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Identification
HMDB Protein ID HMDBP00608
Secondary Accession Numbers
  • 5880
Name Aspartate--tRNA ligase, cytoplasmic
Synonyms
  1. AspRS
  2. Aspartate--tRNA ligase
  3. Cell proliferation-inducing gene 40 protein
  4. Aspartyl-tRNA synthetase
Gene Name DARS
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Pathways
  • Aminoacyl-tRNA biosynthesis
  • Aspartate Metabolism
  • Canavan Disease
  • Hypoacetylaspartia
Reactions
Adenosine triphosphate + L-Aspartic acid + tRNA(Asp) → Adenosine monophosphate + Pyrophosphate + L-aspartyl-tRNA(Asp) details
tRNA(Asp) + L-Aspartic acid + Adenosine triphosphate → L-Aspartyl-tRNA(Asp) + Pyrophosphate + Adenosine monophosphate details
GO Classification
Biological Process
aspartyl-tRNA aminoacylation
protein complex assembly
Cellular Component
cytosol
Component
cell part
intracellular part
cytoplasm
Function
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
ligase activity
aspartate-trna ligase activity
nucleic acid binding
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
nucleic acid binding
ATP binding
aspartate-tRNA ligase activity
aminoacylase activity
Process
rna metabolic process
ncrna metabolic process
trna metabolic process
trna aminoacylation
trna aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
aspartyl-trna aminoacylation
biosynthetic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 2
Locus 2q21.3
SNPs DARS
Gene Sequence
>1506 bp
ATGCCCAGCGCCAGCGCCAGCCGCAAGAGTCAGGAGAAGCCGCGGGAGATCATGGACGCG
GCGGAAGATTATGCTAAAGAGAGATATGGAATATCTTCAATGATACAATCACACGAAAAA
CCAGATCGAGTTTTGGTTCGGGTTAGAGACTTGACAATACAAAAAGCTGATGAAGTTGTT
TGGGTACGTGCAAGAGTTCATACAAGCAGAGCTAAAGGGAAACAGTGCTTCTTAGTCCTA
CGTCAGCAGCAGTTTAATGTCCAGGCTCTTGTGGCGGTGGGAGACCATGCAAGCAAGCAG
ATGGTTAAATTTGCTGCCAACATCAACAAAGAGAGCATTGTGGATGTAGAAGGTGTTGTG
AGAAAAGTGAATCAGAAAATTGGAAGCTGTACACAGCAAGACGTTGAGTTACATGTTCAG
AAGATTTATGTGATCAGTTTGGCTGAACCCCGTCTGCCCCTGCAGCTGGATGATGCTGTT
CGGCCTGAGGCAGAAGGAGAAGAGGAAGGAAGAGCTACTGTTAACCAGGATACAAGATTA
GACAACAGAGTCATTGATCTTAGGACATCAACTAGTCAGGCAGTCTTCCGTCTCCAGTCT
GGCATCTGCCATCTCTTCCGAGAAACTTTAATTAACAAAGGTTTTGTGGAAATCCAAACT
CCTAAAATTATTTCAGCTGCCAGTGAAGGAGGAGCCAATGTTTTTACTGTGTCATATTTT
AAAAATAATGCATACCTGGCTCAGTCCCCACAGCTATATAAGCAAATGTGCATTTGTGCT
GATTTTGAGAAGGTTTTCTCTATTGGACCAGTATTCAGAGCGGAAGACTCTAATACCCAT
AGACATCTAACTGAGTTTGTTGGTTTGGACATTGAAATGGCTTTTAATTACCATTACCAC
GAAGTTATGGAAGAAATTGCTGACACCATGGTACAAATATTCAAAGGACTTCAAGAAAGG
TTTCAGACTGAAATTCAAACAGTGAATAAACAGTTCCCATGTGAGCCATTCAAATTTTTG
GAGCCAACTCTAAGACTAGAATATTGTGAAGCATTGGCTATGCTTAGGGAAGCTGGAGTC
GAAATGGGAGATGAAGACGATCTGAGCACACCAAATGAAAAGCTGTTGGGTCATTTGGTA
AAGGAAAAGTATGATACAGATTTTTATATTCTTGATAAATATCCATTGGCTGTAAGACCT
TTCTATACCATGCCTGACCCAAGAAATCCCAAACAGTCCAACTCTTACGATATGTTCATG
AGAGGAGAAGAAATATTGTCAGGAGCTCAAAGAATACATGATCCTCAACTGCTAACAGAG
AGAGCTTTACATCATGGAATTGATTTGGAGAAAATTAAGGCTTACATTGATTCCTTCCGC
TTTGGAGCCCCTCCTCATGCTGGTGGAGGCATTGGATTGGAACGAGTTACTATGCTGTTT
CTGGGATTGCATAATGTTCGTCAGACCTCCATGTTCCCTCGTGATCCCAAACGACTCACT
CCTTAA
Protein Properties
Number of Residues 501
Molecular Weight 57135.8
Theoretical pI 6.546
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Aspartyl-tRNA synthetase, cytoplasmic
MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVV
WVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVV
RKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRL
DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYF
KNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYH
EVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGV
EMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFM
RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLF
LGLHNVRQTSMFPRDPKRLTP
GenBank ID Protein 62896511
UniProtKB/Swiss-Prot ID P14868
UniProtKB/Swiss-Prot Entry Name SYDC_HUMAN
PDB IDs Not Available
GenBank Gene ID AK222476
GeneCard ID DARS
GenAtlas ID DARS
HGNC ID HGNC:2678
References
General References
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  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Jacobo-Molina A, Peterson R, Yang DC: cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J Biol Chem. 1989 Oct 5;264(28):16608-12. [PubMed:2674137 ]
  7. Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed:18029264 ]