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
ATP + [MHCK A peptide substrate]
ADP + [MHCK A peptide substrate] phosphate
-
i.e. YAYDTRYRR
-
-
?
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + MH-1 peptide
ADP + phosphorylated MH-1 peptide
-
-
-
?
ATP + MH-1 peptide
ADP + phosphorylated MH-1 peptide
-
the MH-1 peptide amino acid sequence is RKKFGESEKTKTKEFL
-
-
?
ATP + MH-1 peptide
ADP + phosphorylated MH-1 peptide
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
Thr348, and presumably its autophosphorylation, are critical for the ability of the enzyme to phosphorylate substrates in trans
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
the calmodulin-binding/alpha-kinase domain of the enzyme itself possesses autokinase activity, but is unable to phosphorylate substrates in trans. The phosphorylation of substrates in trans requires the SEL1-like domains of eEF2K
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
the recombinant human enzyme is able to phosphorylate wheat germ elongation factor 2 with kinetic parameters comparable to the mammalian enzyme
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
the enzyme phosphorylates elongation factor 2 at Ser56 and Thr58
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
the phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 is a key point of regulation of protein synthesis and amino acid homoeostasis in eukaryotes
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
phosphorylation at Thr57 inhibits the elongation factor 2 and blocks translational elongation, enzyme activity is regulated by rampamycin, 5-hydroxytryptamine, and serotonin, regulation mechanism
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
phosphorylation at Thr57 inhibits the elongation factor 2
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
enzyme regulation by de-/phosphorylation, overview
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
enzyme regulation via de-/phosphorylations, especially at Ser78, involving several kinases is dependent on the cellular amino acid status, enzyme regulation, overview
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
phosphorylation at Thr56
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
elongation factor 2 regulates the translation elongation through mTOR, p38, and MEK pathways, and is modulated through protein phosphatase 2A, overview
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
eukaryotic elongation factor 2 is inactivated when it is phosphorylated on Thr56 by the enzyme
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
the enzyme phosphorylates Thr56 of eukaryotic elongation factor 2
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
eEF2 is involved in eEF2 in neurite outgrowth regulation mechanism, since phosphorylated eEF2 inhibits mRNA translation via inhibition of eEF2-ribosome binding, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
eEF2 is involved in eEF2 in neurite outgrowth regulation mechanism, since phosphorylated eEF2 inhibits mRNA translation via inhibition of eEF2-ribosome binding, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
high glucose and high insulin regulate phosphorylation of eEF2 and eEF2 kinase by rapidly increasing activating Thr56 dephosphorylation of eEF2 and inactivating Ser366 phosphorylation of eEF2 kinase, events that facilitate elongation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, regulation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
the enzyme is involved in eukaryotic elongation factor 2 kinase in ER stress-induced signaling and cell death by inducing stress factors, regulation cascade, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the reaction leads to derepression of transcription factor GCN4
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
i.e. eEF2, both AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, phosphorylate eEF2, thus two distinct paths lead to eEF2 phosphorylation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the enzyme exhibits strong preference for threonine as the phosphoacceptor amino acid, substrate specificity and phosphoacceptor amino acid specificity, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the reaction leads to derepression of transcription factor GCN4
-
-
?
ATP + [eukaryotic translation initiation factor 2alpha]
ADP + [eukaryotic translation initiation factor 2alpha]phosphate
-
-
-
-
?
ATP + [eukaryotic translation initiation factor 2alpha]
ADP + [eukaryotic translation initiation factor 2alpha]phosphate
-
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
-
-
?
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
-
-
-
?
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
-
-
-
?
additional information
?
-
-
SCH66336, a farnesyltransferase inhibitor, induces rapid phosphorylation and inhibition of eukaryotic translation elongation factor 2 in head and squamous cell carcinoma cells leading to growth inhibition in the cancer cells, the inhibitor functions independently of the signaling cascade involving the eEF2 kinase and its activators phosphorylated p70S6K and phosphorylated MEK
-
-
?
additional information
?
-
-
the enzyme expression and activity is increased in several forms of malignancy and human cancer, non-specific inhibitors of the enzyme cause cell death
-
-
?
additional information
?
-
-
the enzyme regulates protein synthesis in skeletal muscle
-
-
?
additional information
?
-
-
unphosphorylated elongation factor 2 promotes translational elongation, phosphorylation by the eEF2-kinase inhibits it, eEF2-kinase phosphorylated elongation factor 2 is further phosphorylated by cAMP-dependent protein kinase, EC 2.7.11.11, upon forskolin treatment leading to inhibition of elongation of cyclin D3 in T-lymphocytes, overview
-
-
?
additional information
?
-
the calcium/calmodulin-dependent kinase phosphorylates and inactivates eukaryotic elongation factor 2 and is subject to multisite phosphorylation, which regulates its activity. Phosphorylation at Ser359 by cyclin-dependent kinase 1, as cdc2cyclin B complexe, inactivates the enzyme occuring early in mitosis probably to keep the elongation factor 2 active during mitosis, overview
-
-
?
additional information
?
-
mammalian enzyme elongation factor-2 kinase (eEF2K) a requirement for threonine residues as the target of phosphorylation
-
-
?
additional information
?
-
the enzyme performs autophosphorylation at Thr57. Additional enzyme protein substrates show a strong sequence motif consisting of acidic residues in the -2 position and basic residues in the +3 position and almost exclusively threonine as the phosphorylated residue, peptide mapping and mass spectrometry analysis, overview
-
-
?
additional information
?
-
the enzyme performs autophosphorylation on residue Thr348
-
-
?
additional information
?
-
the enzyme performs autophosphorylation
-
-
?
additional information
?
-
-
rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes
-
-
?
additional information
?
-
-
the GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of the essential amino acid leucine, thus, the enzyme acts as sensor for amino acid deficiency, overview
-
-
?
additional information
?
-
-
a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by eEF-2K, eEF-2K requires basic residues in both the P+1 and P+3 positions to recognize peptide substrates, overview
-
-
?
additional information
?
-
-
non-muscle myosin II is a poor substrate for eEF-2 kinase, while eukaryotic elongation factor 2 is no substrate of kinase TRPM7
-
-
?
additional information
?
-
-
the GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of the essential amino acid leucine, thus, the enzyme acts as sensor for amino acid deficiency, overview
-
-
?
additional information
?
-
-
translation regulation mechanism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
ATP + [elongation factor 3]
ADP + [elongation factor 3]phosphate
-
-
-
-
?
ATP + [elongation translation factor 2]
ADP + [elongation translation factor 2]phosphate
-
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
ATP + [eukaryotic translation initiation factor 2alpha]
ADP + [eukaryotic translation initiation factor 2alpha]phosphate
-
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
-
-
?
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
additional information
?
-
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
the enzyme phosphorylates elongation factor 2 at Ser56 and Thr58
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
the phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 is a key point of regulation of protein synthesis and amino acid homoeostasis in eukaryotes
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
phosphorylation at Thr57 inhibits the elongation factor 2 and blocks translational elongation, enzyme activity is regulated by rampamycin, 5-hydroxytryptamine, and serotonin, regulation mechanism
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
enzyme regulation by de-/phosphorylation, overview
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
enzyme regulation via de-/phosphorylations, especially at Ser78, involving several kinases is dependent on the cellular amino acid status, enzyme regulation, overview
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
phosphorylation at Thr56
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
-
elongation factor 2 regulates the translation elongation through mTOR, p38, and MEK pathways, and is modulated through protein phosphatase 2A, overview
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
eukaryotic elongation factor 2 is inactivated when it is phosphorylated on Thr56 by the enzyme
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
the enzyme phosphorylates Thr56 of eukaryotic elongation factor 2
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
eEF2 is involved in eEF2 in neurite outgrowth regulation mechanism, since phosphorylated eEF2 inhibits mRNA translation via inhibition of eEF2-ribosome binding, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
eEF2 is involved in eEF2 in neurite outgrowth regulation mechanism, since phosphorylated eEF2 inhibits mRNA translation via inhibition of eEF2-ribosome binding, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
high glucose and high insulin regulate phosphorylation of eEF2 and eEF2 kinase by rapidly increasing activating Thr56 dephosphorylation of eEF2 and inactivating Ser366 phosphorylation of eEF2 kinase, events that facilitate elongation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, regulation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
the enzyme is involved in eukaryotic elongation factor 2 kinase in ER stress-induced signaling and cell death by inducing stress factors, regulation cascade, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the reaction leads to derepression of transcription factor GCN4
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the reaction leads to derepression of transcription factor GCN4
-
-
?
