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]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000134440 - Ensembl, May 2017
^ abcGRCm38: 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. PMC147268. PMID 9421509.
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.
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. PMC147956. 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. PMC139241. 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. PMC442147. 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. PMC528928. 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.
This article on a gene on human chromosome 18 is a stub. You can help Wikipedia by expanding it.
nars, gene, asparaginyl, trna, synthetase, cytoplasmic, enzyme, that, humans, encoded, nars, gene, nars1available, structurespdbortholog, search, pdbe, rcsblist, codes4zyaidentifiersaliasesnars1, nars, nedmilg, nedmileg, asnrs, asparaginyl, trna, synthetase, a. Asparaginyl tRNA synthetase cytoplasmic is an enzyme that in humans is encoded by the NARS gene 5 6 7 NARS1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes4ZYAIdentifiersAliasesNARS1 NARS NEDMILG NEDMILEG ASNRS asparaginyl tRNA synthetase 1 asparaginyl tRNA synthetaseExternal IDsOMIM 108410 MGI 1917473 HomoloGene 68404 GeneCards NARS1Gene location Human Chr Chromosome 18 human 1 Band18q21 31Start57 600 656 bp 1 End57 622 213 bp 1 Gene location Mouse Chr Chromosome 18 mouse 2 Band18 18 E1Start64 632 718 bp 2 End64 649 723 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inendothelial cellpancreatic ductal cellBrodmann area 23middle temporal gyruskidney tubuleparotid glandRegion I of hippocampus properrenal medullagerminal epitheliumbronchial epithelial cellTop expressed infacial motor nucleusPaneth cellmotor neuronlacrimal glandcalvariaseminal vesiculaanterior horn of spinal cordparotid glandmedial vestibular nucleuscrypt of lieberkuhn of small intestineMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionaminoacyl tRNA ligase activity nucleotide binding ligase activity asparagine tRNA ligase activity ATP binding nucleic acid bindingCellular componentextracellular exosome mitochondrion cytoplasm cytosolBiological processprotein biosynthesis asparaginyl tRNA aminoacylation tRNA aminoacylation for protein translationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez467770223EnsemblENSG00000134440ENSMUSG00000024587UniProtO43776Q8BP47RefSeq mRNA NM 004539NM 001142950NM 027350NM 001377021NM 001377022NM 001377023RefSeq protein NP 004530NP 001136422NP 081626Location UCSC Chr 18 57 6 57 62 MbChr 18 64 63 64 65 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseAminoacyl 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 edit 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 editMaruyama 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 nbsp This article on a gene on human chromosome 18 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title NARS gene amp oldid 1142674648, wikipedia, wiki, book, books, library,
