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) [1] Band 5p13.3 Start 33,440,696 bp [1] End 33,468,091 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

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

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. 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. 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.