Threonine–tRNA ligase 1, cytoplasmic

TARS1
Identifiers
Aliases	TARS1, ThrRS, threonyl-tRNA synthetase, TARS, threonyl-tRNA synthetase 1, TTD7
External IDs	OMIM: 187790; MGI: 106314; GeneCards: TARS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1WWT, 4HWT, 4P3N, 4TTV
Enzyme activity
Gene location (Human)
Chr.	Chromosome 5 (human)
End	33,468,091 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	11,399,751 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; islet of Langerhans; ; mucosa of transverse colon; ; gums; ; gingival epithelium; ; ventricular zone; ; buccal mucosa cell; ; epithelium of colon; ; oral cavity; ; cartilage tissue;
	Top expressed in
	primitive streak; ; epiblast; ; endothelial cell of lymphatic vessel; ; seminal vesicula; ; calvaria; ; hair follicle; ; left lobe of liver; ; genital tubercle; ; tail of embryo; ; lacrimal gland;
	More reference expression data
	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
Databases	NCBI: entry; OMA: entry
	6897
	110960
	ENSG00000113407
	ENSMUSG00000022241
	P26639
	Q9D0R2
	NM_001258437; NM_001258438; NM_152295
	NM_033074
	NP_001245366; NP_001245367; NP_689508
	NP_149065
	Wikidata
View/Edit Human	View/Edit Mouse

Threonine–tRNA ligase 1, cytoplasmic, also called threonyl-tRNA synthetase 1, is an enzyme that in humans is encoded by the TARS1 gene. Like its relatives, TARS2 and TARS3, this enzyme functions as a threonine–tRNA ligase, which means it attaches the animo acid threonine to its corresponding transfer RNA as part of RNA-to-protein translation.

Function

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.

Comparison with TARS3

Cytoplasmic threonine–tRNA ligase is unique in vertebrate aminoacyl-tRNA synthetases in having a second form, TARS3 (previously called TARSL2), evolved from a gene duplication. In mice, the TARS1 enzyme is significantly more prevalent (55x in lungs, and 3x in muscles). Structurally, TARS1 functions as a homodimer, while TARS3 may instead be a component of the protein complex: multisynthetase complex (MSC). TARS1 is also smaller, 83 kD vs. 93 kD, and this has been used to infer that it is the primary target of the antibodies involved in antisynthetase syndrome.

Medical significance

Pathogenic (homozygous and compound heterozygous) mutations in TARS1 are associated with trichothiodystrophy (a type of hair fragility disorder), with the type caused by TARS1 mutation designated as: nonphotosensitive trichothiodystrophy-7 (TTD7).

References

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

1 2 3 GRCh38: Ensembl release 89: ENSG00000113407 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022241 – 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.
1 2 3 "Entrez Gene: TARS threonyl-tRNA synthetase".
↑ EC 3.1.1.3
↑ Gomez MA, Ibba M (2020-04-17). "Aminoacyl-tRNA synthetases". RNA. 26 (8): 910–936. doi:10.1261/rna.071720.119. PMC 7373986. PMID 32303649.
↑ Zeng QY, Zhang F, Zhang JH, Hei Z, Li ZH, Huang MH, Fang P, Wang ED, Sun XJ, Zhou XL (2023-05-01). "Loss of threonyl-tRNA synthetase-like protein Tarsl2 has little impact on protein synthesis but affects mouse development". Journal of Biological Chemistry. 299 (5) 104704. doi:10.1016/j.jbc.2023.104704. PMC 10200997. PMID 37059185.
1 2 3 Kanaji S, Chen W, Morodomi Y, Shapiro R, Kanaji T, Yang XL (2023-03-01). "Mechanistic perspectives on anti-aminoacyl-tRNA synthetase syndrome". Trends in Biochemical Sciences. 48 (3): 288–302. doi:10.1016/j.tibs.2022.09.011. PMC 9974581. PMID 36280495.
↑ "Threonine--tRNA ligase 1, cytoplasmic". UniProt consortium. Retrieved 2026-10-01.
↑ "TRICHOTHIODYSTROPHY 7, NONPHOTOSENSITIVE; TTD7". Online Mendelian Inheritance in Man. Johns Hopkins University. Retrieved 2026-09-27.

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. Bibcode:2004NaGen..36...40O. 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. {{cite journal}}: Cite uses deprecated parameter |citeseerx= (help)
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) MSB4100134: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000113407 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022241 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 3 "Entrez Gene: TARS threonyl-tRNA synthetase".

[6] EC 3.1.1.3

[7] Gomez MA, Ibba M (2020-04-17). "Aminoacyl-tRNA synthetases". RNA. 26 (8): 910–936. doi:10.1261/rna.071720.119. PMC 7373986. PMID 32303649.

[8] Zeng QY, Zhang F, Zhang JH, Hei Z, Li ZH, Huang MH, Fang P, Wang ED, Sun XJ, Zhou XL (2023-05-01). "Loss of threonyl-tRNA synthetase-like protein Tarsl2 has little impact on protein synthesis but affects mouse development". Journal of Biological Chemistry. 299 (5) 104704. doi:10.1016/j.jbc.2023.104704. PMC 10200997. PMID 37059185.

[Kanaji2023-9] 1 2 3 Kanaji S, Chen W, Morodomi Y, Shapiro R, Kanaji T, Yang XL (2023-03-01). "Mechanistic perspectives on anti-aminoacyl-tRNA synthetase syndrome". Trends in Biochemical Sciences. 48 (3): 288–302. doi:10.1016/j.tibs.2022.09.011. PMC 9974581. PMID 36280495.

[uniprot-10] "Threonine--tRNA ligase 1, cytoplasmic". UniProt consortium. Retrieved 2026-10-01.

[omim-11] "TRICHOTHIODYSTROPHY 7, NONPHOTOSENSITIVE; TTD7". Online Mendelian Inheritance in Man. Johns Hopkins University. Retrieved 2026-09-27.

Threonine–tRNA ligase 1, cytoplasmic

Function

Comparison with TARS3

Medical significance

References

Further reading