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Identification
HMDB Protein ID HMDBP09252
Secondary Accession Numbers
  • 15079
Name Aspartate--tRNA ligase, mitochondrial
Synonyms
  1. AspRS
  2. Aspartate--tRNA ligase
  3. Aspartyl-tRNA synthetase
Gene Name DARS2
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Not Available
Pathways
  • Aminoacyl-tRNA biosynthesis
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
mitochondrial asparaginyl-tRNA aminoacylation
Cellular Component
mitochondrial matrix
nucleus
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
ATP binding
aspartate-tRNA ligase activity
aspartate-tRNA(Asn) ligase activity
tRNA binding
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. Mitochondrion matrix
Gene Properties
Chromosome Location 1
Locus 1q25.1
SNPs DARS2
Gene Sequence
>1938 bp
ATGTACTTCCCTTCTTGGTTAAGTCAGCTGTACAGGGGTTTATCCAGACCCATCAGAAGG
ACCACCCAACCGATCTGGGGTTCTCTCTACAGAAGTCTGTTGCAGAGTTCACAGAGGAGA
ATTCCAGAATTCAGTAGCTTTGTTGTCCGGACCAACACATGTGGAGAGTTGCGTTCGTCT
CACTTAGGCCAAGAAGTCACCTTGTGTGGATGGATTCAGTACCGAAGGCAAAACACATTC
TTGGTCCTAAGAGATTTCGATGGGCTTGTTCAAGTTATCATTCCCCAGGATGAGTCGGCA
GCCTCTGTGAAGAAGATTTTATGTGAAGCCCCTGTGGAATCTGTGGTGCAAGTGTCTGGT
ACAGTCATTTCCCGTCCTGCAGGACAAGAGAATCCAAAAATGCCAACAGGTGAGATTGAA
ATCAAAGTTAAAACAGCTGAGCTTCTGAATGCCTGCAAGAAGCTGCCCTTTGAAATTAAG
AACTTCGTGAAGAAAACAGAGGCTCTTCGGTTGCAGTATCGCTACTTAGACTTGCGTAGT
TTCCAAATGCAGTATAACCTGCGACTGAGGTCCCAGATGGTCATGAAAATGCGGGAATAT
CTCTGTAATCTGCATGGGTTTGTGGATATAGAAACCCCCACATTGTTTAAGAGGACCCCA
GGGGGTGCCAAAGAGTTTTTAGTACCATCCAGGGAACCTGGAAAGTTTTATTCTCTCCCT
CAGAGTCCTCAACAGTTTAAGCAACTTCTGATGGTTGGCGGTTTAGACAGATATTTTCAG
GTTGCCCGATGTTATCGAGATGAAGGTTCAAGACCAGACAGACAGCCTGAGTTTACTCAG
ATTGACATAGAGATGTCATTTGTAGACCAGACTGGGATCCAGAGTTTAATTGAGGGTTTG
CTCCAGTATTCCTGGCCCAATGACAAAGATCCTGTGGTTGTTCCTTTTCCTACTATGACT
TTTGCTGAGGTGCTGGCCACCTATGGAACTGATAAACCTGACACTCGCTTTGGAATGAAG
ATTATAGATATCAGTGATGTGTTTAGAAACACAGAGATTGGATTTCTTCAAGATGCACTT
AGTAAGCCCCATGGAACTGTGAAAGCCATATGTATCCCTGAAGGAGCAAAATACTTAAAA
AGGAAAGACATTGAATCCATTAGAAACTTTGCAGCTGACCATTTTAATCAGGAAATCTTA
CCTGTATTCCTTAACGCCAATAGAAACTGGAATTCTCCAGTTGCTAATTTCATAATGGAG
TCACAAAGACTGGAATTAATCAGACTAATGGAGACCCAAGAGGAAGATGTGGTCCTACTA
ACTGCTGGAGAGCACAATAAAGCATGCTCTTTGTTAGGAAAATTACGACTGGAATGTGCT
GACCTTCTAGAAACAAGAGGAGTGGTGCTCCGTGACCCCACTCTGTTCTCTTTCCTTTGG
GTGGTAGATTTCCCACTCTTCCTGCCCAAGGAGGAAAATCCCAGAGAGCTGGAATCGGCC
CACCACCCATTTACTGCTCCCCACCCCAGTGACATACATCTCCTGTACACTGAGCCCAAA
AAGGCCCGTAGCCAACACTATGACTTGGTTTTAAATGGCAATGAAATAGGAGGTGGTTCA
ATTCGAATTCACAATGCAGAGCTGCAGCGTTATATCCTGGCAACCTTACTAAAGGAGGAT
GTGAAAATGCTCTCCCATCTGCTCCAGGCTTTAGATTATGGGGCACCCCCTCATGGAGGA
ATTGCCTTAGGGTTAGACAGACTGATATGCCTTGTCACTGGATCTCCAAGCATCAGAGAT
GTCATAGCCTTCCCAAAGTCCTTCCGGGGACATGACCTCATGAGCAATACCCCAGATTCT
GTCCCTCCTGAGGAACTGAAGCCCTATCATATCCGAGTCTCCAAGCCAACAGACTCCAAA
GCAGAAAGAGCTCATTGA
Protein Properties
Number of Residues 645
Molecular Weight 73562.02
Theoretical pI 8.011
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Aspartyl-tRNA synthetase, mitochondrial
MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSS
HLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSG
TVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRS
FQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLP
QSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGL
LQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDAL
SKPHGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIME
SQRLELIRLMETQEEDVVLLTAGEHNKACSLLGKLRLECADLLETRGVVLRDPTLFSFLW
VVDFPLFLPKEENPRELESAHHPFTAPHPSDIHLLYTEPKKARSQHYDLVLNGNEIGGGS
IRIHNAELQRYILATLLKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRD
VIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKPTDSKAERAH
GenBank ID Protein 34783643
UniProtKB/Swiss-Prot ID Q6PI48
UniProtKB/Swiss-Prot Entry Name SYDM_HUMAN
PDB IDs
GenBank Gene ID BC045173
GeneCard ID DARS2
GenAtlas ID DARS2
HGNC ID HGNC:25538
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. Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed:15779907 ]
  5. Scheper GC, van der Klok T, van Andel RJ, van Berkel CG, Sissler M, Smet J, Muravina TI, Serkov SV, Uziel G, Bugiani M, Schiffmann R, Krageloh-Mann I, Smeitink JA, Florentz C, Van Coster R, Pronk JC, van der Knaap MS: Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation. Nat Genet. 2007 Apr;39(4):534-9. Epub 2007 Mar 25. [PubMed:17384640 ]