NARS (gene)

Asparaginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the NARS gene.[5][6][7]

NARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4ZYA
Identifiers
Aliases	NARS1, ASNRS, asparaginyl-tRNA synthetase, asparaginyl-tRNA synthetase 1, NARS
External IDs	OMIM: 108410 MGI: 1917473 HomoloGene: 68404 GeneCards: NARS1
Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18q21.31 Start 57,600,656 bp[1] End 57,622,213 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 E1 Start 64,499,647 bp[2] End 64,516,652 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • aminoacyl-tRNA ligase activity • nucleotide binding • ligase activity • asparagine-tRNA ligase activity • ATP binding • nucleic acid binding Cellular component • extracellular exosome • mitochondrion • cytoplasm • cytosol Biological process • protein biosynthesis • asparaginyl-tRNA aminoacylation • tRNA aminoacylation for protein translation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4677	70223
Ensembl	ENSG00000134440	ENSMUSG00000024587
UniProt	O43776	Q8BP47
RefSeq (mRNA)	NM_004539	NM_001142950 NM_027350 NM_001377021 NM_001377022 NM_001377023
RefSeq (protein)	NP_004530	NP_001136422 NP_081626
Location (UCSC)	Chr 18: 57.6 – 57.62 Mb	Chr 18: 64.5 – 64.52 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase is localized to the cytoplasm and belongs to the class II family of tRNA synthetases. The N-terminal domain represents the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000134440 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024587 - 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.
5. Cirullo RE, Arredondo-Vega FX, Smith M, Wasmuth JJ (May 1983). "Isolation and characterization of interspecific heat-resistant hybrids between a temperature-sensitive chinese hamster cell asparaginyl-tRNA synthetase mutant and normal human leukocytes: assignment of human asnS gene to chromosome 18". Somatic Cell Genet. 9 (2): 215–33. doi:10.1007/BF01543178. PMID 6836455.
6. Beaulande M, Tarbouriech N, Hartlein M (Feb 1998). "Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen". Nucleic Acids Res. 26 (2): 521–4. doi:10.1093/nar/26.2.521. PMC 147268. PMID 9421509.
7. "Entrez Gene: NARS asparaginyl-tRNA synthetase".

Further reading

• Maruyama K, Sugano S (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.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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.
• Shiba K, Motegi H, Yoshida M, Noda T (1999). "Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family". Nucleic Acids Res. 26 (22): 5045–51. doi:10.1093/nar/26.22.5045. PMC 147956. PMID 9801298.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (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.
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.