Variant position: 288 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 390 The length of the canonical sequence.
Location on the sequence:
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 FAAAYCRSGKGPILMELQTY RYHGHSMSDPGVSYRTREEIQ
Chimpanzee FAAAYCRSGKGPILMELQTY RYHGHSMSGPGVSYRTREEIQ
Mouse FAAAYCRSGKGPILMELQTY RYHGHSMSDPGVSYRTREEIQ
Rat FAAAYCRSGKGPILMELQTY RYHGHSMSDPGVSYRTREEIQ
Bovine FAAAYCRSGKGPILMELQTY RYHGHSMSDPGVSYRTREEIQ
Caenorhabditis elegans WAKEYCDSGKGPLMMEMATY RYHGHSMSDPGTSYRTREEIQ
Slime mold YAAEWCRAGNGPIILEMDTY RYVGHSMSDPGITYRTREEVN
Baker's yeast FAKDWCLSGKGPLVLEYETY RYGGHSMSDPGTTYRTRDEIQ
Fission yeast FAKKYTVENSQPLLMEFVTY RYGGHSMSDPGTTYRSREEVQ
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
31 – 390 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
277 – 277 N6-succinyllysine
293 – 293 Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
295 – 295 Phosphoserine
300 – 300 Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
301 – 301 Phosphotyrosine
293 – 293 S -> A. Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300.
293 – 293 S -> E. Interferes with substrate binding.
300 – 300 S -> A. Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency.
Lissens W.; de Meirleir L.; Seneca S.; Benelli C.; Marsac C.; Poll-The B.T.; Briones P.; Ruitenbeek W.; van Diggelen O.; Chaigne D.; Ramaekers V.; Liebaers I.;
Hum. Mutat. 7:46-51(1996)
Cited for: VARIANTS PDHAD CYS-72; ASP-113; ARG-162; GLY-263; HIS-288 AND CYS-302;
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.