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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P31513: Variant p.Glu308Gly

Flavin-containing monooxygenase 3
Gene: FMO3
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Variant information Variant position: help 308 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Glutamate (E) to Glycine (G) at position 308 (E308G, p.Glu308Gly). 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 medium size and acidic (E) to glycine (G) 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 16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 308 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 532 The length of the canonical sequence.
Location on the sequence: help LPASILCGIVSVKPNVKEFT E TSAIFEDGTIFEGIDCVIFA 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.
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 2 – 532 Flavin-containing monooxygenase 3



Literature citations
Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS HIS-132; LYS-158; CYS-205; MET-257; ALA-277; GLY-308; PRO-360 AND GLN-362; Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication.
Treacy E.P.; Akerman B.R.; Chow L.M.L.; Youil R.; Bibeau C.; Lin J.; Bruce A.G.; Knight M.; Danks D.M.; Cashman J.R.; Forrest S.M.;
Hum. Mol. Genet. 7:839-845(1998)
Cited for: CATALYTIC ACTIVITY; VARIANTS TMAU ILE-66 AND LEU-153; VARIANTS LYS-158; MET-257 AND GLY-308; Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria.
Yeung C.K.; Adman E.T.; Rettie A.E.;
Arch. Biochem. Biophys. 464:251-259(2007)
Cited for: BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS TMAU SER-61; ILE-66; LEU-153 AND TRP-492; CHARACTERIZATION OF VARIANTS LYS-158; MET-257 AND GLY-308; Trimethylaminuria is caused by mutations of the FMO3 gene in a North American cohort.
Akerman B.R.; Lemass H.; Chow L.M.L.; Lambert D.M.; Greenberg C.; Bibeau C.; Mamer O.A.; Treacy E.P.;
Mol. Genet. Metab. 68:24-31(1999)
Cited for: VARIANTS TMAU THR-52 AND LEU-387; VARIANTS LYS-158 AND GLY-308; Identification and functional analysis of common human flavin-containing monooxygenase 3 genetic variants.
Koukouritaki S.B.; Poch M.T.; Henderson M.C.; Siddens L.K.; Krueger S.K.; VanDyke J.E.; Williams D.E.; Pajewski N.M.; Wang T.; Hines R.N.;
J. Pharmacol. Exp. Ther. 320:266-273(2007)
Cited for: VARIANTS ASP-24; LYS-61; LYS-158; MET-257; GLY-308 AND ASN-416; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS ASP-24; LYS-61 AND ASN-416;
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.