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
-
-
-
?
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
-
-
-
?
additional information
?
-
-
SCH66336, a farnesyltransferase inhibitor, induces rapid phosphorylation and inhibition of eukaryotic translation elongation factor 2 in head and squamous cell carcinoma cells leading to growth inhibition in the cancer cells, the inhibitor functions independently of the signaling cascade involving the eEF2 kinase and its activators phosphorylated p70S6K and phosphorylated MEK
-
-
?
additional information
?
-
-
the enzyme expression and activity is increased in several forms of malignancy and human cancer, non-specific inhibitors of the enzyme cause cell death
-
-
?
additional information
?
-
-
the enzyme regulates protein synthesis in skeletal muscle
-
-
?
additional information
?
-
-
unphosphorylated elongation factor 2 promotes translational elongation, phosphorylation by the eEF2-kinase inhibits it, eEF2-kinase phosphorylated elongation factor 2 is further phosphorylated by cAMP-dependent protein kinase, EC 2.7.11.11, upon forskolin treatment leading to inhibition of elongation of cyclin D3 in T-lymphocytes, overview
-
-
?
additional information
?
-
the calcium/calmodulin-dependent kinase phosphorylates and inactivates eukaryotic elongation factor 2 and is subject to multisite phosphorylation, which regulates its activity. Phosphorylation at Ser359 by cyclin-dependent kinase 1, as cdc2cyclin B complexe, inactivates the enzyme occuring early in mitosis probably to keep the elongation factor 2 active during mitosis, overview
-
-
?
additional information
?
-
mammalian enzyme elongation factor-2 kinase (eEF2K) a requirement for threonine residues as the target of phosphorylation
-
-
?
additional information
?
-
-
rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes
-
-
?
additional information
?
-
-
the GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of the essential amino acid leucine, thus, the enzyme acts as sensor for amino acid deficiency, overview
-
-
?
additional information
?
-
-
the GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of the essential amino acid leucine, thus, the enzyme acts as sensor for amino acid deficiency, overview
-
-
?
additional information
?
-
-
translation regulation mechanism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(4-[[4-(1H-benzimidazol-5-ylamino)-5-(trifluoromethyl)pyrimidin-2-yl]amino]benzene-1,2-diyl)dicyanamide
-
1,1'-(cyclopropane-1,1-diyldisulfonyl)bis(4-chlorobenzene)
-
-
1-benzyl-3-cetyl-2-methylimidazolium iodide
1-[3-[(5,6,7-trimethyl-2-phenyl-7H-cyclopenta[d]pyrimidin-4-yl)amino]propyl]pyrrolidin-2-one
-
2,6-diamino-4-(2-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2-((3,5-di-tert-butyl-4-hydroxyphenyl)-methylene)-4-cyclopentene-1,3-dione
-
TX-1123
2-((3,5-dimethyl-4-hydroxyphenyl)-methylene)-4-cyclopentene-1,3-dione
-
TX-1918
2-((3-cyano-4-(4-methoxyphenyl)pyridine-2-ylthio)-2-phenylacetic)acid
-
2-chloro-4-hydroxy-5-(3-phenoxyphenyl)-7,7a-dihydrothieno[2,3-b]pyridin-6(3aH)-one
21% inhibition at 0.05 mM
3-([4-[(5-methoxy-2-methylphenyl)amino]pyrimidin-2-yl]amino)benzamide
36% inhibition at 0.05 mM
3-amino-4-(furan-2-yl)-6,7,8,9,10,11-hexahydro-5H-cyclonona[b]thieno[3,2-e]pyridine-2-carboxamide
3-phenyl-7-(pyrrolidin-1-yl)-2,3-dihydro-1H-inden-1-one
-
-
3-[4-(pyridin-4-yl)-1,3-thiazol-2-yl]-3,4-dihydroquinazolin-2(1H)-one
48% inhibition at 0.05 mM
3-[[(6-bromonaphthalen-1-yl)oxy]methyl]-1-methyl-4-phenylpiperidine
-
-
4-(4-amino-2-methylphenyl)-N-methylpyridin-2-amine
75% inhibition at 0.05 mM
4-benzyl-N-(2,4-difluorophenyl)-1,4-diazepane-1-carboxamide
-
-
7-amino-1-cyclopropyl-3-ethyl-1,2,3,4-tetrahydro-2,4-dioxo-pyrido[2,3-d]pyrimidine-6-carboxamide
inhibits eEF2 phosphorylation in cells as well as in vitro
7-amino-1-cyclopropyl-3-ethyl-1,2,3,4-tetrahydro-2,4-dioxopyrido[2,3-d]pyrimidine-6-carboxamide
-
A-484954, highly selective inhibitor
7-amino-1-cyclopropyl-3-ethyl-2,4-dioxo-1,2,3,4-tetrahydropyrido[2,3-d] pyrimidine-6-carboxamide
7-amino-1-cyclopropyl-3-ethyl-2,4-dioxo-1,2,3,4-tetrahydropyrido[2,3-d]pyrimidine-6-carboxamide
-
inhibits eEF2 phosphorylation in cells as well as in vitro
bombesin
-
a secretagogue, increases elongation rates, and decreases elongation factor 2 phosphorylation
Carbachol
-
a secretagogue, increases elongation rates, and decreases elongation factor 2 phosphorylation
Cholecystokinin
-
a secretagogue, increases elongation rates, increases phosphorylation of eEF2 kinase, and decreases elongation factor 2 phosphorylation reversed by rapamycin, PD98059, calyculin, or SB202190
compound C
-
AMPK inhibitor compound C blocks eEF2K and eEF2 phosphorylation
ethanol
-
decreases phosphorylation of eEF2K, whereas elongation factor 2 phosphorylation increases, but this response is not mediated by eEF2K
JAN-849
potent inhibitor
-
lopinavir
-
i.e. LPV, increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview
N,N'-bis(2-methylphenyl)quinazoline-2,4-diamine
-
N-(2,6-dimethylphenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-methoxyphenyl]urea
-
N-(2,6-dimethylphenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]urea
8.7% inhibition at 0.02 mM
N-(2-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]urea
53.6% inhibition at 0.02 mM
N-(2-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-methoxyphenyl]urea
6.4% inhibition at 0.02 mM
N-(2-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]urea
21.7% inhibition at 0.02 mM
N-(2-hydroxyethyl)-1-(4-[(E)-[(7-hydroxy-6H-[1,3]thiazolo[5,4-e]indol-8-yl)methylidene]amino]phenyl)methanesulfonamide
-
N-(3-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]urea
82.7% inhibition at 0.02 mM
N-(3-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-fluorophenyl]urea
52.5% inhibition at 0.02 mM
N-(3-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-methoxyphenyl]urea
30.6% inhibition at 0.02 mM
N-(3-chlorophenyl)-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]urea
73.4% inhibition at 0.02 mM
N-(3-chlorophenyl)-N'-[4-[2-(propylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]urea
38.2% inhibition at 0.02 mM
N-(3-chlorophenyl)-N'-[4-[2-[(cyclopropylmethyl)amino]pyridin-4-yl]-3-(trifluoromethyl)phenyl]urea
27.8% inhibition at 0.02 mM
N-dodecyl-N,N-dimethyl-9H-fluoren-9-aminium bromide
-
-
N-[3,5-bis(trifluoromethyl)phenyl]-N'-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]urea
37.2% inhibition at 0.02 mM
N-[4-([4-(azetidin-1-yl)-6-[(3-methyl-1H-pyrazol-5-yl)amino]pyrimidin-2-yl]sulfanyl)phenyl]propanamide
-
N-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]-N'-(4-methoxyphenyl)urea
51.3% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]-N'-(4-methylphenyl)urea
37.9% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]-N'-[4-(naphthalen-2-yl)phenyl]urea
44% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]-N'-[4-(trifluoromethyl)phenyl]urea
76.3% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-fluorophenyl]-N'-(4-methoxyphenyl)urea
34.4% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-fluorophenyl]-N'-[4-(trifluoromethyl)phenyl]urea
41.2% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-methoxyphenyl]-N'-(4-methoxyphenyl)urea
9.0% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-methoxyphenyl]-N'-[4-(trifluoromethyl)phenyl]urea
34.6% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]-N'-(4-methoxyphenyl)urea
33.4% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]-N'-(4-methylphenyl)urea
35.4% inhibition at 0.02 mM
N-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]-N'-[4-(naphthalen-2-yl)phenyl]urea
-
N-[4-[2-(ethylamino)pyridin-4-yl]-3-methylphenyl]-N'-[4-(trifluoromethyl)phenyl]urea
55.3% inhibition at 0.02 mM
N-[4-[2-(propylamino)pyridin-4-yl]-3-(trifluoromethyl)phenyl]-N'-[4-(trifluoromethyl)phenyl]urea
33.3% inhibition at 0.02 mM
N-[4-[2-[(cyclopropylmethyl)amino]pyridin-4-yl]-3-(trifluoromethyl)phenyl]-N'-[4-(trifluoromethyl)phenyl]urea
15.1% inhibition at 0.02 mM
N2,N2-dimethyl-6-[[(2-phenoxyethyl)amino]methyl]-N4-[(1S)-1-phenylethyl]-1,3,5-triazine-2,4-diamine
-
serotonin
-
inhibits the enzyme in synaptosomes and in isolated neurites, antagonizes rapamycin/5-hydroxytryptamine, mechanism
TX1918
