Enzymes
| UniProtKB help_outline | 1 proteins |
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Namehelp_outline
N-terminal glycyl-L-lysyl-L-glutamyl-[protein]
Identifier
RHEA-COMP:15140
Reactive part
help_outline
- Name help_outline N-terminal glycyl-L-lysyl-L-glutamate residue Identifier CHEBI:142597 Charge 1 Formula C13H24N4O5 SMILEShelp_outline [NH3+]CC(=O)N[C@H](C(=O)N[C@H](C(*)=O)CCC(=O)[O-])CCCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N-terminal N,N,N-trimethyl-glycyl-L-lysyl-L-glutamyl-[protein]
Identifier
RHEA-COMP:15143
Reactive part
help_outline
- Name help_outline N-terminal N,N,N-trimethyl-glycyl-L-lysyl-L-glutamate residue Identifier CHEBI:142600 Charge 1 Formula C16H30N4O5 SMILEShelp_outline [N+](CC(=O)N[C@H](C(=O)N[C@H](C(*)=O)CCC(=O)[O-])CCCC[NH3+])(C)(C)C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 768 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58440 | RHEA:58441 | RHEA:58442 | RHEA:58443 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates.
Jakobsson M.E., Malecki J.M., Halabelian L., Nilges B.S., Pinto R., Kudithipudi S., Munk S., Davydova E., Zuhairi F.R., Arrowsmith C.H., Jeltsch A., Leidel S.A., Olsen J.V., Falnes P.O.
Eukaryotic elongation factor 1 alpha (eEF1A) delivers aminoacyl-tRNA to the ribosome and thereby plays a key role in protein synthesis. Human eEF1A is subject to extensive post-translational methylation, but several of the responsible enzymes remain unknown. Using a wide range of experimental appr ... >> More
Eukaryotic elongation factor 1 alpha (eEF1A) delivers aminoacyl-tRNA to the ribosome and thereby plays a key role in protein synthesis. Human eEF1A is subject to extensive post-translational methylation, but several of the responsible enzymes remain unknown. Using a wide range of experimental approaches, we here show that human methyltransferase (MTase)-like protein 13 (METTL13) contains two distinct MTase domains targeting the N terminus and Lys55 of eEF1A, respectively. Our biochemical and structural analyses provide detailed mechanistic insights into recognition of the eEF1A N terminus by METTL13. Moreover, through ribosome profiling, we demonstrate that loss of METTL13 function alters translation dynamics and results in changed translation rates of specific codons. In summary, we here unravel the function of a human MTase, showing that it methylates eEF1A and modulates mRNA translation in a codon-specific manner. << Less
Nat. Commun. 9:3411-3411(2018) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
Comments
Multi-step reaction: RHEA:58444 + RHEA:58448 + RHEA:58452.