QARS

Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene.[3][4][5]

QARS1
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesQARS1, GLNRS, MSCCA, PRO2195, glutaminyl-tRNA synthetase, glutaminyl-tRNA synthetase 1, QARS
External IDsOMIM: 603727 HomoloGene: 3704 GeneCards: QARS1
Gene location (Human)
Chr.Chromosome 3 (human)[1]
Band3p21.31Start49,095,932 bp[1]
End49,105,130 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5859

n/a

Ensembl

ENSG00000172053

n/a

UniProt

P47897

n/a

RefSeq (mRNA)

NM_001272073
NM_005051

n/a

RefSeq (protein)

NP_001259002
NP_005042

n/a

Location (UCSC)Chr 3: 49.1 – 49.11 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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.[5] 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.[6]

Interactions

QARS has been shown to interact with RARS.[7]

References

  1. GRCh38: Ensembl release 89: ENSG00000172053 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M (Aug 1994). "Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer". Proceedings of the National Academy of Sciences of the United States of America. 91 (18): 8670–4. Bibcode:1994PNAS...91.8670L. doi:10.1073/pnas.91.18.8670. PMC 44668. PMID 8078941.
  4. Durkin ME, Jäger AC, Khurana TS, Nielsen FC, Albrechtsen R, Wewer UM (July 1999). "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)". Cytogenetics and Cell Genetics. 84 (3–4): 173–8. doi:10.1159/000015249. PMID 10393422. S2CID 36315977.
  5. "Entrez Gene: QARS glutaminyl-tRNA synthetase".
  6. Hadd A, Perona JJ (Oct 2014). "Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases". Journal of Molecular Biology. 426 (21): 3619–33. doi:10.1016/j.jmb.2014.08.006. PMID 25149203.
  7. 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.

Further reading

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