i.e. 2-((3,5-dimethyl-4-hydroxyphenyl)-methylene)-4-cyclopentene-1,3-dione
-
1-benzyl-3-cetyl-2-methylimidazolium iodide
-
i.e. NH125, inhibits in vitro, but is not a cellular inhibitor elongation factor 2 kinase
1-benzyl-3-cetyl-2-methylimidazolium iodide
i.e. NH125, inhibits eEF2K activity via inhibition of alpha-kinase, a catalytic domain of eEF2K
1-benzyl-3-cetyl-2-methylimidazolium iodide
-
NH125
1-benzyl-3-cetyl-2-methylimidazolium iodide
i.e. NH125, inhibits eEF2K activity via inhibition of alpha-kinase, a catalytic domain of eEF2K. In mesenteric artery from spontaneously hypertensive rats, the acetylcholine-induced endothelium-dependent relaxation is significantly impaired after long-term treatment with the inhibitor
2,6-diamino-4-(2-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
-
-
2,6-diamino-4-(2-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
-
2-((3-cyano-4-(4-methoxyphenyl)pyridine-2-ylthio)-2-phenylacetic)acid
-
-
-
2-((3-cyano-4-(4-methoxyphenyl)pyridine-2-ylthio)-2-phenylacetic)acid
-
-
3-amino-4-(furan-2-yl)-6,7,8,9,10,11-hexahydro-5H-cyclonona[b]thieno[3,2-e]pyridine-2-carboxamide
-
-
3-amino-4-(furan-2-yl)-6,7,8,9,10,11-hexahydro-5H-cyclonona[b]thieno[3,2-e]pyridine-2-carboxamide
-
7-amino-1-cyclopropyl-3-ethyl-2,4-dioxo-1,2,3,4-tetrahydropyrido[2,3-d] pyrimidine-6-carboxamide
i.e. A-484954, a pyrido-pyrimidinedione derivative that inhibits eEF2K in an ATP-competitive but CaM-independent manner
7-amino-1-cyclopropyl-3-ethyl-2,4-dioxo-1,2,3,4-tetrahydropyrido[2,3-d] pyrimidine-6-carboxamide
i.e. A-484954, a pyrido-pyrimidinedione derivative that inhibits eEF2K in an ATP-competitive but CaM-independent manner
A-484954
-
-
A484954
-
-
-
A484954
highly selective inhibitor, i.e. 7-amino-1-cyclopropyl-3-ethyl-1,2,3,4-tetrahydro-2,4-dioxopyrido[2,3-d]pyrimidine-6-carboxamide
-
JAN-384
-
-
JAN-384
a JAN-384 highly selective eEF2K inhibitor, comparison to inhibition of other protein kinases
-
JAN-452
less potent inhibitor
-
JAN-452
slight inhibition
-
NH125
-
an imidazolium histidine kinase inhibitor also inhibits the eukaryotic eEF-2 kinase enzyme in vitro and in vivo, IC50 is 60 nM, decreases viability of cancer cell lines with IC50S of 0.0007 to 0.0048 mM, overview
NH125
-
i.e. 1-benzyl-3-acetyl-2-methylimidazolium iodide
NH125
i.e. 1-benzyl-3-acetyl-2-methylimidazolium iodide
NH125
1-benzyl-3-cetyl-2-methylimidazolium iodide
rottlerin
-
unspecific inhibition
rottlerin
-
i.e. 1-[6-[(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)methyl]-5,7-dihydroxy-2,2-dimethyl-2H-1-benzopyran-8-yl]-3-phenyl-2-propen-1-one, mallotoxin
rottlerin
i.e. 1-[6-[(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)methyl]-5,7-dihydroxy-2,2-dimethyl-2H-1-benzopyran-8-yl]-3-phenyl-2-propen-1-one, mallotoxin
rottlerin
-
blocks the effects of stimulators AICAR and FBS
rottlerin
unspecific inhibition
shRNA
-
decreases eEF-2 kinase expression by 90%
-
shRNA
-
eEF2K protein levels are 8fold reduced
-
siRNA
-
knockdown of eEF-2 kinase and inhibition of autophagy in several cell types
-
siRNA
-
decreases eEF-2 kinase expression by 90%, inhibition of autophagy in several cell types
-
siRNA
-
eEF2K protein levels are decreased ca. 90% in cells transfected with eEF2K siRNA and unaltered by NS siRNA
-
TS2
-
1,3-selenazine derivative
TS2
-
i.e. 4-ethyl-4-hydroxy-2-p-tolyl-5,6-dihydro-4H-1,3-selenazine
TS2
i.e. 4-ethyl-4-hydroxy-2-p-tolyl-5,6-dihydro-4H-1,3-selenazine
TS4
-
1,3-selenazine derivative
TS4
-
i.e. 4-hydroxy-6-isopropyl-4-methyl-2-p-tolyl-5,6-dihydro-4H-1,3-selenazine
TS4
i.e. 4-hydroxy-6-isopropyl-4-methyl-2-p-tolyl-5,6-dihydro-4H-1,3-selenazine
TX-1123
-
inhibits eEF2K, but also affects the activity of tyrosine kinases and exhibits mitochondrial toxicity
TX-1123
inhibits eEF2K, but also affects the activity of tyrosine kinases and exhibits mitochondrial toxicity
additional information
-
phosphorylation by p70-S6 kinase inhibits EF2K, Ca2+ decreases the phosphorylation of the enzyme
-
additional information
-
non-specific inhibitors of the enzyme cause cell death
-
additional information
-
inhibition of elongation factor 2 phosphorylation by the eEF2-kinase prevents the forskolin-induced down-regulation of cyclin D3 elongation
-
additional information
-
eEF2K can be directly inhibited by mTOR phosphorylation and indirectly inhibited by mTOR through p70S6k phosphorylation
-
additional information
phosphorylation at Ser359 by cyclin-dependent kinase 1, as cdc2-cyclin B complex, inhibits eEF2K activity
-
additional information
-
eEF2K activity is also regulated by phosphorylation. Ser366 is phosphorylated by S6 kinases, enzymes which are phosphorylated and activated by mTORC1, phosphorylation at this site desensitizes eEF2K to activation by Ca2+/CaM. Phosphorylation of Ser359, a site whose modification strongly inhibits eEF2K, and Ser78, immediately next to the CaM-binding motif, are also promoted by mTORC1. The latter strongly impairs the interaction of eEF2K with CaM thereby impairing its activation
-
additional information
the enzyme is not inhibited by staurosporine
-
additional information
the C-terminal fragment of the enzyme, eEF-2K562-725, is able to inhibit the phosphorylation of eukaryotic elongation factor 2 by full-length enzyme in trans
-
additional information
-
rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes
-
additional information
-
no effect by CPT-cAMP and A23187
-
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evolution
eEF2K is a calcium/calmodulin dependent kinase that belongs to the alpha kinase family, which has negligible sequence identity to the conventional protein kinase family
evolution
-
eukaryotic elongation factor 2 kinase (eEF2K) is a member of the small group of atypical alpha-kinases, eEF2K is not a member of the main kinase superfamily. alpha-Kinases show no sequence similarity to the main protein kinase superfamily, although they do display limited three-dimensional structural similarity
evolution
eukaryotic elongation factor 2 kinase (eEF2K) is a member of the small group of atypical alpha-kinases, eEF2K is not a member of the main kinase superfamily. alpha-Kinases show no sequence similarity to the main protein kinase superfamily, although they do display limited three-dimensional structural similarity
evolution
eukaryotic elongation factor 2 kinase is a member of the atypical alpha-kinase family
malfunction
-
in vivo studies with Gcn2 knockout mice show increased susceptibility to both acute or chronic liver damage induced by CCl4, as shown by higher alanine aminotransferase and aspartate aminotransferase activities, increased necrosis and higher inflammatory infiltrates compared with wild-type mice. Chronic CCl4 treatment increases deposition of interstitial collagen type I. Col1a1 and col1a2 mRNA levels also increase in CCl4-treated Gcn2-/- mice compared with wild-type mice
malfunction
-
loss of GCN2 enhances immunosuppression by asparaginase
malfunction
eEF2K gene knockdown on TNF-alpha-induced inflammatory responses in HUVECs
malfunction
eEF2K-knockout mice are viable and fertile under standard vivarium conditions. mGluR-induced long-term depression (LTD), but not LTD induced by other stimuli, is impaired in eEF2K knockout mice. The memory deficits in eEF2K knock-in mice are due to sleep-related alterations. Fear-conditioning responses in mice are deficient in eEF2K activity
malfunction
enzyme silencing with eEF2K siRNA inhibits phosphorylation of JNK and NF-kappaB p65 as well as reactive oxygen species (ROS) production by TNF-alpha. In vascular smooth muscle cells, eEF2K siRNA also inhibits VCAM-1 induction and phosphorylation of JNK and NF-kappaB by TNF-alpha. In vascular endothelial cells, siRNA against eEF2K inhibited induction of VCAM-1 and endothelial-selectin as well as monocyte adhesion by TNF-alpha. Phenotypes, overview
malfunction
kinase-dead and other activity-deficient mutants of eEF2K are stabilized, as is a mutant lacking a critical autophosphorylation site (Thr348 in eEF2K), which is thought to be required for eEF2K and other alpha-kinases to achieve their active conformations. In contrast, application of small-molecule eEF2K inhibitors does not stabilize the protein. Achieving an active conformation, rather than eEF2K activity per se, is required for its susceptibility to degradation
