TARS (gene)

Threonyl-tRNA synthetase
PDB rendering based on 1wwt.
Available structures PDB 1wwt
Identifiers
Symbols	TARS; MGC9344; ThrRS
External IDs	OMIM: 187790 MGI: 106314 HomoloGene: 11852 GeneCards: TARS Gene
EC number	6.1.1.3
Gene Ontology Molecular function • nucleotide binding • threonine-tRNA ligase activity • threonine-tRNA ligase activity • protein binding • ATP binding • ligase activity • protein homodimerization activity Cellular component • cytoplasm • cytosol Biological process • translation • tRNA aminoacylation for protein translation • threonyl-tRNA aminoacylation • gene expression Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6897	110960
Ensembl	ENSG00000113407	ENSMUSG00000022241
UniProt	P26639	Q3U630
RefSeq (mRNA)	NM_152295	NM_033074.3
RefSeq (protein)	NP_689508	NP_149065.2
Location (UCSC)	Chr 5: 33.44 – 33.47 Mb	Chr 15: 11.31 – 11.33 Mb
PubMed search	[1]	[2]

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

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

See also

• Aminoacyl 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. PMC 362973. PMID 2747635. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=362973. 
• 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. 
• 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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. 
• 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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.