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DARS1
Identifiers
Aliases	DARS1, HBSL, aspRS, aspartyl-tRNA synthetase, aspartyl-tRNA synthetase 1, DARS
External IDs	OMIM: 603084; MGI: 2442544; GeneCards: DARS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4J15
Enzyme activity
Gene location (Human)
Chr.	Chromosome 2 (human)
End	135,986,100 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	128,345,105 bp
RNA expression pattern
	Top expressed in
	oocyte; ; pericardium; ; cartilage tissue; ; ventricular zone; ; secondary oocyte; ; parotid gland; ; beta cell; ; nipple; ; vena cava; ; seminal vesicula;
	Top expressed in
	yolk sac; ; spermatocyte; ; epiblast; ; ventricular zone; ; embryo; ; granulocyte; ; migratory enteric neural crest cell; ; spermatid; ; embryo; ; muscle of thigh;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	aspartate-tRNA ligase activity; aminoacyl-tRNA ligase activity; nucleotide binding; ligase activity; protein binding; ATP binding; aminoacylase activity; nucleic acid binding; RNA binding;
Cellular component	extracellular exosome; membrane; cytoplasm; aminoacyl-tRNA synthetase multienzyme complex; cytosol; synapse;
Biological process	tRNA aminoacylation for protein translation; protein biosynthesis; aspartyl-tRNA aminoacylation; protein-containing complex assembly;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	1615
	226414
	ENSG00000115866
	ENSMUSG00000026356
	P14868
	Q922B2
	NM_001349; NM_001293312
	NM_145507; NM_177445
	NP_001280241; NP_001340
	NP_663482; NP_803228
	Wikidata
View/Edit Human	View/Edit Mouse

Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene.^[5]^[6]

Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases. Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.^[6]

Clinical significance

Mutations in DARS have been identified as the cause of leukoencephalopathy, hypomyelination with brain stem and spinal cord involvement and leg spasticity (HBSL).^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000115866 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026356 – 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.
^ Jacobo-Molina A, Peterson R, Yang DC (Oct 1989). "cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase". J Biol Chem. 264 (28): 16608–12. doi:10.1016/S0021-9258(19)84749-X. PMID 2674137.
^ ^a ^b "Entrez Gene: DARS aspartyl-tRNA synthetase".
^ Taft RJ, Vanderver A, Leventer RJ, Damiani SA, Simons C, Grimmond SM, Miller D, Schmidt J, Lockhart PJ, Pope K, Ru K, Crawford J, Rosser T, de Coo IF, Juneja M, Verma IC, Prabhakar P, Blaser S, Raiman J, Pouwels PJ, Bevova MR, Abbink TE, van der Knaap MS, Wolf NI (2013). "Mutations in DARS cause hypomyelination with brain stem and spinal cord involvement and leg spasticity". American Journal of Human Genetics. 92 (5): 774–780. doi:10.1016/j.ajhg.2013.04.006. PMC 3644624. PMID 23643384.

Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". J. Biol. Chem. 266 (23): 15398–405. doi:10.1016/S0021-9258(18)98629-1. PMID 1651330.
Reed VS, Wastney ME, Yang DC (1995). "Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha". J. Biol. Chem. 269 (52): 32932–6. doi:10.1016/S0021-9258(20)30080-6. PMID 7806521.
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.
Escalante C, Yang DC (1993). "Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix". J. Biol. Chem. 268 (8): 6014–23. doi:10.1016/S0021-9258(18)53420-7. PMID 8449960.
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.
Quevillon S, Robinson JC, Berthonneau E, et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
Rho SB, Kim MJ, Lee JS, et al. (1999). "Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (8): 4488–93. Bibcode:1999PNAS...96.4488R. doi:10.1073/pnas.96.8.4488. PMC 16359. PMID 10200289.
Kang J, Kim T, Ko YG, et al. (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
Sang Lee J, Gyu Park S, Park H, et al. (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID 11829477.
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.
Cheong HK, Park JY, Kim EH, et al. (2004). "Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function". Int. J. Biochem. Cell Biol. 35 (11): 1548–57. doi:10.1016/S1357-2725(03)00070-0. PMID 12824064. S2CID 39165251.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
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.
Bonnefond L, Fender A, Rudinger-Thirion J, et al. (2005). "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 (12): 4805–16. doi:10.1021/bi047527z. PMID 15779907.
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.
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.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000115866 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026356 – 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.

[pmid2674137-5] Jacobo-Molina A, Peterson R, Yang DC (Oct 1989). "cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase". J Biol Chem. 264 (28): 16608–12. doi:10.1016/S0021-9258(19)84749-X. PMID 2674137.

[entrez-6] "Entrez Gene: DARS aspartyl-tRNA synthetase".

[7] Taft RJ, Vanderver A, Leventer RJ, Damiani SA, Simons C, Grimmond SM, Miller D, Schmidt J, Lockhart PJ, Pope K, Ru K, Crawford J, Rosser T, de Coo IF, Juneja M, Verma IC, Prabhakar P, Blaser S, Raiman J, Pouwels PJ, Bevova MR, Abbink TE, van der Knaap MS, Wolf NI (2013). "Mutations in DARS cause hypomyelination with brain stem and spinal cord involvement and leg spasticity". American Journal of Human Genetics. 92 (5): 774–780. doi:10.1016/j.ajhg.2013.04.006. PMC 3644624. PMID 23643384.

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DARS1

Clinical significance

See also

References

Further reading

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