DARS (gene)

DARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4J15
Identifiers
Aliases	DARS1 , HBSL, aspRS, aspartyl-tRNA synthetase, aspartyl-tRNA synthetase 1, DARS
External IDs	OMIM: 603084 MGI: 2442544 HomoloGene: 1032 GeneCards: DARS1
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2q21.3 Start 135,905,881 bp [1] End 135,986,100 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 E3 Start 128,291,444 bp [2] End 128,345,105 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte pericardium secondary oocyte parotid gland nipple vena cava seminal vesicula lactiferous duct inferior olivary nucleus embryo Top expressed in yolk sac spermatocyte spermatid myocardium of ventricle abdominal wall triceps brachii muscle skeletal muscle tissue soleus muscle maxillary prominence sternocleidomastoid muscle More reference expression data BioGPS 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 Species Human Mouse Entrez 1615 226414 Ensembl ENSG00000115866 ENSMUSG00000026356 UniProt P14868 Q922B2 RefSeq (mRNA) NM_001349 NM_001293312 NM_145507 NM_177445 RefSeq (protein) NP_001280241 NP_001340 NP_663482 NP_803228 Location (UCSC) Chr 2: 135.91 – 135.99 Mb Chr 1: 128.29 – 128.35 Mb PubMed search [3] [4]
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]

See also

• Aspartate-tRNA ligase

References

1. GRCh38: Ensembl release 89: ENSG00000115866 - Ensembl, May 2017
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.
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.
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.

Further reading

• 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.