Variant position: 456 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:
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 EDNLKNSWVWKELYSVRNIR PSCHGVLGVYGGMIYTGIFYW
Mouse EDNLKQSWVWKELHAVRNIR PSCHGILGVYGGMIYTGIFYW
Rat EDNLKQSWVWKELHAVRNIR PSCHGILGVYGGMIYTGIFYW
Pig EDNLKNSWVWKELYSVRNIR PSCHGILGVYGGMIYTGIFYW
Bovine EDNLKKSWVWKELYAVRNIR PSCHSILGVYGGMIYTGIFYW
Caenorhabditis elegans DKNIRDTYVVKELKATRNIR PSFNTSLGYIGGLIYSGIFYV
Slime mold PEELKKSWVWKELREVRNYR PSLH--WGTIPGLIYGALEMY
Baker's yeast ESAFKESSIYKELYEVRNIR PSFSGKLGGYGGMIYSGIDSL
Fission yeast EENLKNTYVFKELYSVRNIR PSFHSFLGNYGGMAYSAVEAY
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.
Type Positions Description
34 – 617 Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
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;
The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene.
Gempel K.; Topaloglu H.; Talim B.; Schneiderat P.; Schoser B.G.; Hans V.H.; Palmafy B.; Kale G.; Tokatli A.; Quinzii C.; Hirano M.; Naini A.; DiMauro S.; Prokisch H.; Lochmueller H.; Horvath R.;
Cited for: VARIANTS GA2C PRO-377; LEU-456; LEU-483 AND GLU-590;
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.