MARS (gene)

Methionyl-tRNA synthetase
File:PBB Protein MARS image.jpg PDB rendering based on 2djv.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 2djv​
Identifiers
Symbols	MARS ; FLJ35667; METRS; MTRNS
External IDs	Template:OMIM5 Template:MGI HomoloGene: 3656
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE MARS 213671 s at tn.png
File:PBB GE MARS 201475 x at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Methionyl-tRNA synthetase, also known as MARS, is a human gene.

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene belongs to the class I family of tRNA synthetases.

Further reading

• Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". J. Biol. Chem. 266 (23): 15398–405. PMID 1651330.
• Ogata K, Kurahashi A, Kenmochi N, Terao K (1992). "Role of 5SrRNA as a positive effector of some aminoacyl-tRNA synthetases in macromolecular complexes, with specific reference to methionyl-tRNA synthetase". J. Biochem. 110 (6): 1037–44. PMID 1665486.CS1 maint: Multiple names: authors list (link)
• Cirullo RE, Wasmuth JJ (1984). "Assignment of the human MARS gene, encoding methioninyl-tRNA synthetase, to chromosome 12 using human X Chinese hamster cell hybrids". Somat. Cell Mol. Genet. 10 (3): 225–34. PMID 6585969.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
• Lage H, Dietel M (1996). "Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase". Gene. 178 (1–2): 187–9. PMID 8921912.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Quevillon S, Robinson JC, Berthonneau E; et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ubeda M, Schmitt-Ney M, Ferrer J, Habener JF (1999). "CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability". Biochem. Biophys. Res. Commun. 262 (1): 31–8. doi:10.1006/bbrc.1999.1140. PMID 10448063.CS1 maint: Multiple names: authors list (link)
• Ko YG, Kang YS, Kim EK; et al. (2000). "Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis". J. Cell Biol. 149 (3): 567–74. PMID 10791971.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kang J, Kim T, Ko YG; et al. (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kaminska M, Shalak V, Mirande M (2002). "The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function". Biochemistry. 40 (47): 14309–16. PMID 11714285.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ahn HC, Kim S, Lee BJ (2003). "Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43". FEBS Lett. 542 (1–3): 119–24. PMID 12729910.CS1 maint: Multiple names: authors list (link)
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)