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, NARS, NEDMILG, NEDMILEG, ASNRS, asparaginyl-tRNA synthetase 1, asparaginyl-tRNA synthetase
External IDs	OMIM: 108410; MGI: 1917473; HomoloGene: 68404; GeneCards: NARS1; OMA:NARS1 - orthologs
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 64,632,718 bp[2] End 64,649,723 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell pancreatic ductal cell Brodmann area 23 lateral nuclear group of thalamus middle temporal gyrus kidney tubule gingival epithelium mucosa of sigmoid colon parotid gland Epithelium of choroid plexus Top expressed in facial motor nucleus Paneth cell motor neuron lacrimal gland gastrula calvaria seminal vesicula anterior horn of spinal cord parotid gland decidua More reference expression data BioGPS 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: 64.63 – 64.65 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. S2CID 42353500.
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. S2CID 4427026.
• 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. S2CID 13709685.