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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P09622: Variant p.Lys72Glu

Dihydrolipoyl dehydrogenase, mitochondrial
Gene: DLD
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Variant information Variant position: help 72 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 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: help 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: 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 DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 72 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 509 The length of the canonical sequence.
Location on the sequence: help 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALL

                              GGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALL

Mouse                         GGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALL

Rat                           GGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALL

Pig                           GGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALL

Bovine                        GGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALL

Caenorhabditis elegans        GGYVAAIKAAQLGMKTVCVEKNATLGGTCLNVGCIPSKALL

Slime mold                    GGYVAGIKAGQLGMKVTVVEKRGKLGGTCLNVGCIPSKALL

Baker's yeast                 AGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALL

Fission yeast                 GGYVAAIRGAQLGLKTICVEKRGTLGGTCLNVGCIPSKALL
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 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.