Search results for EEF2

Showing 18 results out of 28

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Protein (6 results from a total of 13)

Identifier: R-HSA-6801504
Species: Homo sapiens
Compartment: secretory granule lumen
Primary external reference: UniProt: EEF2: P13639
Identifier: R-HSA-6801513
Species: Homo sapiens
Compartment: ficolin-1-rich granule lumen
Primary external reference: UniProt: EEF2: P13639
Identifier: R-HSA-6806499
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: P13639
Identifier: R-HSA-156901
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P13639
Identifier: R-HSA-5358478
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: EEF2: P13639
Identifier: R-HSA-8932237
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: EEF2: P13639

Reaction (6 results from a total of 9)

Identifier: R-HSA-156930
Species: Homo sapiens
Compartment: cytosol
At the beginning of this reaction, 1 molecule of 'eEF2', and 1 molecule of 'GTP' are present. At the end of this reaction, 1 molecule of 'eEF2:GTP' is present.

This reaction takes place in the 'cytosol' (Guillot et al. 2013).
Identifier: R-HSA-8932243
Species: Homo sapiens
Compartment: cytosol
Protein-lysine N-methyltransferase EEF2KMT (EEF2KMT) catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on Lys-525.
Identifier: R-HSA-5367022
Species: Homo sapiens
Compartment: cytosol
By analogy to the activity of its experimentally characterized budding yeast homolog (Lin et al. 2014; Schaffrath et al. 2014), cytosolic DPH7 is inferred to catalyze the removal of a methyl group of Me-diphthine EEF2, yielding diphthine EEF2.
Identifier: R-HSA-5358484
Species: Homo sapiens
Compartment: cytosol
Cytosolic diphthamide biosynthesis protein 5 (DPH5) transfers four methyl groups from S-adenosylmethionine (AdoMet) to elongation factor 2 (EEF2) whose histidine residue at position 715 has been conjugated with a 3-amino 3-carboxypropyl group, forming methylated diphthine EEF2 and S-adenosylhomocysteine (AdoHcy). DPH5 activity has been identified in cells of diverse eukaryotic species including humans and has been characterized in detail in budding yeast (Liu et al. 2004; Matteakis et al. 1992; Moehring & Moehring 1988).
Identifier: R-HSA-5358494
Species: Homo sapiens
Compartment: cytosol
The diphthamide biosynthesis protein 2 (DPH2) subunit of the cytosolic DPH1:DPH2:DPH3 complex catalyzes the transfer of a 3-amino-3-carboxypropyl group from S-adenosylmethionine (AdoMet) to residue 715 of nascent elongation factor 2 (EEF2), forming aminocarboxypropyl EEF2 and S-methylthioadenosine (MTAD). The association of DPH1, 2, and 3 to form a complex is inferred from studies of the homologous yeast proteins (Abdel-Fattah et al. 2013; Bar et al. 2008) and more limited studies of interactions among mouse and human ones (Liu et al. 2004). The identification of DPH2 as the catalytically active subunit of the DPH1:DPH2:DPH3 complex is inferred from the properties of the homologous Pyrococcus horikoshii protein (Zhang et al. 2010). DPH4 (DNAJC24) is needed for the reaction to occur but its exact role is unknown (Liu et al. 2004; Su et al. 2013). DPH3 is an electron donor for DPH1-DPH2 in the first step of diphthamide biosynthesis (Dong et al. 2014).
Identifier: R-HSA-5358475
Species: Homo sapiens
Compartment: cytosol
Cytosolic diphthamide biosynthesis protein 6 (DPH6) ligates an ammonium ion to diphthine-EEF2 to generate diphthamide-EEF2 in a reaction coupled to the hydrolysis of ATP to yield AMP and PPi (Su et al. 2012; Uthman et al. 2013; Wei et al. 2013).

