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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y3A0: Variant p.Trp184Arg

Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
Gene: COQ4
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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 Tryptophan (W) to Arginine (R) at position 184 (W184R, p.Trp184Arg). 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 large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In SPAX10 and COQ10D7; likely pathogenic. 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 265 The length of the canonical sequence.
Location on the sequence: help DMLHTLLGMPTNILGEIVVK W FEAVQTGLPMCILGAFFGPI 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                         DMLHTLLGMPTNILGEIVVKWFEAVQTGLPMCILGAFFGPI

Mouse                         DMLHTLLGMPTNMLGEVVVKWFEAVQTGLPMCILGALFGPI

Rat                           DMLHTLLGMPTNMLGEVVVKWFEAVQTGLPMCILGALFGPV

Bovine                        DMLHALLGMPTNILGEIVVKWFEAVQTGLPMCVLSALFGPI

Xenopus laevis                DLMHTLLGMPTNMLGEVVVKWFEAVQTGLPMCILGAAFGPL

Xenopus tropicalis            DLMHTLLGMPTNMLGEVVVKWFEAVQTGLPMCILGAAFGPL

Zebrafish                     DLLHTLLGMPTNMLGEVAVKWFEAAQTGLPMCILGAALGPL

Caenorhabditis elegans        DFTHIALEQKTNMLGEVTVKYFEGIQYGLPMCVTGGIFGGA

Drosophila                    DLIHTVLDMPTNMLGEVAVKWVEALNTGLPMCYGGAVFGAV

Slime mold                    DFWHVLAGVRPDFQGEVAIKWFEFLQTGLPMNAIGSIIGPL

Baker's yeast                 DFYHAITNMPIIIEGEITIKALEGANLGVPMAILGGILAPL

Fission yeast                 DFYHAICNMPTNIEGELAIKWLEFVNMGLPVGALSALFGPL
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 31 – 265 Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
Binding site 164 – 164
Binding site 167 – 167
Binding site 179 – 179
Mutagenesis 164 – 164 D -> A. Abolished zinc-binding; when associated with A-179. Abolished zinc-binding and ability to promote formation of ubiquinone.



Literature citations
Primary coenzyme Q10 deficiency-7: expanded phenotypic spectrum and a founder mutation in southern Chinese.
Yu M.H.; Tsang M.H.; Lai S.; Ho M.S.; Tse D.M.L.; Willis B.; Kwong A.K.; Chou Y.Y.; Lin S.P.; Quinzii C.M.; Hwu W.L.; Chien Y.H.; Kuo P.L.; Chan V.C.; Tsoi C.; Chong S.C.; Rodenburg R.J.T.; Smeitink J.; Mak C.C.; Yeung K.S.; Fung J.L.; Lam W.; Hui J.; Lee N.C.; Fung C.W.; Chung B.H.;
NPJ Genom. Med. 4:18-18(2019)
Cited for: VARIANTS COQ10D7 SER-124; VAL-124 AND ARG-184;
Biallelic COQ4 Variants in Hereditary Spastic Paraplegia: Clinical and Molecular Characterization.
Lin X.; Jiang J.Y.; Hong D.J.; Lin K.J.; Li J.J.; Chen Y.J.; Qiu Y.S.; Wang Z.; Liao Y.C.; Yang K.; Shi Y.; Wang M.W.; Hsu S.L.; Hong S.; Zeng Y.H.; Chen X.C.; Wang N.; Lee Y.C.; Chen W.J.;
Mov. Disord. 39:152-163(2024)
Cited for: VARIANTS SPAX10 SER-124; HIS-145; ARG-184; HIS-240 AND TRP-249; CHARACTERIZATION OF VARIANT SPAX10 HIS-240; ALTERNATIVE SPLICING;
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.