malfunction
knockdown of eEF-2K expression leads to a significant increase in phosphatase 2A-A (PP2A-A) protein synthesis and remarkable downregulation of c-Myc and pyruvate kinase M2 isoform, the key glycolytic enzyme transcriptionally activated by c-Myc. In addition, depletion of eEF-2K reduces the ability of the transformed cells to proliferate and enhance the sensitivity of tumor cells to chemotherapy both in vitro and in vivo. The glucose level is significantly higher in the conditioned medium of the cells with eEF-2K knockdown than that of the control cells. Activation of adenosine monophosphate-activated protein kinase, which increases phosphorylation of AMPK at Thr172, is observed in the cells subjected to silencing of eEF-2K expression. Downregulation of PKM2 mRNA and protein in the cells deficient in eEF-2K, but Overexpression of c-Myc reverses the eEF-2K-mediated downregulation of PKM2 mRNA expression. Silencing of eEF-2K expression blunts the hypoxia-stimulated glycolysis and reduces survival of hypoxic tumor cells. Phenotype, overview
malfunction
-
knocking down eEF2K in hippocampal neurons inhibits synaptic activity induced increases in BDNF production and decreases the stability of dendritic spines
malfunction
knockout of eEF2K protects mice from a lethal dose of whole-body ionizing radiation at 8 Gy by reducing apoptosis levels in both bone marrow and gastrointestinal tracts. eEF2K deficiency results in more severe damage to the gastrointestinal tract at 20 Gy with the increased mitotic cell death in small intestinal stem cells. Elevation of Akt/ERK activity as well as the reduction of p21 expression occur in Eef2k-/- cells Eef2k-/- mice display opposite sensitivities at low dose and high dose of ionizing radiation according to tissue and cell types, overview. Consistent with the role of eEF2K in apoptosis, cleaved caspase-3-positive and TUNEL-positive cells are reduced in Eef2k-deficient mice
malfunction
mutation of the hydrophobic CaM anchor on eEF-2K disrupts its cellular activity. Mutation of residue W85 to S85 substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells
malfunction
processes related to microtubules are particularly sensitive to eEF2K inhibition
malfunction
enzyme deficiency leads to impaired mGluR-long term potentiation, higher miniature inhibitory postsynaptic current frequency and amplitude in hippocampal granule cells, higher tonic inhibition measured in the in granule cells of the dentate gyrus, and impaired AMPAR-endocytosis following mGluR activation. The heterozygous deletion of the enzyme in mice models of Alzheimer's disease rescue cognitive, morphological and electrophysiological alterations associated to Alzheimer's disease
malfunction
enzyme gene knockdown significantly augments glucose deprivation-induced cleavage of caspase-3 and apoptotic nuclear condensation. In contrast, enzyme gene knockdown significantly inhibits glucose deprivation-induced increase of microtubule-associated protein 1 light chain 3-II to -I ratio and autophagosome formation. Enzyme gene knockdown significantly inhibits GD-induced phosphorylation of adenosine monophosphate-activated protein kinase alpha and its downstream substrate, unc-51 like autophagy activating kinase 1
malfunction
enzyme silencing blunts autophagic responses, but promotes doxorubicin-induced pyroptotic cell death in melanoma cells. Enzyme suppressionresults in inhibiting autophagy and augmenting pyroptosis, thus modulating the sensitivity of melanoma cells to doxorubicin
malfunction
inhibiting the enzyme or knocking down its expression renders cancer cells sensitive to death under nutrient-starved conditions
malfunction
-
inhibition of the enzyme markedly augments cell proliferation and differentiation, suppresses apoptosis and autophagy, and reverses the anti-fibrotic effects of a p38 MAPK inhibitor. Enzyme inhibition induces resistance to apoptosis in MRC-5 cells treated with transforming growth factor beta 1
malfunction
knocking down or inhibiting the enzyme in cancer cells impairs migration and invasion of cancer cells
malfunction
-
pharmacological inhibition or knockdown of the enzyme in highly metastatic liver cancer cells inhibits their colony forming and migratory capacities, as well as reducing their invasiveness. Knocking down the enzyme reduces the expression of angiogenesis-related growth factors in liver cancer cells and the expression of growth factor receptors on HUVEC cells, and thus restricts signalling crosstalk that promotes angiogenesis between hepatocellular carcinoma cells and endothelial cells
malfunction
-
processes related to microtubules are particularly sensitive to eEF2K inhibition
-
malfunction
-
enzyme silencing with eEF2K siRNA inhibits phosphorylation of JNK and NF-kappaB p65 as well as reactive oxygen species (ROS) production by TNF-alpha. In vascular smooth muscle cells, eEF2K siRNA also inhibits VCAM-1 induction and phosphorylation of JNK and NF-kappaB by TNF-alpha. In vascular endothelial cells, siRNA against eEF2K inhibited induction of VCAM-1 and endothelial-selectin as well as monocyte adhesion by TNF-alpha. Phenotypes, overview
-
metabolism
eEF2K is degraded by a proteasome-dependent pathway in response to genotoxic stress requiring a phosphodegron that includes an autophosphorylation site. The enzyme is also degraded under stress like including acidosis or treatment of cells with 2-deoxyglucose not requiring a phosphodegron
metabolism
the eEF2K protein is degraded via a proteasome-dependent pathway
metabolism
-
the eEF2K protein is degraded via a proteasome-dependent pathway, e.g., during normoxia in breast cancer cells or in response to inhibition of hsp90, which acts as a chaperone for eEF2K. Degradation of eEF2K requires the autophosphorylation site at Ser445, which forms part of a typical bTrCP-binding motif or phosphodegron
physiological function
-
the eIF2 kinase GCN2 is essential for the murine immune system to adapt to amino acid deprivation by asparaginase
physiological function
-
the enzyme has a key role in collagen type I production by hepatic stellate cells
physiological function
-
the enzyme is a key regulator of the fibrogenic response to liver injury
physiological function
-
the enzyme is implicated in induction of apoptosis and endoplasmic reticulum stress-responsive genes by sodium salicylate
physiological function
-
the enzyme plays an important role in the regulation of genes encoding enzymes of amino acid biosynthesis in wheat. The enzyme is implicated in sulfur signalling
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
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
physiological function
eEF2K appears to be a non-essential gene
physiological function
eEF2K likely contributes to neuronal function by regulating the synthesis of microtubule-related proteins. Phosphorylation of elongation factor 2, EF2, results in slower elongation which then result in the increased synthesis of specific proteins. Expression levels of eEF2K targets with unaltered, enhanced, and reduced eEF2K enzyme activity, overview. Synthesis of MAP1B, ARC, and CAMKIIa is sensitive to eEF2K inhibition
physiological function
-
eEF2K phosphorylates and inhibits eukaryotic elongation factor 2, to slow down the elongation stage of protein synthesis, which normally consumes a great deal of energy and amino acids.. eEF2K is dependent on Ca2+ and calmodulin, and is also regulated by a plethora of other inputs, including inhibition by signalling downstream of anabolic signalling pathways such as the mammalian target of rapamycin complex 1. Enzyme eEF2K helps to protect cancer cells against nutrient starvation and is also cytoprotective in other settings, including hypoxia. Roles for eEF2K in neurological processes such as learning and memory and perhaps in depression. Regulation by phosphorylation of eukaryotic elongation factor 2 (eEF2), overview. In addition to being dependent upon Ca2+/calmodulin, eEF2K activity is also regulated by phosphorylation, which occurs at several sites downstream of various signalling pathways. eEF2K activity is negatively regulated by signalling through the mammalian target of rapamycin complex 1 (mTORC1). Consequence of increasing eEF2K activity in the brain may be to regulate the synthesis of specific proteins. Increases in eEF2K activity are important for the synthesis of Arc, an immediate-early gene involved in the trafficking of glutamate receptors and cytoskeletal rearrangement that is implicated in various types of synaptic plasticity and memory. Stimulation of metabotropic glutamate receptors (mGluRs) results in an eEF2Kdependent increase in Arc synthesis
