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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q6PI48: Variant p.Gln184Lys

Aspartate--tRNA ligase, mitochondrial
Gene: DARS2
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Variant information Variant position: help 184 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Glutamine (Q) to Lysine (K) at position 184 (Q184K, p.Gln184Lys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and polar (Q) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help In LBSL; Significant impairment of its mitochondrial matrix localization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 184 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 645 The length of the canonical sequence.
Location on the sequence: help KKTEALRLQYRYLDLRSFQM Q YNLRLRSQMVMKMREYLCNL The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         KKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNL

Mouse                         KKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNL

Rat                           KKTEALRLQYRYLDLRSSQMQHNLRLRSQMVMKMREYLCTL

Bovine                        KKTETLRLQYRYLDLRSVQMQYNLRLRSQMVMKMREYLCNL

Slime mold                    AVSEELRLKYRYVDLRRDKVQSNIRLRSKVAMAARNYLIN-

Baker's yeast                 KLSAIYPPEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNN-

Fission yeast                 KPGMRIQLANRHIQLRAPKYNSYLRQRSRLAYQVHSFFND-

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 48 – 645 Aspartate--tRNA ligase, mitochondrial



Literature citations
Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation.
Scheper G.C.; van der Klok T.; van Andel R.J.; van Berkel C.G.M.; Sissler M.; Smet J.; Muravina T.I.; Serkov S.V.; Uziel G.; Bugiani M.; Schiffmann R.; Kraegeloh-Mann I.; Smeitink J.A.M.; Florentz C.; Van Coster R.; Pronk J.C.; van der Knaap M.S.;
Nat. Genet. 39:534-539(2007)
Cited for: VARIANTS LBSL GLY-45; PHE-152; HIS-179; LYS-184; LYS-248; GLN-263; VAL-560; PHE-613; VAL-626; GLN-626 AND CYS-629; Three human aminoacyl-tRNA synthetases have distinct sub-mitochondrial localizations that are unaffected by disease-associated mutations.
Gonzalez-Serrano L.E.; Karim L.; Pierre F.; Schwenzer H.; Roetig A.; Munnich A.; Sissler M.;
J. Biol. Chem. 293:13604-13615(2018)
Cited for: CHARACTERIZATION OF VARIANTS LBSL GLY-45; LYS-184; LYS-GLN-263; PHE-613; VAL-626 AND GLN-626; MUTAGENESIS OF ARG-58; THR-136 AND GLY-338; SUBCELLULAR LOCATION;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.