UniProtKB/Swiss-Prot P09622: Variant p.Lys104Thr

Dihydrolipoyl dehydrogenase, mitochondrial
Gene: DLD
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Variant information Variant position:

104 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Lysine (K) to Threonine (T) at position 104 (K104T, p.Lys104Thr). 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 polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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
Other resources:

Links to websites of interest for the variant.

Variant rs1130477 [ dbSNP | Ensembl ]

Sequence information Variant position:

104 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:

GCIPSKALLNNSHYYHMAHG K DFASRGIEMSEVRLNLDKMM 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                         GCIPSKALLNNSHYYHMAHGKDFASRGIEMS-EVRLNLDKMM

                              GCIPSKALLNNSHYYHMAHGKDFASRGIEMS-EVRLNLEKM

Mouse                         GCIPSKALLNNSHYYHMAHGKDFASRGIEIP-EVRLNLEKM

Rat                           GCIPSKALLNNSHYYHLAHGKDFASRGIEIP-EVRLNLEKM

Pig                           GCIPSKALLNNSHYYHMAHGKDFASRGIEMS-EVRLNLEKM

Bovine                        GCIPSKALLNNSHFYHLAHGKDFASRGIEMS-EVRLNLEKM

Caenorhabditis elegans        GCIPSKALLNNSHYLHMAQ-HDFAARGIDCT--ASLNLPKM

Slime mold                    GCIPSKALLNASHLYEEATTK-MSKYGVKCS-GVELDLGAM

Baker's yeast                 GCIPSKALLNNSHLFHQMH-TEAQKRGIDVNGDIKINVANF

Fission yeast                 GCIPSKALLNNSHIYHTVK-HDTKRRGIDVS-GVSVNLSQM

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	89 – 89
Modified residue	104 – 104	N6-acetyllysine; alternate
Modified residue	104 – 104	N6-succinyllysine; alternate
Modified residue	122 – 122	N6-acetyllysine; alternate
Modified residue	122 – 122	N6-succinyllysine; alternate
Mutagenesis	89 – 89	K -> E. Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.

Literature citations
Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases.
Otulakowski G.; Robinson B.H.;
J. Biol. Chem. 262:17313-17318(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT THR-104; The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements.
Feigenbaum A.S.; Robinson B.H.;
Genomics 17:376-381(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT THR-104;

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.