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UniProtKB/Swiss-Prot Q96H96: Variant p.Tyr247Cys

4-hydroxybenzoate polyprenyltransferase, mitochondrial
Gene: COQ2
Variant information

Variant position:  247
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 Tyrosine (Y) to Cysteine (C) at position 247 (Y247C, p.Tyr247Cys).
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 aromatic (Y) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In COQ10D1; decreased 4-hydroxybenzoate decaprenyltransferase activity.
Any additional useful information about the variant.



Sequence information

Variant position:  247
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  371
The length of the canonical sequence.

Location on the sequence:   SCDPSVCLPLYFSGVMWTLI  Y DTIYAHQDKRDDVLIGLKST
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                         S--CDPSVCLPLYFSGVMWTLIYDTIYAHQDKRDDVLIGLKST

Mouse                         S--CDPAVCLPLYFSGVMWTLIYDTIYAHQDKKDDALIGLK

Rat                           S--CDPAVCLPLYFSGVMWTLIYDTIYAHQDKKDDALIGLK

Bovine                        S--CDPSVCLPLYFSGIMWTLIYDTIYAHQDKKDDALIGLK

Caenorhabditis elegans        D--LSSSAPFWMYAAALQWTLIYDTIYAHQDKADDIMIGVK

Drosophila                    S--VNLAACLPLYLSGVCWTIVYDTIYAHQDKLDDLQIGVK

Slime mold                    S--CNWSIVAPLYLAGISWTMVYDTIYAHQDKRDDILVGVK

Baker's yeast                 V--MSWPTMIPLYLSSYLWCMTYDTIYAHQDKKFDIKAGIK

Fission yeast                 EACMNWSVVAPLYLSTISWIVLYDTIYAHQDKRDDVKANIY

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 35 – 371 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Transmembrane 232 – 252 Helical


Literature citations

Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis.
Lopez-Martin J.M.; Salviati L.; Trevisson E.; Montini G.; DiMauro S.; Quinzii C.; Hirano M.; Rodriguez-Hernandez A.; Cordero M.D.; Sanchez-Alcazar J.A.; Santos-Ocana C.; Navas P.;
Hum. Mol. Genet. 16:1091-1097(2007)
Cited for: CHARACTERIZATION OF VARIANTS COQ10D1 CYS-247; FUNCTION; CATALYTIC ACTIVITY;

The COQ2 genotype predicts the severity of coenzyme Q10 deficiency.
Desbats M.A.; Morbidoni V.; Silic-Benussi M.; Doimo M.; Ciminale V.; Cassina M.; Sacconi S.; Hirano M.; Basso G.; Pierrel F.; Navas P.; Salviati L.; Trevisson E.;
Hum. Mol. Genet. 25:4256-4265(2016)
Cited for: FUNCTION; SUBCELLULAR LOCATION; TOPOLOGY; CHARACTERIZATION OF VARIANTS COQ10D1 VAL-78; ASN-96; ARG-132; HIS-147; SER-178; CYS-247 AND VAL-252;

A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency.
Quinzii C.; Naini A.; Salviati L.; Trevisson E.; Navas P.; Dimauro S.; Hirano M.;
Am. J. Hum. Genet. 78:345-349(2006)
Cited for: VARIANT COQ10D1 CYS-247; CHARACTERIZATION OF VARIANT COQ10D1 CYS-247; FUNCTION; CATALYTIC ACTIVITY;

COQ2 nephropathy: a newly described inherited mitochondriopathy with primary renal involvement.
Diomedi-Camassei F.; Di Giandomenico S.; Santorelli F.M.; Caridi G.; Piemonte F.; Montini G.; Ghiggeri G.M.; Murer L.; Barisoni L.; Pastore A.; Muda A.O.; Valente M.L.; Bertini E.; Emma F.;
J. Am. Soc. Nephrol. 18:2773-2780(2007)
Cited for: VARIANTS COQ10D1 ASN-96; HIS-147; SER-178 AND CYS-247;

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.