Version 5.4
Homo sapiens Gene: NARS
Summary
InnateDB Gene IDBG-3763.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol NARS
Gene Name asparaginyl-tRNA synthetase
Synonyms ASNRS; NARS1
Species Homo sapiens
Ensembl Gene ENSG00000134440
Encoded Proteins
IDBP-3765
asparaginyl-tRNA synthetase
IDBP-584710
asparaginyl-tRNA synthetase
IDBP-725967
IDBP-726803
IDBP-726214
IDBP-726665
IDBP-725705
IDBP-727908
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase is localized to the cytoplasm and belongs to the class II family of tRNA synthetases. The N-terminal domain represents the signature sequence for the eukaryotic asparaginyl-tRNA synthetases. [provided by RefSeq, Jul 2008]
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase is localized to the cytoplasm and belongs to the class II family of tRNA synthetases. The N-terminal domain represents the signature sequence for the eukaryotic asparaginyl-tRNA synthetases. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 18:57600656-57622213
Strand Reverse strand
Band q21.31
Transcripts
ENST00000256854 ENSP00000256854
ENST00000411676
ENST00000540592 ENSP00000442496
ENST00000588661 ENSP00000467421
ENST00000590123 ENSP00000466919
ENST00000589001
ENST00000589314
ENST00000586807 ENSP00000464988
ENST00000587366
ENST00000587675 ENSP00000466606
ENST00000591599 ENSP00000467651
ENST00000587194 ENSP00000464899
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 35 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 35 [view]
Protein-Protein 35 [view]
Protein-DNA 0
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:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0004816 asparagine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006421 asparaginyl-tRNA aminoacylation
GO:0006422 aspartyl-tRNA aminoacylation
GO:0010467 gene expression
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000024587
View Gene Order
ENSBTAG00000019271
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 K7EMQ6
UniProt Splice Variant
Entrez Gene 4677
UniGene Hs.465224 Hs.739975
RefSeq NM_004539 XM_005266700
HUGO HGNC:7643
OMIM 108410
CCDS CCDS32837
HPRD 00154
IMGT
EMBL AC100847
GenPept
RNA Seq Atlas 4677

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