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UniProtKB/Swiss-Prot Q8NI60: Variant p.Arg213Trp

Atypical kinase COQ8A, mitochondrial
Gene: COQ8A
Variant information

Variant position:  213
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Arginine (R) to Tryptophan (W) at position 213 (R213W, p.Arg213Trp).
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:  Change from large size and basic (R) to large size and aromatic (W)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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:  In COQ10D4.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  213
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  647
The length of the canonical sequence.

Location on the sequence:   HKQTLSEHARERKVPVTRIG  R LANFGGLAVGLGFGALAEVA
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         HKQTLSEHARERKVPVTRIGRLANFGGLAVGLGFGALAEVA

Mouse                         HKQMLSERARERKVPVTRIGRLANFGGLAVGLGIGALAEVA

Rat                           HKQMLSERARERKVPVTRIGRLANFGGLAVGLGFGALAEVA

Bovine                        HKQALSEHARERKVPVTRIGRLANFGGLAVGLGFGALAEVA

Zebrafish                     HKQMLSERARERKVPVTRLGRLANFGGLAVGLGIGALAEVA

Sequence annotation in neighborhood:  
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 163 – 647 Atypical kinase COQ8A, mitochondrial
Alternative sequence 1 – 484 Missing. In isoform 2.
Alternative sequence 1 – 279 Missing. In isoform 4.
Mutagenesis 214 – 214 L -> AILF. Strongly impairs homodimerization.
Mutagenesis 214 – 214 L -> IFGV. Slightly impaired homodimerization.
Mutagenesis 215 – 215 A -> ILG. Does not impair homodimerization.
Mutagenesis 216 – 216 N -> ALFM. Does not impair homodimerization.
Mutagenesis 217 – 217 F -> A. Slightly impaired homodimerization.
Mutagenesis 218 – 218 G -> ILF. Slightly impaired homodimerization.
Mutagenesis 219 – 219 G -> AF. Slightly impaired homodimerization.
Mutagenesis 219 – 219 G -> I. Strongly impairs homodimerization.
Mutagenesis 220 – 220 L -> G. Impaired homodimerization.
Mutagenesis 221 – 221 A -> L. Slightly impaired homodimerization.
Mutagenesis 222 – 222 V -> A. Slightly impaired homodimerization.
Mutagenesis 223 – 223 G -> AILF. Strongly impairs homodimerization.
Mutagenesis 224 – 224 L -> V. Impaired homodimerization.
Mutagenesis 225 – 225 G -> L. Slightly impaired homodimerization.
Mutagenesis 226 – 226 F -> A. Slightly impaired homodimerization.
Mutagenesis 227 – 227 G -> VFLI. Strongly impairs homodimerization.
Mutagenesis 228 – 228 A -> ILF. Does not impair homodimerization.
Mutagenesis 229 – 229 L -> A. Slightly impaired homodimerization.
Mutagenesis 230 – 230 A -> I. Slightly impaired homodimerization.


Literature citations

CABC1 gene mutations cause ubiquinone deficiency with cerebellar ataxia and seizures.
Mollet J.; Delahodde A.; Serre V.; Chretien D.; Schlemmer D.; Lombes A.; Boddaert N.; Desguerre I.; de Lonlay P.; de Baulny H.O.; Munnich A.; Roetig A.;
Am. J. Hum. Genet. 82:623-630(2008)
Cited for: VARIANTS COQ10D4 TRP-213; VAL-272; ASP-272 AND LYS-551;

Adult-onset cerebellar ataxia due to mutations in CABC1/ADCK3.
Horvath R.; Czermin B.; Gulati S.; Demuth S.; Houge G.; Pyle A.; Dineiger C.; Blakely E.L.; Hassani A.; Foley C.; Brodhun M.; Storm K.; Kirschner J.; Gorman G.S.; Lochmuller H.; Holinski-Feder E.; Taylor R.W.; Chinnery P.F.;
J. Neurol. Neurosurg. Psych. 83:174-178(2012)
Cited for: VARIANTS COQ10D4 TRP-213; CYS-271; ASP-272; VAL-272; TRP-299; THR-304; VAL-304; CYS-429; SER-549 AND LYS-551;

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.