Complex (2 results from a total of 2)

Identifier: R-HSA-156916
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-156922
Species: Homo sapiens
Compartment: cytosol

Pathway (3 results from a total of 3)

Identifier: R-HSA-5358493
Species: Homo sapiens
Compartment: cytosol
Eukaryotic elongation factor 2 (EEF2) catalyzes the GTP dependent ribosomal translocation step during translation elongation. This function requires the presence of a posttranslational modification, the conversion of histidine residue 715 to diphthamide (2' [3 carboxamido 3 (trimethylammonio)propyl] L histidine) (Van Ness et al. 1978). No other protein is known to undergo this modification. The diphthamide residue is also the target of ADP ribosylation catalyzed by diphtheria toxin, which inactivates EEF2 and leads to cell death (Collier 1975; Pappenheim 1977).

Diphthamide synthesis proceeds in four steps: the transfer of 3 amino 3 carboxypropyl group from S adenosylmethionine to histidine 715 of EEF2, the addition of four methyl groups to the 3 amino 3 carboxypropyl moiety, the demethylation of the methylated carboxylate group to form diphthine, and the amidation of the diphthine carboxyl group (Liu et al. 2004; Lin et al. 2014; Schaffrath et al. 2014; Su et al. 2013; Uthman et al. 2013).

Identifier: R-HSA-156842
Species: Homo sapiens
Compartment: cytosol
The translation elongation cycle adds one amino acid at a time to a growing polypeptide according to the sequence of codons found in the mRNA. The next available codon on the mRNA is exposed in the aminoacyl-tRNA (aa-tRNA) binding site (A site) on the 30S subunit.
A: Ternary complexes of aa -tRNA:eEF1A:GTP enter the ribosome and enable the anticodon of the tRNA to make a codon/anticodon interaction with the A-site codon of the mRNA. B: Upon cognate recognition, the eEF1A:GTP is brought into the GTPase activating center of the ribosome, GTP is hydrolyzed and eEF1A:GDP leaves the ribosome. C: The peptidyl transferase center of ribosome catalyses the formation of a peptide bond between the incoming amino acid and the peptide found in the peptidyl-tRNA binding site (P site). D: In the pre-translocation state of the ribosome, the eEF2:GTP enters the ribosome, physically translocating the peptidyl-tRNA out of the A site to P site and leaves the ribosome eEF2:GDP. This action of eEF2:GTP accounts for the precise movement of the mRNA by 3 nucleotides.Consequently, deacylated tRNA is shifted to the E site. A ribosome associated ATPase activity is proposed to stimulate the release of deacylated tRNA from the E site subsequent to translocation (Elskaya et al., 1991). In this post-translocation state, the ribosome is now ready to receive a new ternary complex.
This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH, and a ribosome with A,P and E sites to accommodate these three forms of tRNA.
Identifier: R-HSA-5336415
Species: Homo sapiens
Diphtheria is a serious, often fatal human disease associated with damage to many tissues. Bacteria in infected individuals, however, are typically confined to the lining of the throat or to a skin lesion; systemic effects are due to the secretion of an exotoxin encoded by a lysogenic bacteriophage. The toxin is encoded as a single polypeptide but is cleaved by host furin-like proteases to yield an aminoterminal fragment A and a carboxyterminal fragment B, linked by a disulfide bond. Toxin cleavage can occur when it first contacts the target cell surface, as annotated here, or as late as the point at which fragment A is released into the cytosol. Fragment B mediates toxin uptake into target cell endocytic vesicles, where acidification promotes a conformational change enabling fragment B to form a channel in the vesicle membrane through which fragment A is extruded into the target cell cytosol. Cleavage of the inter-fragment disulfide bond frees DT fragment A, which catalyzes ADP ribosylation of the translation elongation factor 2 (EEF2) in a target cell, thereby blocking protein synthesis. Neither fragment is toxic to human cells by itself (Collier 1975; Pappenheim 1977; Murphy 2011).

Icon (1 results from a total of 1)

Species: Homo sapiens
Curator: Bruce May
Designer: Cristoffer Sevilla
eEF2 icon
Elongation factor 2
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