QARS

Glutaminyl-tRNA synthetase, also known as QARS, is a human gene.cite web | title = Entrez Gene: QARS glutaminyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5859| accessdate = ]

PBB_Summary
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summary_text = Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.cite web | title = Entrez Gene: QARS glutaminyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5859| 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=Lamour V, Quevillon S, Diriong S, "et al." |title=Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 18 |pages= 8670–4 |year= 1994 |pmid= 8078941 |doi=
*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=
*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=
*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=Durkin ME, Jäger AC, Khurana TS, "et al." |title=Characterization of the human laminin beta2 chain locus (LAMB2): linkage to a gene containing a nonprocessed, transcribed LAMB2-like pseudogene (LAMB2L) and to the gene encoding glutaminyl tRNA synthetase (QARS). |journal=Cytogenet. Cell Genet. |volume=84 |issue= 3-4 |pages= 173–8 |year= 1999 |pmid= 10393422 |doi=
*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=
*cite journal | author=Kim T, Park SG, Kim JE, "et al." |title=Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21768–72 |year= 2000 |pmid= 10801842 |doi= 10.1074/jbc.M002404200
*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=Ko YG, Kim EY, Kim T, "et al." |title=Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 6030–6 |year= 2001 |pmid= 11096076 |doi= 10.1074/jbc.M006189200
*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=Lehner B, Semple JI, Brown SE, "et al." |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=
*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=Colland F, Jacq X, Trouplin V, "et al." |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104
*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=Rush J, Moritz A, Lee KA, "et al." |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209

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