physiological function
elongation factor-2 kinase (eEF2K), a protein kinase that suppresses protein synthesis during elongation phase, is a positive regulator of apoptosis both in vivo and in vitro. eEF2K is required for G2/M arrest induced by radiation to prevent mitotic catastrophe in a p53-independent manner in epithelial cells. eEF2K also provides a protective strategy to maintain genomic integrity by arresting cell cycle in response to stress. Protective versus pro-apoptotic roles of eEF2K depend on the type of cells: eEF2K is protective in highly proliferative cells, such as small intestinal stem cells and cancer cells, which are more susceptible to mitotic catastrophe. The dynamics of eEF2K activity in DNA damage response is distinct in different cell types and are related to cell proliferating status. eEF2K suppresses intestinal mitotic cell death in response to gamma-irradiation
physiological function
eukaryotic elongation factor 2 kinase (eEF-2K) phosphorylates eEF-2 leading to a decrease in global protein synthesis
physiological function
eukaryotic elongation factor 2 kinase (eEF2K) is an atypical protein kinase which negatively regulates protein synthesis, is activated under stress conditions and plays a role in cytoprotection, e.g. in cancer cells
physiological function
eukaryotic elongation factor 2 kinase (eEF2K) prevents binding of eEF to the ribosome via phosphorylation of eEF and thus prevents further translation. The enzyme regulates the development of hypertension through oxidative stress-dependent vascular inflammation
physiological function
eukaryotic elongation factor 2 kinase (eEF2K) prevents binding of eEF to the ribosome via phosphorylation of eEF and thus prevents further translation. The enzyme regulates the development of hypertension through oxidative stress-dependent vascular inflammation. eEF2K protein increases in mesenteric artery from spontaneously hypertensive rats. Enzyme eEF2K mediates TNF-alpha-induced vascular inflammation via reactive oxygen species-dependent mechanism, which is at least partly responsible for the development of hypertension in spontaneously hypertensive rats
physiological function
phosphorylation of eEF-2 by eEF-2K is an essential system in regulation of global protein synthesis. Cancer cells predominantly metabolize glucose by glycolysis to produce energy in order to meet their metabolic requirement, a phenomenon known as Warburg effect. Enzyme eEF-2 kinase is a critical regulator of Warburg effect through controlling synthesis of protein phosphatase 2A-A (PP2A-A), a key factor that facilitates the ubiquitin-proteasomal degradation of c-Myc protein. Eukaryotic elongation factor-2 kinase (eEF-2K) has a negative regulator of protein synthesis, has a critical role in promoting glycolysis in cancer cells. eEF-2K is required for the hypoxia-stimulated glycolysis and promotes survival of hypoxic tumor cells. Enzyme eEF-2K activates PKM2 through stabilizing c-Myc protein, MG132, a proteasome inhibitor, can rescue the downregulation of c-Myc in the cells with knockdown of eEF-2K expression. eEF-2K is supportive to growth and proliferation of tumor cells
physiological function
the phosphorylation of eEF2 through eEF2 kinase blocks translation elongation, which is thought to be critical to regulating cellular energy usage. eEF2K has a role in regulating cellular energy usage that involves multiple pathways and regulatory feedback
physiological function
transcription elongation is controlled by phosphorylation of eukaryotic elongation factor 2 (eEF2), which inhibits its activity and is catalyzed by eEF2 kinase (eEF2K), a calcium/calmodulin-dependent alpha-kinase. eEF2K activity is regulated through several signaling pathways linked, e.g., to nutrient availability. Hypoxia causes the activation of eEF2K and induces eEF2 phosphorylation. eEF2K is subject to hydroxylation on proline 96. Proline hydroxylation is catalyzed by proline hydroxylases, oxygen-dependent enzymes which are inactivated during hypoxia. Hypoxia-induced eEF2 phosphorylation requires eEF2K and is not catalyzed by AMPK, it does also not require signaling via AMPK or mTORC1. Pharmacological inhibition of proline hydroxylases, e.g. by DMOG treatment, also stimulates eEF2 phosphorylation. Pro96 lies in a universally conserved linker between the calmodulin-binding and catalytic domains of eEF2K. Its hydroxylation partially impairs the binding of calmodulin to eEF2K and markedly limits the calmodulin-stimulated activity of eEF2K. Neuronal cells depend on oxygen, and eEF2K helps to protect them from hypoxia. eEF2K is cytoprotective during hypoxia and other conditions of nutrient insufficiency, it aids the survival of neuronal cells during hypoxia and has a key role in helping cells withstand nutrient deficiency
physiological function
transcription elongation is controlled by phosphorylation of eukaryotic elongation factor 2 (eEF2), which inhibits its activity and is catalyzed by eEF2 kinase (eEF2K), a calcium/calmodulin-dependent alpha-kinase. eEF2K activity is regulated through several signaling pathways linked, e.g., to nutrient availability. Hypoxia causes the activation of eEF2K and induces eEF2 phosphorylation. eEF2K is subject to hydroxylation on proline 98. Proline hydroxylation is catalyzed by proline hydroxylases, oxygen-dependent enzymes which are inactivated during hypoxia. Hypoxia-induced eEF2 phosphorylation requires eEF2K and is not catalyzed by AMPK, it does also not require signaling via AMPK or mTORC1. Pharmacological inhibition of proline hydroxylases, e.g. by DMOG treatment, also stimulates eEF2 phosphorylation. Pro98 lies in a universally conserved linker between the calmodulin-binding and catalytic domains of eEF2K. Its hydroxylation partially impairs the binding of calmodulin to eEF2K and markedly limits the calmodulin-stimulated activity of eEF2K. Neuronal cells depend on oxygen, and eEF2K helps to protect them from hypoxia. eEF2K is cytoprotective during hypoxia and other conditions of nutrient insufficiency, it aids the survival of neuronal cells during hypoxia and has a key role in helping cells withstand nutrient deficiency
physiological function
cardiac hypertrophy may be regulated at least partly via enzyme-eukaryotic elongation factor 2 signaling pathway
physiological function
cardiac hypertrophy may be regulated at least partly via enzyme-eukaryotic elongation factor 2 signaling pathway
physiological function
In many types of tumour cells, and likely in more advanced solid tumours, the enzyme helps protect cells against nutrient depletion and other stresses by slowing down protein synthesis (thereby conserving resources) and/or altering the translation rates of specific mRNAs and thus the levels of the corresponding proteins. The enzyme aids the growth of solid tumours in vivo and aids cell migration. The enzyme is required for the resistance of tumors to caloric restriction-induced cell death. The enzyme plays a role in protecting breast cancer cells against endoplasmic reticulum stress, apparently by activating autophagy
physiological function
-
the enzyme acts downstream of p38 MAPK to regulate proliferation, apoptosis and autophagy in human lung fibroblasts. The enzyme might inhibit transforming growth factor beta 1-induced NHLF proliferation and differentiation and activates normal lung fibroblast cell apoptosis and autophagy through p38 MAPK signaling, which might ameliorate lung fibroblast-to-myofibroblast differentiation
physiological function
-
the enzyme contributes to angiogenesis and tumor progression in hepatocellular carcinoma via transcription factors SP1/KLF5-mediated endothelial growth factor expression, as well as the subsequent stimulation of PI3K/Akt and STAT3 signalling
