DARS (gene)

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

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; OMA:DARS1 - orthologs
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 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 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
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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