MARS (gene)

Methionyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the MARS gene.

MARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DJV, 4BL7, 4BVX, 4BVY
Identifiers
Aliases	MARS1, METRS, MRS, MTRNS, SPG70, CMT2U, ILFS2, ILLD, methionyl-tRNA synthetase, methionyl-tRNA synthetase 1, MARS, TTD9
External IDs	OMIM: 156560; MGI: 1345633; HomoloGene: 90878; GeneCards: MARS1; OMA:MARS1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q13.3 Start 57,475,445 bp End 57,517,569 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 D3 Start 127,132,090 bp End 127,147,655 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum anterior pituitary right frontal lobe tendon of biceps brachii granulocyte epithelium of colon left lobe of thyroid gland right lobe of thyroid gland upper lobe of left lung body of pancreas Top expressed in lacrimal gland fossa primitive streak epiblast tail of embryo condyle seminal vesicula calvaria muscle of thigh abdominal wall More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity tRNA binding nucleotide binding ligase activity ATP binding RNA binding methionine-tRNA ligase activity Cellular component extracellular exosome membrane nucleolus cytoplasm aminoacyl-tRNA synthetase multienzyme complex cytosol nucleus Biological process protein biosynthesis tRNA aminoacylation for protein translation cellular response to starvation rRNA transcription cellular response to insulin stimulus cellular response to platelet-derived growth factor stimulus cellular response to epidermal growth factor stimulus positive regulation of transcription of nucleolar large rRNA by RNA polymerase I methionyl-tRNA aminoacylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4141 216443 Ensembl ENSG00000166986 ENSMUSG00000040354 UniProt P56192 Q68FL6 RefSeq (mRNA) NM_004990 NM_001003913 NM_001171582 RefSeq (protein) NP_004981 NP_001003913 NP_001165053 Location (UCSC) Chr 12: 57.48 – 57.52 Mb Chr 10: 127.13 – 127.15 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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. doi:10.1016/S0021-9258(18)98629-1. 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. doi:10.1093/oxfordjournals.jbchem.a123674. PMID 1665486.
• 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. doi:10.1007/BF01535245. PMID 6585969. S2CID 44887504.
• 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/0378-1119(96)00313-7. 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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.
• 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. doi:10.1083/jcb.149.3.567. PMC 2174846. PMID 10791971.
• 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.
• 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. doi:10.1021/bi015670b. PMID 11714285.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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. doi:10.1016/S0014-5793(03)00362-4. PMID 12729910. S2CID 39222196.
• 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.
• 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. PMC 528928. PMID 15489334.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.