Version 5.4
Homo sapiens Gene: DARS
Summary
InnateDB Gene IDBG-70984.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol DARS
Gene Name aspartyl-tRNA synthetase
Synonyms aspRS; HBSL
Species Homo sapiens
Ensembl Gene ENSG00000115866
Encoded Proteins
IDBP-70986
aspartyl-tRNA synthetase
IDBP-386196
aspartyl-tRNA synthetase
IDBP-386197
aspartyl-tRNA synthetase
IDBP-386198
aspartyl-tRNA synthetase
IDBP-386199
aspartyl-tRNA synthetase
IDBP-386200
aspartyl-tRNA synthetase
IDBP-590363
aspartyl-tRNA synthetase
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary 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. [provided by RefSeq, Jul 2008]
This gene encodes a member of a multienzyme complex that functions in mediating the attachment of amino acids to their cognate tRNAs. The encoded protein ligates L-aspartate to tRNA(Asp). Mutations in this gene have been found in patients showing hypomyelination with brainstem and spinal cord involvement and leg spasticity. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2014]
Gene Information
Type Protein coding
Genomic Location Chromosome 2:135906677-135986100
Strand Reverse strand
Band q21.3
Transcripts
ENST00000264161 ENSP00000264161
ENST00000422708 ENSP00000387508
ENST00000441323 ENSP00000389867
ENST00000456565 ENSP00000397616
ENST00000449218 ENSP00000388801
ENST00000435076 ENSP00000404445
ENST00000478212
ENST00000489964
ENST00000491481
ENST00000463008
ENST00000474184
ENST00000537273 ENSP00000444192
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 59 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 59 [view]
Protein-Protein 57 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004046 aminoacylase activity
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0044822 poly(A) RNA binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006422 aspartyl-tRNA aminoacylation
GO:0006461 protein complex assembly
GO:0010467 gene expression
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000026356
View Gene Order
ENSBTAG00000009949
Not yet available
Pathways
NETPATH
REACTOME
REACT_15306
Cytosolic tRNA aminoacylation pathway
REACT_15482
tRNA Aminoacylation pathway
REACT_71
Gene Expression pathway
KEGG
hsa00970
Aminoacyl-tRNA biosynthesis pathway
INOH
INOH website
Alanine Aspartate Asparagine metabolism pathway
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Hs.503787 Hs.602640
RefSeq NM_001349
HUGO
OMIM
CCDS CCDS2180
HPRD 04361
IMGT
EMBL
GenPept
RNA Seq Atlas

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca