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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y3A0: Variant p.Phe146Cys

Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
Gene: COQ4
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Variant information Variant position: help 146 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 Phenylalanine (F) to Cysteine (C) at position 146 (F146C, p.Phe146Cys). 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 (F) to medium size and polar (C) 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 COQ10D7 and SPAX10; 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 146 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 EYLRFLDVNRVSPDTRAPTR F VDDEELAYVIQRYREVHDML 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                         EYLRFLDVNRVSPDTRAPTRFVDDEELAYVIQRYREVHDML

Mouse                         EYLRFLDVNKVSPDTRAPTRFVDDEELAYVIQRYREVHDML

Rat                           EYLRFLNANKVSPDTRAPTRFVDDEELAYVIQRYREVHDML

Bovine                        AYLHFLDVNRVSPDTRAPTRFVDDEELAYVIQRYREIHDML

Xenopus laevis                EYARFLDVNRVTPDTRMPVKFVDDEELAYVAQRYREVHDLM

Xenopus tropicalis            EYARFLDVNHVTPDTRMPVKFVDDEELAYVAQRYREVHDLM

Zebrafish                     EYLRFLEENRVTPDTRAEVKFVDNEELAYVMQRYREVHDLL

Caenorhabditis elegans        LYSNFLDRLNTSPDARPTVKYIDNLEHLYVMQRYRETHDFT

Drosophila                    AYVKFLKDNQVTPDSRMAVRFLEDPKLAYLMTRYRECHDLI

Slime mold                    AYYRWMKEHGYSPDERTEVTLIQDEDDAYVMQRYREVHDFW

Baker's yeast                 VYYQWLKRENVSPDTRAPVKFIDDPMHAYIFKRYRQCHDFY

Fission yeast                 IYVDWIDKEHVGPDTRSPTRFVDDPEEAYVMQRYRESHDFY
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 163 – 163
Binding site 164 – 164
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
Clinical spectrum in multiple families with primary COQ10 deficiency.
Hashemi S.S.; Zare-Abdollahi D.; Bakhshandeh M.K.; Vafaee A.; Abolhasani S.; Inanloo Rahatloo K.; DanaeeFard F.; Farboodi N.; Rohani M.; Alavi A.;
Am. J. Med. Genet. A 185:440-452(2021)
Cited for: VARIANT COQ10D7 CYS-146;
Bi-allelic COQ4 variants cause adult-onset ataxia-spasticity spectrum disease.
Cordts I.; Semmler L.; Prasuhn J.; Seibt A.; Herebian D.; Navaratnarajah T.; Park J.; Deininger N.; Laugwitz L.; Goericke S.L.; Lingor P.; Brueggemann N.; Muenchau A.; Synofzik M.; Timmann D.; Mayr J.A.; Haack T.B.; Distelmaier F.; Deschauer M.;
Mov. Disord. 37:2147-2153(2022)
Cited for: VARIANTS SPAX10 HIS-102; LYS-126; HIS-145; CYS-146 AND GLN-158; VARIANT COQ10D7 GLY-145; INVOLVEMENT IN SPAX10;
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.