QARS

For the radio enthusiasts of Qatar, see Qatar Amateur Radio Society. For the village in Azerbaijan, see Qars.

QARS1
Identifiers
Aliases	QARS1, GLNRS, MSCCA, PRO2195, glutaminyl-tRNA synthetase, glutaminyl-tRNA synthetase 1, QARS
External IDs	OMIM: 603727; MGI: 1915851; HomoloGene: 3704; GeneCards: QARS1; OMA:QARS1 - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4R3Z, 4YE9, 4YE6, 4YE8
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 6.1.1.18 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.31 Start 49,095,932 bp End 49,105,130 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 F2 Start 108,384,905 bp End 108,393,140 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vulva skin of arm gonad mucosa of sigmoid colon tonsil gums skin of thigh gingival epithelium palpebral conjunctiva rectum Top expressed in seminal vesicula external carotid artery internal carotid artery hair follicle parotid gland primary oocyte lacrimal gland transitional epithelium of urinary bladder submandibular gland condyle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding ligase activity protein binding ATP binding protein kinase inhibitor activity protein kinase binding glutamine-tRNA ligase activity Cellular component cytoplasm mitochondrial matrix aminoacyl-tRNA synthetase multienzyme complex cytosol protein-containing complex Biological process brain development glutaminyl-tRNA aminoacylation tRNA aminoacylation protein biosynthesis tRNA aminoacylation for protein translation negative regulation of protein kinase activity negative regulation of stress-activated MAPK cascade negative regulation of transcription, DNA-templated negative regulation of apoptotic signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5859 97541 Ensembl ENSG00000172053 ENSMUSG00000032604 UniProt P47897 Q8BML9 RefSeq (mRNA) NM_001272073 NM_005051 NM_001168270 NM_133794 RefSeq (protein) NP_001259002 NP_005042 NP_598555 Location (UCSC) Chr 3: 49.1 – 49.11 Mb Chr 9: 108.38 – 108.39 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS1 gene (previously QARS).

Function

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. Almost all eukaryotic GlnRS enzymes possess a YqeY domain at the N-terminus, which affects affinity for the tRNA; in some bacterial species, such as Deinococcus radiodurans, YqeY is present as a C-terminal domain with similar function.

Interactions

QARS has been shown to interact with RARS.

Further reading

• Norcum MT (Aug 1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". The Journal of Biological Chemistry. 266 (23): 15398–405. doi:10.1016/S0021-9258(18)98629-1. PMID 1651330.
• Maruyama K, Sugano S (Jan 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.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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, Siatecka M, Mirande M (Jan 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
• Ko YG, Kang YS, Kim EK, Park SG, Kim S (May 2000). "Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis". The Journal of Cell Biology. 149 (3): 567–74. doi:10.1083/jcb.149.3.567. PMC 2174846. PMID 10791971.
• Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S (Jul 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". The Journal of Biological Chemistry. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. PMID 10801842.
• Kang J, Kim T, Ko YG, Rho SB, Park SG, Kim MJ, Kwon HJ, Kim S (Oct 2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". The Journal of Biological Chemistry. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
• Ko YG, Kim EY, Kim T, Park H, Park HS, Choi EJ, Kim S (Feb 2001). "Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1". The Journal of Biological Chemistry. 276 (8): 6030–6. doi:10.1074/jbc.M006189200. PMID 11096076.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (Jan 2004). "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". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (Jan 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.