NARS (gene)

NARS1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
4ZYA

Identifiers

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]
Band	18q21.31	End	57,622,213 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 18 (mouse)^[2]

Band	18\|18 E1	Start	64,632,718 bp^[2]
Band	18\|18 E1	End	64,649,723 bp^[2]

RNA expression pattern

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


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

Species

Human

Mouse


4677


70223


ENSG00000134440


ENSMUSG00000024587


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]

View/Edit Human

View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000134440 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024587 – 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.
^ 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.
^ 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.
^ ^a ^b "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.

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