Search by BoMiProt ID - Bomi4055


Primary Information

BoMiProt ID Bomi4055
Protein Name Aspartate--tRNA ligase, mitochondrial/Aspartyl-tRNA synthetase/AspRS
Organism Bos taurus
Uniprot IdA6QPU5
Milk FractionWhey
Ref Sequence Id NP_001095692.1
Aminoacid Length 651
Molecular Weight 73688
Fasta Sequence https://www.uniprot.org/uniprot/A6QPU5.fasta
Gene Name DARS2
Gene Id 538772
Protein Existence Status reviewed

Secondary Information

Protein Function Recognition of Asp for protein synthesis.
Biochemical Properties Binds to Asp and ATP.DARS2 contains conserved residues involved in ATP binding, tRNA binding, and aspartic acid recognition, as well as catalytic site motifs characteristic of amino acid tRNA synthetases. arg263-to-ter (R263X) mutation in the DARS2 gene that was found in compound heterozygous state in a patient with leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation
PTMs Acetylation, Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A6QPU5|SYDM_BOVIN Aspartate--tRNA ligase, mitochondrial OS=Bos taurus OX=9913 GN=DARS2 PE=2 SV=1 MFCWLSRLCGELSTPTRRTTQLIWSSAARSMVLSSQRIPELSSFVARTNTCGELRSSHLG QEVTLCGWIQFRRQNIFLVLRDFHGLVQVVIPQDESAASVKKILCEAPMESVVQVSGTVI SRPPGQKNPKMPTGEIEIKVKTAKLLNSCKKLPFEIKDFMKKTETLRLQYRYLDLRSVQM QYNLRLRSQMVMKMREYLCNLHGFVDVETPTLFKRT*216PGGAKEFVIPSREPGKFYSLPQS*239P QQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGVQSLIEGLLQY SWPSDKDPLVVPFPSMPFAEALASYGTDKPDTRFGMKIVDISDMFRNTEVGFLQDALSKP QGTVKAICIRKGAKYLKRKDIESIRKFAADHFNEEVLPIFLKTNENWNSPVAKFIMEEQG LGLVKLLETQEEDVVLLTAGEHKKACSLMGKLRLECADLLEARGVVLRDPALFSFLWVVD FPLFLPKEENPQELESAHHPFTAPHPSDIHLLYTEPHKVRSQHYDLVLNGNEIGGGSIRI HNSELQHCVLDTVLKEDVKLLSHLLQALDYGAPPHGGIALGLDRLMCLVTGAPSIRDVIA FPKSFRGHDLMSNAPDSIPPEELKPYHIQVSWPMDAETEKSSSNHPCRSES
Predicted Disorder Regions 634-651
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography Bonnefond L, Fender A, Rudinger-Thirion J, Giegé 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. doi: 10.1021/bi047527z. PMID: 15779907.