physiological function
the enzyme controls the translation of mRNAs encoding proteins involving in cell migration
physiological function
the enzyme is cytoprotective for cells faced with glucose starvation. The enzyme promotes cell survival by inhibiting protein synthesis without inducing autophagy. The enzyme makes a substantial contribution to the cytoprotective effect of mammalian target of rapamycin complex 1 inhibition
physiological function
the enzyme mediates the inhibition of cardiomyocyte death under glucose deprivation condition
physiological function
the enzyme plays a the regulatory role of in pyroptosis in doxorubicin-treated human melanoma cells. The enzyme dictates the cross-talk between pyroptosis and autophagy in doxorubicin-treated human melanoma cells
physiological function
the enzyme protects cancer cells against acidosis and impedes tumorigenesis
physiological function
-
eEF2K likely contributes to neuronal function by regulating the synthesis of microtubule-related proteins. Phosphorylation of elongation factor 2, EF2, results in slower elongation which then result in the increased synthesis of specific proteins. Expression levels of eEF2K targets with unaltered, enhanced, and reduced eEF2K enzyme activity, overview. Synthesis of MAP1B, ARC, and CAMKIIa is sensitive to eEF2K inhibition
-
physiological function
-
eukaryotic elongation factor 2 kinase (eEF2K) prevents binding of eEF to the ribosome via phosphorylation of eEF and thus prevents further translation. The enzyme regulates the development of hypertension through oxidative stress-dependent vascular inflammation. eEF2K protein increases in mesenteric artery from spontaneously hypertensive rats. Enzyme eEF2K mediates TNF-alpha-induced vascular inflammation via reactive oxygen species-dependent mechanism, which is at least partly responsible for the development of hypertension in spontaneously hypertensive rats
-
additional information
homology modelling of eEF2K using the structure of myosin heavy chain kinase, EC 2.7.11.7, PDB ID 3LMH. A glutamate might act as gatekeeper and makes likely hydrogen bonds to the adenine in the active site and is essential for activity in the alpha kinase family
additional information
solution structure of the Ca2+-CaM-eEF-2KCBD complex, structure analysis, NMR spectrometric analysis, detailed overview
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phosphoprotein
-
phosphoprotein
-
phosphorylation by p70-S6 kinase inhibits EF2K, Ca2+ decreases the phosphorylation of the enzyme
phosphoprotein
-
the eEF2 kinase is activated by phosphorylation through AMPK, phosphorylation sites of the eEF2 kinase are Ser366, Ser398, and Ser78, the phosphorylation of the latter is regulated by insulin in an mTOR protein-dependent manner, Ser78 is no target for the kinase S6K1
phosphoprotein
-
the enzyme performs autophosphorylation, stimulation of AMP-activated protein kinase, EC 2.7.11.11, by AMP leads to activation of the wild-type and mutant enzyme and to its phosphorylation at Ser398 in the regulatory domain, other phosphorylation sites of the enzyme are Ser78, Ser359, Ser377, and Ser366, the latter is phosphorylated by kinases S6K1 and p90RSK inhibiting the enzyme
phosphoprotein
the calcium/calmodulin-dependent kinase, that phosphorylates and inactivates eukaryotic elongation factor 2, is subject to multisite phosphorylation, which regulates its activity, overview
phosphoprotein
-
phosphorylated GCN2 is the active form of the enzyme
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
phosphoprotein
-
phosphorylation sites: Ser61, Ser66, Ser78, Ser366, Ser445, Ser474, Ser491, Thr348, Thr353. The autophosphorylation sites Thr348, Thr353, Ser366 and Ser445 are are highly conserved among vertebrate elongation factor 2 kinases. None of the sites lies in the catalytic domain. Ser366 is phosphorylated not only autocatalytically but also in trans by other kinases. Thr348 appears to be constitutively autophosphorylated in vitro. Thr348, and presumably its autophosphorylation, are critical for the ability of the enzyme to phosphorylate substrates in trans
phosphoprotein
upon incubation with Ca2+ and calmodulin, the enzyme undergoes rapid autophosphorylation. Identification of five major autophosphorylation sites: Thr348, Thr353, Ser445, Ser474, and Ser500. Phosphorylation of Thr348 is required for substrate phosphorylation, but not selfphosphorylation
phosphoprotein
AMPK activates eEF2K via phosphorylation. Inhibition of proline hydroxylases, e.g. by DMOG, induces the phosphorylation of eEF2 independently of altered mTORC1 or AMPK signaling
phosphoprotein
autophosphorylation site is Thr348 in eEF2K
phosphoprotein
-
eEF2K activity is also regulated by phosphorylation. Ser366 is phosphorylated by S6 kinases, enzymes which are phosphorylated and activated by mTORC1, phosphorylation at this site desensitizes eEF2K to activation by Ca2+/CaM. Phosphorylation of Ser359, a site whose modification strongly inhibits eEF2K, and Ser78, immediately next to the CaM-binding motif, are also promoted by mTORC1. The latter strongly impairs the interaction of eEF2K with CaM thereby impairing its activation. For eEF2K stimulation, cAMP, a catabolic signal which inhibits protein synthesis, stimulates cAMP-dependent protein kinase, PKA, which phosphorylates eEF2K at Ser500. Degradation of eEF2K requires the autophosphorylation site at Ser445, which forms part of a typical bTrCP-binding motif or phosphodegron. eEF2K is also phosphorylated at several sites in response to activation of stress-stimulated MAP kinase cascades, either directly by MAPKs or by their downstream effectors. Phosphorylation of eEF2 at Thr56 impairs its binding to the ribosome. The enzyme is regulated by its phosphorylation status, overview
phosphoprotein
the enzyme performs autophosphorylation at Thr57
phosphoprotein
the enzyme autophosphorylates at Thr-348. Phosphorylation of Ser-500 integrates with Ca2+ and calmodulin to regulate the enzyme activity. Phosphorylation of Thr-348 and Ser-500 regulates the Ca2+/calmodulin-dependent activity of the enzyme
phosphoprotein
the enzyme autophosphorylates on Thr348. The enzyme is extensively regulated by phosphorylation. S6 kinase phosphorylates the enzyme on Ser366 and impairs its activation by Ca2+/calmodulin. Mammalian target of rapamycin complex 1 directly phosphorylates the enzyme on Ser78/Ser396 thereby negatively regulating the enzyme activity
phosphoprotein
the enzyme undergoes autophosphorylation, with a major site being Thr348. The phosphorylation of Thr348 enhances the enzyme activity by increasing its affinity for a (peptide) substrate and its intrinsic catalytic activity. The 70 kDa ribosomal protein S6 kinase phosphorylates the enzyme at Ser366, inactivating it. Ser78 of the enzyme is also phosphorylated in an mTORC1-dependent manner. This phosphorylation impairs calmodulin binding, and thus, the activation of the enzyme. The Ras/Raf/MEK/ERK pathway also makes direct inputs into the inactivation of the enzyme via direct phosphorylation of the enzyme by ERK (at Ser359). Enzyme phosphorylation increases during hypoxia
phosphoprotein
-
inactivating Ser366 phosphorylation of eEF2 kinase
phosphoprotein
-
phosphorylation by p70-S6 kinase inhibits EF2K, Ca2+ decreases the phosphorylation of the enzyme
phosphoprotein
-
phosphorylation of eEF2K can either inhibit or enhance the activity of its downstream substrate, depending on the site of phosphorylation and the type of stimul, lopinavir increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview
phosphoprotein
AMPK activates eEF2K via phosphorylation. Inhibition of proline hydroxylases, e.g. by DMOG, induces the phosphorylation of eEF2 independently of altered mTORC1 or AMPK signaling
phosphoprotein
the enzyme is phosphorylated by diverse kinases with stimulating or suppressing effect, the enzyme is regulated by its phosphorylation status, overview
phosphoprotein
phosphorylation sites at Ser366 and Thr56
phosphoprotein
-
phosphorylation at Ser366 inhibits the enzyme, mediated by cholecystokinin
phosphoprotein
-
