MARS (gene)

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

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: MARS methionyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4141| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398–405 |year= 1991 |pmid= 1651330 |doi=
*cite journal | author=Ogata K, Kurahashi A, Kenmochi N, Terao K |title=Role of 5SrRNA as a positive effector of some aminoacyl-tRNA synthetases in macromolecular complexes, with specific reference to methionyl-tRNA synthetase. |journal=J. Biochem. |volume=110 |issue= 6 |pages= 1037–44 |year= 1992 |pmid= 1665486 |doi=
*cite journal | author=Cirullo RE, Wasmuth JJ |title=Assignment of the human MARS gene, encoding methioninyl-tRNA synthetase, to chromosome 12 using human X Chinese hamster cell hybrids. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 3 |pages= 225–34 |year= 1984 |pmid= 6585969 |doi=10.1007/BF01535245
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8
*cite journal | author=Lage H, Dietel M |title=Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. |journal=Gene |volume=178 |issue= 1-2 |pages= 187–9 |year= 1996 |pmid= 8921912 |doi=10.1016/0378-1119(96)00313-7
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3
*cite journal | author=Quevillon S, Robinson JC, Berthonneau E, "et al." |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183–95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316
*cite journal | author=Ubeda M, Schmitt-Ney M, Ferrer J, Habener JF |title=CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability. |journal=Biochem. Biophys. Res. Commun. |volume=262 |issue= 1 |pages= 31–8 |year= 1999 |pmid= 10448063 |doi= 10.1006/bbrc.1999.1140
*cite journal | author=Ko YG, Kang YS, Kim EK, "et al." |title=Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis. |journal=J. Cell Biol. |volume=149 |issue= 3 |pages= 567–74 |year= 2000 |pmid= 10791971 |doi=10.1083/jcb.149.3.567
*cite journal | author=Kang J, Kim T, Ko YG, "et al." |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682–8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199
*cite journal | author=Kaminska M, Shalak V, Mirande M |title=The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function. |journal=Biochemistry |volume=40 |issue= 47 |pages= 14309–16 |year= 2002 |pmid= 11714285 |doi=10.1021/bi015670b
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ahn HC, Kim S, Lee BJ |title=Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43. |journal=FEBS Lett. |volume=542 |issue= 1-3 |pages= 119–24 |year= 2003 |pmid= 12729910 |doi=10.1016/S0014-5793(03)00362-4
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Ewing RM, Chu P, Elisma F, "et al." |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes