TARS (gene)

Threonyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the TARS gene.[4]

TARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WWT, 4HWT, 4P3N, 4TTV
Identifiers
Aliases	TARS1, ThrRS, threonyl-tRNA synthetase, TARS, threonyl-tRNA synthetase 1, TTD7
External IDs	OMIM: 187790 MGI: 106314 HomoloGene: 11852 GeneCards: TARS1
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5p13.3 Start 33,440,696 bp[1] End 33,469,539 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • aminoacyl-tRNA ligase activity • nucleotide binding • ligase activity • GO:0001948 protein binding • ATP binding • protein homodimerization activity • threonine-tRNA ligase activity • tRNA binding • RNA binding Cellular component • extracellular exosome • actin cytoskeleton • cytoplasm • cytosol Biological process • tRNA aminoacylation • tRNA aminoacylation for protein translation • protein biosynthesis • threonyl-tRNA aminoacylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6897	110960
Ensembl	ENSG00000113407	ENSMUSG00000022241
UniProt	P26639	Q9D0R2
RefSeq (mRNA)	NM_001258437 NM_001258438 NM_152295	NM_033074
RefSeq (protein)	NP_001245366 NP_001245367 NP_689508	NP_149065
Location (UCSC)	Chr 5: 33.44 – 33.47 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

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. Threonyl-tRNA synthetase belongs to the class-II aminoacyl-tRNA synthetase family[4]

See also

• Aminoacyl tRNA synthetase

References

1. GRCh38: Ensembl release 89: ENSG00000113407 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Entrez Gene: TARS threonyl-tRNA synthetase".

Further reading

• Freist W, Gauss DH (1995). "Threonyl-tRNA synthetase". Biol. Chem. Hoppe-Seyler. 376 (4): 213–24. PMID 7626230.
• Cruzen ME, Arfin SM (1991). "Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes". J. Biol. Chem. 266 (15): 9919–23. PMID 2033077.
• Kontis KJ, Arfin SM (1989). "Isolation of a cDNA clone for human threonyl-tRNA synthetase: amplification of the structural gene in borrelidin-resistant cell lines". Mol. Cell. Biol. 9 (5): 1832–8. doi:10.1128/MCB.9.5.1832. PMC 362973. PMID 2747635.
• Gerken SC, Wasmuth JJ, Arfin SM (1986). "Threonyl-tRNA synthetase gene maps close to leucyl-tRNA synthetase gene on human chromosome 5". Somat. Cell Mol. Genet. 12 (5): 519–22. doi:10.1007/BF01539923. PMID 3464105. S2CID 32380159.
• Pan F, Lee HH, Pai SH, Lo KY (1982). "Purification and subunit structure studies of human placental threonyl-tRNA synthetase". Int. J. Pept. Protein Res. 19 (3): 300–9. doi:10.1111/j.1399-3011.1982.tb03042.x. PMID 7118399.
• Pan F, Lo KY, Pai SH, Lee HH (1982). "Kinetic mechanism of threonyl-tRNA synthetase from human placenta". Int. J. Pept. Protein Res. 20 (2): 159–66. doi:10.1111/j.1399-3011.1982.tb02670.x. PMID 7118437.
• Ogata K, Kurahashi A, Nishiyama C, Terao K (1994). "Presence of role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol". Biochim. Biophys. Acta. 1218 (3): 388–400. doi:10.1016/0167-4781(94)90192-9. PMID 8049265.
• 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.
• 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.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Vasilescu J, Zweitzig DR, Denis NJ, et al. (2007). "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells". J. Proteome Res. 6 (1): 298–305. CiteSeerX 10.1.1.401.4220. doi:10.1021/pr060438j. PMID 17203973.
• Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell. Proteomics. 6 (4): 575–88. doi:10.1074/mcp.M600249-MCP200. PMID 17220478.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.