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UniProtKB/Swiss-Prot Q16134: Variant p.Ser82Pro

Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
Gene: ETFDH
Variant information

Variant position:  82
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Serine (S) to Proline (P) at position 82 (S82P, p.Ser82Pro).
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 small size and polar (S) to medium size and hydrophobic (P)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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

Involvement in disease:  Glutaric aciduria 2C (GA2C) [MIM:231680]: An autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. {ECO:0000269|PubMed:12359134, ECO:0000269|PubMed:12815589, ECO:0000269|PubMed:16527485, ECO:0000269|PubMed:17412732, ECO:0000269|PubMed:19249206, ECO:0000269|PubMed:20370797}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In GA2C.
Any additional useful information about the variant.



Sequence information

Variant position:  82
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  617
The length of the canonical sequence.

Location on the sequence:   MERFAEEADVVIVGAGPAGL  S AAVRLKQLAVAHEKDIRVCL
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                         MERFAEEADVVIVGAGPAGLSAAVRLKQLAVAHEK-DIRVCL

Mouse                         MERFAEEADVVIVGAGPAGLSAAIRLKQLAAEQGK-DIRVC

Rat                           MERFAEEADVVIVGAGPAGLSAAIRLKQLAAEQEK-DIRVC

Pig                           MERFAEEADVVIVGAGPAGLSAATRLKQLAAQHEK-DLRVC

Bovine                        MERFAEEADVVIVGAGPAGLSAAARLKQLAAQHEK-DIRVC

Caenorhabditis elegans        LARESDVYDVVIVGGGPSGLSAAIRLRQLAEKAQK-ELRVC

Slime mold                    PPRDSDQFDVVIVGAGPSGLSTAIRLKQLSEKAGK-DLRVC

Baker's yeast                 EPRARDYVDVCIVGGGPAGLATAIKLKQLDNSSGTGQLRVV

Fission yeast                 IEREVEDVDVCIVGAGPAGLSAAIRIKQQAAKANR-DIRVV

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 34 – 617 Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
Nucleotide binding 71 – 85 FAD
Modified residue 96 – 96 N6-acetyllysine


Literature citations

Glutaric acidemia type II: gene structure and mutations of the electron transfer flavoprotein:ubiquinone oxidoreductase (ETF:QO) gene.
Goodman S.I.; Binard R.J.; Woontner M.R.; Frerman F.E.;
Mol. Genet. Metab. 77:86-90(2002)
Cited for: VARIANTS GA2C CYS-49; PHE-82; PRO-82; ARG-138; ASN-218; PRO-222; PHE-262; PRO-334; ARG-346; LYS-452; LEU-456; LEU-562 AND GLU-611; VARIANTS CYS-16 AND ILE-31;

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.