Variant position: 302 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 MELQTYRYHGHSMSDPGVSY RTREEIQEVRSKSDPIMLLKD
Chimpanzee MELQTYRYHGHSMSGPGVSY RTREEIQEVRSKSDPIMLLKD
Mouse MELQTYRYHGHSMSDPGVSY RTREEIQEVRSKSDPIMLLKD
Rat MELQTYRYHGHSMSDPGVSY RTREEIQEVRSKSDPIMLLKD
Bovine MELQTYRYHGHSMSDPGVSY RTREEIQEVRSKSDPIMLLKD
Caenorhabditis elegans MEMATYRYHGHSMSDPGTSY RTREEIQEVRKTRDPITGFKD
Slime mold LEMDTYRYVGHSMSDPGITY RTREEVNHVRQTRDPIENIRQ
Baker's yeast LEYETYRYGGHSMSDPGTTY RTRDEIQHMRSKNDPIAGLKM
Fission yeast MEFVTYRYGGHSMSDPGTTY RSREEVQKVRAARDPIEGLKK
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
30 – 390 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
293 – 293 Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
295 – 295 Phosphoserine
300 – 300 Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
301 – 301 Phosphotyrosine
313 – 313 N6-acetyllysine; alternate
313 – 313 N6-succinyllysine; alternate
321 – 321 N6-acetyllysine
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.
300 – 302
X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation.
Dahl H.-H.M.; Hansen L.L.; Brown R.M.; Danks D.M.; Rogers J.G.; Brown G.K.;
J. Inherit. Metab. Dis. 15:835-847(1992)
Cited for: VARIANT PDHAD CYS-302;
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;
Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity.
Otero L.J.; Brown R.M.; Brown G.K.;
Hum. Mutat. 12:114-121(1998)
Cited for: VARIANTS PDHAD CYS-302 AND HIS-302;
Diagnostic targeted resequencing in 349 patients with drug-resistant pediatric epilepsies identifies causative mutations in 30 different genes.
Parrini E.; Marini C.; Mei D.; Galuppi A.; Cellini E.; Pucatti D.; Chiti L.; Rutigliano D.; Bianchini C.; Virdo S.; De Vita D.; Bigoni S.; Barba C.; Mari F.; Montomoli M.; Pisano T.; Rosati A.; Guerrini R.;
Hum. Mutat. 38:216-225(2017)
Cited for: VARIANT PDHAD 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.