the enzyme performs autophosphorylation, stimulation of AMP-activated protein kinase, EC 2.7.11.11, by AMP leads to activation of the enzyme and to its phosphorylation at Ser398 in the regulatory domain, other phosphorylation sites of the enzyme are Ser78, Ser359, Ser377, and Ser366
phosphoprotein
phosphorylation sites at Ser366 and Thr56
side-chain modification
eEF2K is subject to hydroxylation on proline 98 catalyzed by proline hydroxylases. Hydroxylation of Pro98 impairs binding of eEF2K to calmodulin and its activation by calmodulin
side-chain modification
eEF2K is subject to hydroxylation on proline 98 catalyzed by proline hydroxylases
additional information
-
the enzyme is ubiquitinated in vivo, ubiquitination and turnover is increased by inhibition of heat shock protein 90, enzyme degradation involves the proteasome
additional information
-
the enzyme is ubiquitinated in vivo, ubiquitination and turnover is increased by inhibition of heat shock protein 90, enzyme degradation involves the proteasome
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S454A
neurons injected with mutant enzyme S454A shows significantly more phosphorylation of elongation factor 2 than do neurons injected with wild-type enzyme
C314A
-
complete loss of activity
C318A
-
complete loss of activity
D274A
-
loss of ability to bind ATP
D284A
catalytically inactive
D97A
site-directed mutagenesis
E717A
the mutation in the C-terminal fragment of the enzyme reduces elongation factor 2 phosphorylation activity
H213A
-
complete loss of activity
H260A
-
complete loss of activity
K170M
-
complete loss of activity, loss of ability to bind ATP
K170R
-
complete loss of activity, loss of ability to bind ATP
P98A
site-directed mutagenesis
S366A
-
activity with RKKFGESEKTKTKEFL is decreased approximately 90% compared to wild-type activity after preincubation for 60 min with MgATP2-
S445A
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
S445D
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
S474A
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
S474D
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
S500A
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
S78A/S366A
-
phosphorylation-defective mutant, mutation results in an increased stability under normal culture conditions, t1/2 is above 24 h
T348E
-
the mutant enzyme phosphorylates purified elongation factor 2 poorly compared with wild-type
T353A
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
T353D
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate
T482A
catalytically inactive mutant
W85S
site-directed mutagenesis, Mutation of residue W85 to S85 substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells
W99A
site-directed mutagenesis
W99L
site-directed mutagenesis
Y712A
the mutation in the C-terminal fragment of the enzyme reduces elongation factor 2 phosphorylation activity
Y712A/Y713A
the mutations in the C-terminal fragment of the enzyme abolish elongation factor 2 phosphorylation activity
Y713A
the mutation in the C-terminal fragment of the enzyme reduces elongation factor 2 phosphorylation activity
D97A
site-directed mutagenesis
P96A
site-directed mutagenesis
W99A
site-directed mutagenesis
W99L
site-directed mutagenesis
S398A
-
site-directed mutagenesis, mutation of a phosphorylation site, no phosphorylation by AMPK, altered regulation by phosphorylation compared to the wild-type enzyme
S398A
-
phosphorylation-defective mutant, mutation results in an increased stability under normal culture conditions, t1/2 is above 24 h
S500D
no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate. The mutation renders the enzyme Ca2+-independent
S500D
the mutation enhances the rate of activation (Thr-348 autophosphorylation) by 6fold and lowers the EC50 for Ca2+/calmpdulin binding to activated enzyme (Thr-348 phosphorylated) by 20fold as compared to the wild type
S78A
-
site-directed mutagenesis, mutation of a phosphorylation site, altered regulation by phosphorylation compared to the wild-type enzyme, but the mutation does not influence AMPK
S78A
-
activity with RKKFGESEKTKTKEFL is decreased approximately 50% compared to wild-type activity after preincubation for 60 min with MgATP2-
T348A
about 95% loss of the kinase activity
T348A
-
activity with RKKFGESEKTKTKEFL is decreased approximately 90% compared to wild-type activity after preincubation for 60 min with MgATP2-. The mutant enzyme phosphorylates purified elongation factor 2 poorly compared with wild-type
T348D
about 93% loss of the kinase activity
T348D
-
the mutant enzyme phosphorylates purified elongation factor 2 poorly compared with wild-type
additional information
-
the eEF2 kinase level is higher in PDK1-lacking cells, constitutive phosphorylation at Ser78 of the eEF2 kinase occurs in TSC2-deficient cells
additional information
knockdown of eEF2K gene by small interfering RNA (siRNA)
additional information
-
GCN2-deficient mice fed a leucine-deprived diet, develop liver steatosis, genes related to triglyceride synthesis and expression of SREBP-1c and PPARg are not repressed. Beta-oxidation genes and fatty-acid transport genes are upregulated, mutant exhibits reduced lipid mobilization
additional information
-
construction of Gcn2 knockout mice and effects on enzyme activity and leucine metabolism, phenotype, overview
additional information
construction of gene eEF-2K deletion mutants, phenotype, overview
additional information
generation of eEF2K knockout mice and eEF2K knock-in mice, phenotype, overview
additional information
-
GCN2-deficient mice fed a leucine-deprived diet, develop liver steatosis, genes related to triglyceride synthesis and expression of SREBP-1c and PPARg are not repressed. Beta-oxidation genes and fatty-acid transport genes are upregulated, mutant exhibits reduced lipid mobilization
-
additional information
-
construction of Gcn2 knockout mice and effects on enzyme activity and leucine metabolism, phenotype, overview
-
additional information
generation of enzyme knoockout mice, silencing of the enzyme by siRNA expression
additional information
-
generation of enzyme knoockout mice, silencing of the enzyme by siRNA expression
-
additional information
-
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
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Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase
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Homo sapiens
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Homo sapiens
brenda
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Homo sapiens
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The GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of an essential amino acid
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5
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Homo sapiens
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Mus musculus
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841-855
2011
Aplysia californica (F8S834)
brenda
Gentz, S.H.; Bertollo, C.M.; Souza-Fagundes, E.M.; da Silva, A.M.
Implication of eIF2alpha kinase GCN2 in induction of apoptosis and endoplasmic reticulum stress-responsive genes by sodium salicylate
J. Pharm. Pharmacol.
65
430-440
2013
Mus musculus
brenda
Arriazu, E.; Ruiz de Galarreta, M.; Lopez-Zabalza, M.J.; Leung, T.M.; Nieto, N.; Iraburu, M.J.
GCN2 kinase is a key regulator of fibrogenesis and acute and chronic liver injury induced by carbon tetrachloride in mice
Lab. Invest.
93
303-310
2013
Homo sapiens, Mus musculus
brenda
Byrne, E.H.; Prosser, I.; Muttucumaru, N.; Curtis, T.Y.; Wingler, A.; Powers, S.; Halford, N.G.
Overexpression of GCN2-type protein kinase in wheat has profound effects on free amino acid concentration and gene expression
Plant Biotechnol. J.
10
328-340
2012
Triticum aestivum
brenda
Abramczyk, O.; Tavares, C.D.; Devkota, A.K.; Ryazanov, A.G.; Turk, B.E.; Riggs, A.F.; Ozpolat, B.; Dalby, K.N.
Purification and characterization of tagless recombinant human elongation factor 2 kinase (eEF-2K) expressed in Escherichia coli
Protein Expr. Purif.
79
237-244
2011
Homo sapiens (O00418), Homo sapiens
brenda
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)
brenda
Kenney, J.W.; Moore, C.E.; Wang, X.; Proud, C.G.
Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles
Adv. Biol. Regul.
