Variant position: 266 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 333 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 GASRAAVDAGFVPNDMQVGQ TGKIVAPELYIAVGISGAIQH
Mouse GASRAAVDAGFVPNDMQVGQ TGKIVAPELYIAVGISGAIQH
Rat GASRAAVDAGFVPNDMQVGQ TGKIVAPELYIAVGISGAIQH
Bovine GASRAAVDAGFVTNDLQVGQ TGKIVAPELYIAVGISGAIQH
Caenorhabditis elegans GASRAAVDAGYVPNDMQVGQ TGKIVAPELYIAIGISGAIQH
Slime mold GASRAAVDSGFVSNDLQVGQ TGKIVAPELYIAVGISGAIQH
Baker's yeast GATRASVDNGLCDNSLQIGQ TGKVVAPNLYIAIGVSGAVQH
Fission yeast GATRVAVDSGYADNSLQIGQ TGKIIAPKLYIAVGIDGAIQH
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
20 – 333 Electron transfer flavoprotein subunit alpha, mitochondrial
263 – 266 FAD
205 – 333 Domain II
248 – 248 FAD
249 – 249 R -> A. Loss of electron transfer activity.
Clear relationship between ETF/ETFDH genotype and phenotype in patients with multiple acyl-CoA dehydrogenation deficiency.
Olsen R.K.J.; Andresen B.S.; Christensen E.; Bross P.; Skovby F.; Gregersen N.;
Hum. Mutat. 22:12-23(2003)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; ALTERNATIVE SPLICING; FUNCTION; VARIANT GA2A MET-266;
Glutaric acidemia type II. Heterogeneity in beta-oxidation flux, polypeptide synthesis, and complementary DNA mutations in the alpha subunit of electron transfer flavoprotein in eight patients.
Freneaux E.; Sheffield V.C.; Molin L.; Shires A.; Rhead W.;
J. Clin. Invest. 90:1679-1686(1992)
Cited for: VARIANTS GA2A ARG-116 AND MET-266; FUNCTION; CHARACTERIZATION OF VARIANT GA2A MET-266;
Expression and characterization of two pathogenic mutations in human electron transfer flavoprotein.
Salazar D.; Zhang L.; deGala G.D.; Frerman F.E.;
J. Biol. Chem. 272:26425-26433(1997)
Cited for: CHARACTERIZATION OF VARIANTS GA2A ARG-116 AND MET-266; FUNCTION; COFACTOR; SUBUNIT;
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.