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UniProtKB/Swiss-Prot P09622 : Variant p.Lys72Glu
Dihydrolipoyl dehydrogenase, mitochondrial
Gene: DLD
Variant information
Variant position: 72 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]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: From Lysine (K) to Glutamate (E) at position 72 (K72E, p.Lys72Glu).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 large size and basic (K) to medium size and acidic (E)The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: 1The 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: In DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX.Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.
Sequence information
Variant position: 72 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 509 The length of the canonical sequence.
Location on the sequence:
GGYVAAIKAAQLGFKTVCIE
K NETLGGTCLNVGCIPSKALL
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 GGYVAAIKAAQLGFKTVCIEK NETLGGTCLNVGCIPSKALL
GGYVAAIKAAQLGFKTVCVEK NETLGGTCLNVGCIPSKALL
Mouse GGYVAAIKSAQLGFKTVCIEK NETLGGTCLNVGCIPSKALL
Rat GGYVAAIKAAQLGFKTVCIEK NETLGGTCLNVGCIPSKALL
Pig GGYVAAIKAAQLGFKTVCIEK NETLGGTCLNVGCIPSKALL
Caenorhabditis elegans GGYVAAIKAAQLGMKTVCVEK NATLGGTCLNVGCIPSKALL
Slime mold GGYVAGIKAGQLGMKVTVVEK RGKLGGTCLNVGCIPSKALL
Baker's yeast AGYVAAIKAAQLGFNTACVEK RGKLGGTCLNVGCIPSKALL
Fission yeast GGYVAAIRGAQLGLKTICVEK RGTLGGTCLNVGCIPSKALL
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
Chain
36 – 509
Dihydrolipoyl dehydrogenase, mitochondrial
Binding site
71 – 80
Binding site
89 – 89
Modified residue
66 – 66
N6-acetyllysine; alternate
Modified residue
66 – 66
N6-succinyllysine; alternate
Alternative sequence
1 – 99
Missing. In isoform 2.
Mutagenesis
89 – 89
K -> E. Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
Literature citations
Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex.
Patel M.S.; Korotchkina L.G.; Sidhu S.;
J. Mol. Catal., B Enzym. 61:2-6(2009)
Cited for: CATALYTIC ACTIVITY; INTERACTION WITH PDHX; MUTAGENESIS OF LYS-89; ARG-482; GLU-492 AND LYS-505; CHARACTERIZATION OF VARIANTS DLDD GLU-72; LYS-375; LEU-488 AND GLY-495;
Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient.
Liu T.-C.; Kim H.; Arizmendi C.; Kitano A.; Patel M.S.;
Proc. Natl. Acad. Sci. U.S.A. 90:5186-5190(1993)
Cited for: VARIANTS DLDD GLU-72 AND LEU-488;
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.