QARS

QARS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4R3Z, 4YE9, 4YE6, 4YE8
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
Gene location (Human)
Chr.	Chromosome 3 (human)
End	49,105,130 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	108,393,140 bp
RNA expression pattern
	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
	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
	5859
	97541
	ENSG00000172053
	ENSMUSG00000032604
	P47897
	Q8BML9
	NM_001272073 ; NM_005051
	NM_001168270 ; NM_133794
	NP_001259002 ; NP_005042
	NP_598555
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 01, 2024

Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene.^[5]^[6]^[7]

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.^[7] 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.^[8]

Interactions

QARS has been shown to interact with RARS.^[9]

Related Research Articles

An aminoacyl-tRNA synthetase, also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. It does so by catalyzing the transesterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. In humans, the 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code.

Apoptosis signal-regulating kinase 1 (ASK1) also known as mitogen-activated protein kinase 5 (MAP3K5) is a member of MAP kinase family and as such a part of mitogen-activated protein kinase pathway. It activates c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinases in a Raf-independent fashion in response to an array of stresses such as oxidative stress, endoplasmic reticulum stress and calcium influx. ASK1 has been found to be involved in cancer, diabetes, rheumatoid arthritis, cardiovascular and neurodegenerative diseases.

Elongation factor 1-delta is a protein that in humans is encoded by the EEF1D gene.

Glutamine-tRNA ligase or glutaminyl-tRNA synthetase (GlnRS) is an aminoacyl-tRNA synthetase, also called tRNA-ligase. is an enzyme that attaches glutamine amino acid onto its cognate tRNA.

Elongation factor 1-alpha 1 (eEF1a1) is a translation elongation protein, expressed across eukaryotes. In humans, it is encoded by the EEF1A1 gene.

Tryptophanyl-tRNA synthetase, cytoplasmic is an aminoacyl-tRNA synthetase enzyme that attaches the amino acid tryptophan to its cognate tRNA. In humans, it is encoded by the WARS gene.

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 is a protein that in humans is encoded by the AIMP1 gene.

Lysyl-tRNA synthetase is an enzyme that in humans is encoded by the KARS gene.

ARF GTPase-activating protein GIT2 is an enzyme that in humans is encoded by the GIT2 gene.

Tyrosyl-tRNA synthetase, cytoplasmic, also known as Tyrosine-tRNA ligase, is an enzyme that in humans is encoded by the YARS gene.

TERF1-interacting nuclear factor 2 is a protein that in humans is encoded by the TINF2 gene. TINF2 is a component of the shelterin protein complex found at the end of telomeres.

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.

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

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

<span class="mw-page-title-main">Multisynthetase complex auxiliary component p38</span> Protein-coding gene in the species Homo sapiens

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 2 is an enzyme that in humans is encoded by the AIMP2 gene.

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

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

Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS1 gene.

Tryptophanyl-tRNA synthetase, mitochondrial is an enzyme that in humans is encoded by the WARS2 gene.

In molecular biology, YqeY is a type of protein domain of unknown function. It is thought to have a role in protein synthesis, facilitating the production of charged transfer RNA used in the process of translating mRNA into protein. It is present as a domain of glutaminyl-tRNA synthetase (GlnRS) in almost all eukaryotes.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000172053 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032604 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: QARS glutaminyl-tRNA synthetase".
↑ 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.
↑ 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.

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000172053 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032604 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8078941-5] 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.

[pmid10393422-6] 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.

[entrez-7] 1 2 "Entrez Gene: QARS glutaminyl-tRNA synthetase".

[hadd-8] 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.

[pmid10801842-9] 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.

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QARS

Contents

Function

Interactions

Related Research Articles

References

Further reading