TARS (gene)

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) Band 5p13.3 Start 33,440,696 bp End 33,468,091 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 A1|15 5.6 cM Start 11,382,387 bp End 11,399,751 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve islet of Langerhans gums oral cavity right lobe of liver body of pancreas rectum Achilles tendon anterior pituitary stromal cell of endometrium Top expressed in primitive streak seminal vesicula calvaria hair follicle left lobe of liver lacrimal gland ureter somite maxillary prominence crypt of lieberkuhn of small intestine More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding ligase activity 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 Chr 15: 11.38 – 11.4 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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. doi:10.1016/S0021-9258(18)92906-6. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. 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.