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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UGM6: Variant p.Trp13Gly

Tryptophan--tRNA ligase, mitochondrial
Gene: WARS2
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Variant information Variant position: help 13 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 Tryptophan (W) to Glycine (G) at position 13 (W13G, p.Trp13Gly). 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 large size and aromatic (W) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 NEMMLAS and PKDYS3; hypomorphic variant, clinically relevant when present in trans with an amorphic variant; impaired mitochondrial localization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 13 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 360 The length of the canonical sequence.
Location on the sequence: help MALHSMRKARER W SFIRALHKGSAAAPALQKDS 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                         MALHSMRKARERWSFIRALHKGSAAAPALQKDS

Mouse                         MALFSVRKARECWRFIRALHKGPAATLAPQKES

Bovine                        MALRSMRKARECWNFIRALHQGPDAAPVPQKDA

Caenorhabditis elegans        -MIFSGKFTSHLLNY----GFKPNNLRLLSTST

Slime mold                    MKIDEVNFKDK---------------------T

Baker's yeast                 MSNKQAVLKLISKRWISTVQRADFKLNSEALHS

Fission yeast                 MAKLPKITSLL---------------------P
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
Transit peptide 1 – 18 Mitochondrion



Literature citations
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Burke E.A.; Frucht S.J.; Thompson K.; Wolfe L.A.; Yokoyama T.; Bertoni M.; Huang Y.; Sincan M.; Adams D.R.; Taylor R.W.; Gahl W.A.; Toro C.; Malicdan M.C.V.;
Clin. Genet. 93:712-718(2018)
Cited for: VARIANTS PKDYS3 GLY-13 AND TRP-228; INVOLVEMENT IN PKDYS3; Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated in the aetiology of autosomal recessive intellectual disability.
Musante L.; Puettmann L.; Kahrizi K.; Garshasbi M.; Hu H.; Stehr H.; Lipkowitz B.; Otto S.; Jensen L.R.; Tzschach A.; Jamali P.; Wienker T.; Najmabadi H.; Ropers H.H.; Kuss A.W.;
Hum. Mutat. 38:621-636(2017)
Cited for: VARIANT NEMMLAS GLY-13; CHARACTERIZATION OF VARIANT NEMMLAS GLY-13; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; INVOLVEMENT IN NEMMLAS; Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Huebers A.; Huppertz H.J.; Wortmann S.B.; Kassubek J.;
Mov. Disord. Clin. Pract. 7:88-90(2020)
Cited for: VARIANTS PKDYS3 GLY-13 AND ASP-50; INVOLVEMENT IN PKDYS3; WARS2 mutations cause dopa-responsive early-onset parkinsonism and progressive myoclonus ataxia.
Skorvanek M.; Rektorova I.; Mandemakers W.; Wagner M.; Steinfeld R.; Orec L.; Han V.; Pavelekova P.; Lackova A.; Kulcsarova K.; Ostrozovicova M.; Gdovinova Z.; Plecko B.; Brunet T.; Berutti R.; Kuipers D.J.S.; Boumeester V.; Havrankova P.; Tijssen M.A.J.; Kaiyrzhanov R.; Rizig M.; Houlden H.; Winkelmann J.; Bonifati V.; Zech M.; Jech R.;
Parkinsonism Relat. Disord. 94:54-61(2022)
Cited for: VARIANTS PKDYS3 GLY-13; ASP-50; LEU-100 DEL AND 208-GLU--LEU-360 DEL;
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.