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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95831: Variant p.Val243Leu

Apoptosis-inducing factor 1, mitochondrial
Gene: AIFM1
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Variant information Variant position: help 243 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Valine (V) to Leucine (L) at position 243 (V243L, p.Val243Leu). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 243 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 613 The length of the canonical sequence.
Location on the sequence: help GGVAVLTGKKVVQLDVRDNM V KLNDGSQITYEKCLIATGGT 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGT

Mouse                         GGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGT

Rat                           GGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGT

Drosophila                    GGIAVAQGFSVKKVDAQKRIVTLNDGYEISYDECLIATGCA

Slime mold                    EILQFIRTKKVIDLHIDEKLVLLNDGKLIRYDKCLIATGGE
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 102 – 613 Apoptosis-inducing factor 1, mitochondrial
Region 134 – 483 FAD-dependent oxidoreductase
Binding site 233 – 233
Cross 255 – 255 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 1 – 352 Missing. In isoform 5.
Alternative sequence 36 – 322 Missing. In isoform 2.
Alternative sequence 44 – 613 Missing. In isoform 6.
Beta strand 242 – 245



Literature citations
Structure/Function Relations in AIFM1 Variants Associated with Neurodegenerative Disorders.
Sevrioukova I.F.;
J. Mol. Biol. 428:3650-3665(2016)
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 103-613 IN COMPLEX WITH FAD; CHARACTERIZATION OF VARIANT SER-262; CHARACTERIZATION OF VARIANTS COXPD6 LEU-243; GLU-308 AND GLU-338; FUNCTION; DNA-BINDING; FAD-BINDING; CATALYTIC ACTIVITY; COFACTOR; From ventriculomegaly to severe muscular atrophy: Expansion of the clinical spectrum related to mutations in AIFM1.
Kettwig M.; Schubach M.; Zimmermann F.A.; Klinge L.; Mayr J.A.; Biskup S.; Sperl W.; Gaertner J.; Huppke P.;
Mitochondrion 21C:12-18(2015)
Cited for: VARIANT COXPD6 LEU-243; CHARACTERIZATION OF VARIANT COXPD6 LEU-243;
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.