55
15-27
2014
Homo sapiens, Mus musculus (O08796)
brenda
Usui, T.; Okada, M.; Hara, Y.; Yamawaki, H.
Eukaryotic elongation factor 2 kinase regulates the development of hypertension through oxidative stress-dependent vascular inflammation
Am. J. Physiol. Heart Circ. Physiol.
305
H756-H768
2013
Homo sapiens (O00418), Rattus norvegicus (P70531), Rattus norvegicus Wistar (P70531)
brenda
Wang, X.; Xie, J.; da Mota, S.R.; Moore, C.E.; Proud, C.G.
Regulated stability of eukaryotic elongation factor 2 kinase requires intrinsic but not ongoing activity
Biochem. J.
467
321-331
2015
Homo sapiens (O00418)
brenda
Lazarus, M.; Levin, R.; Shokat, K.
Discovery of new substrates of the elongation factor-2 kinase suggests a broader role in the cellular nutrient response
Cell. Signal.
29
78-83
2017
Homo sapiens (O00418)
brenda
Liao, Y.; Chu, H.P.; Hu, Z.; Merkin, J.J.; Chen, J.; Liu, Z.; Degenhardt, K.; White, E.; Ryazanov, A.G.
Paradoxical roles of elongation factor-2 kinase in stem cell survival
J. Biol. Chem.
291
19545-19557
2016
Mus musculus (O08796)
brenda
Kenney, J.W.; Genheden, M.; Moon, K.M.; Wang, X.; Foster, L.J.; Proud, C.G.
Eukaryotic elongation factor 2 kinase regulates thesynthesis of microtubule-related proteins in neurons
J. Neurochem.
136
276-284
2016
Mus musculus (O08796), Mus musculus, Mus musculus C57/BL6J (O08796)
brenda
Moore, C.E.; Mikolajek, H.; Regufe da Mota, S.; Wang, X.; Kenney, J.W.; Werner, J.M.; Proud, C.G.
Elongation factor 2 kinase is regulated by proline hydroxylation and protects cells during hypoxia
Mol. Cell. Biol.
35
1788-1804
2015
Homo sapiens (O00418), Mus musculus (O08796)
brenda
Cheng, Y.; Ren, X.; Yuan, Y.; Shan, Y.; Li, L.; Chen, X.; Zhang, L.; Takahashi, Y.; Yang, J.W.; Han, B.; Liao, J.; Li, Y.; Harvey, H.; Ryazanov, A.; Robertson, G.P.; Wan, G.; Liu, D.; Chen, A.F.; Tao, Y.; Yang, J.M.
eEF-2 kinase is a critical regulator of Warburg effect through controlling PP2A-A synthesis
Oncogene
2016
1-16
2016
Homo sapiens (O00418)
brenda
Lee, K.; Alphonse, S.; Piserchio, A.; Tavares, C.D.; Giles, D.H.; Wellmann, R.M.; Dalby, K.N.; Ghose, R.
Structural basis for the recognition of eukaryotic elongation factor 2 kinase by calmodulin
Structure
24
1441-1451
2016
Homo sapiens (O00418)
brenda
Xiao, T.; Liu, R.; Proud, C.G.; Wang, M.W.
A high-throughput screening assay for eukaryotic elongation factor 2 kinase inhibitors
Acta Pharm. Sin. B
6
557-563
2016
Homo sapiens
brenda
Liu, R.; Proud, C.G.
Eukaryotic elongation factor 2 kinase as a drug target in cancer, and in cardiovascular and neurodegenerative diseases
Acta Pharmacol. Sin.
37
285-294
2016
Homo sapiens (O00418), Homo sapiens
brenda
Yu, P.; Wang, H.Y.; Tian, M.; Li, A.X.; Chen, X.S.; Wang, X.L.; Zhang, Y.; Cheng, Y.
Eukaryotic elongation factor-2 kinase regulates the cross-talk between autophagy and pyroptosis in doxorubicin-treated human melanoma cells in vitro
Acta Pharmacol. Sin.
40
1237-1244
2019
Homo sapiens (O00418), Homo sapiens
brenda
Kameshima, S.; Okada, M.; Yamawaki, H.
Eukaryotic elongation factor 2 (eEF2) kinase/eEF2 plays protective roles against glucose deprivation-induced cell death in H9c2 cardiomyoblasts
Apoptosis
24
359-368
2019
Rattus norvegicus (P70531)
brenda
Kameshima, S.; Okada, M.; Ikeda, S.; Watanabe, Y.; Yamawaki, H.
Coordination of changes in expression and phosphorylation of eukaryotic elongation factor 2 (eEF2) and eEF2 kinase in hypertrophied cardiomyocytes
Biochem. Biophys. Rep.
7
218-224
2016
Mus musculus (O08796), Rattus norvegicus (P70531)
brenda
Will, N.; Piserchio, A.; Snyder, I.; Ferguson, S.B.; Giles, D.H.; Dalby, K.N.; Ghose, R.
Structure of the C-terminal helical repeat domain of eukaryotic elongation factor 2 kinase
Biochemistry
55
5377-5386
2016
Homo sapiens (O00418)
brenda
Wang, X.; Xie, J.; Proud, C.G.
Eukaryotic elongation factor 2 kinase (eEF2K) in cancer
Cancers (Basel)
9
162
2017
Homo sapiens (O00418)
brenda
Moore, C.E.; Wang, X.; Xie, J.; Pickford, J.; Barron, J.; Regufe da Mota, S.; Versele, M.; Proud, C.G.
Elongation factor 2 kinase promotes cell survival by inhibiting protein synthesis without inducing autophagy
Cell. Signal.
28
284-293
2016
Homo sapiens (O00418)
brenda
Pan, Z.; Chen, Y.; Liu, J.; Jiang, Q.; Yang, S.; Guo, L.; He, G.
Design, synthesis, and biological evaluation of polo-like kinase 1/eukaryotic elongation factor 2 kinase (PLK1/EEF2K) dual inhibitors for regulating breast cancer cells apoptosis and autophagy
Eur. J. Med. Chem.
144
517-528
2018
Homo sapiens (O00418)
brenda
Wang, Y.; Huang, G.; Wang, Z.; Qin, H.; Mo, B.; Wang, C.
Elongation factor-2 kinase acts downstream of p38 MAPK to regulate proliferation, apoptosis and autophagy in human lung fibroblasts
Exp. Cell Res.
363
291-298
2018
Homo sapiens
brenda
Xie, J.; Shen, K.; Lenchine, R.V.; Gethings, L.A.; Trim, P.J.; Snel, M.F.; Zhou, Y.; Kenney, J.W.; Kamei, M.; Kochetkova, M.; Wang, X.; Proud, C.G.
Eukaryotic elongation factor 2 kinase upregulates the expression of proteins implicated in cell migration and cancer cell metastasis
Int. J. Cancer
142
1865-1877
2018
Homo sapiens (O00418)
brenda
Zhou, Y.; Li, Y.; Xu, S.; Lu, J.; Zhu, Z.; Chen, S.; Tan, Y.; He, P.; Xu, J.; Proud, C.G.; Xie, J.; Shen, K.
Eukaryotic elongation factor 2 kinase promotes angiogenesis in hepatocellular carcinoma via PI3K/Akt and STAT3
Int. J. Cancer
146
1383-1395
2020
Homo sapiens
brenda
Tavares, C.D.; Giles, D.H.; Stancu, G.; Chitjian, C.A.; Ferguson, S.B.; Wellmann, R.M.; Kaoud, T.S.; Ghose, R.; Dalby, K.N.
Signal integration at elongation factor 2 kinase the roles of calcium, calmodulin, and Ser-500 phosphorylation
J. Biol. Chem.
292
2032-2045
2017
Homo sapiens (O00418)
brenda
Piserchio, A.; Will, N.; Giles, D.H.; Hajredini, F.; Dalby, K.N.; Ghose, R.
Solution structure of the carboxy-terminal tandem repeat domain of eukaryotic elongation factor 2 kinase and its role in substrate recognition
J. Mol. Biol.
431
2700-2717
2019
Homo sapiens (O00418)
brenda
Beretta, S.; Gritti, L.; Verpelli, C.; Sala, C.
Eukaryotic elongation factor 2 kinase a pharmacological target to regulate protein translation dysfunction in neurological diseases
Neuroscience
445
42-49
2020
Mus musculus (O08796)
brenda