Variant position: 263 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 YKRGDFIPGLRVDGMDILCV REATRFAAAYCRSGKGPILME
Chimpanzee YKRGDFIPGLRVDGMDILCV REATRFAAAYCRSGKGPILME
Mouse YKRGDFIPGLRVDGMDILCV REATKFAAAYCRSGKGPILME
Rat YKRGDFIPGLRVDGMDILCV REATKFAAAYCRSGKGPILME
Bovine YKRGDFIPGLRVDGMDILCV REATKFAAAYCRSGKGPILME
Caenorhabditis elegans YTRGDYVPGIWVDGMDILAV REATKWAKEYCDSGKGPLMME
Slime mold YTRGHYVAGLKVDGMDVFAV KEAGKYAAEWCRAGNGPIILE
Baker's yeast FKRGQYIPGLKVNGMDILAV YQASKFAKDWCLSGKGPLVLE
Fission yeast YKRGQYIPGLLVNGMDVLAV LQASKFAKKYTVENSQPLLME
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
244 – 244 N6-acetyllysine; alternate
244 – 244 N6-succinyllysine; alternate
277 – 277 N6-succinyllysine
259 – 274
Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex.
Chun K.; McKay N.; Petrova-Benedict R.; Robinson B.H.;
Hum. Mol. Genet. 2:449-454(1993)
Cited for: VARIANTS PDHAD MET-167; THR-199; ALA-231; GLY-263 AND LEU-292;
Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex.
Chun K.; MacKay N.; Petrova-Benedict R.; Federico A.; Fois A.; Cole D.E.C.; Robertson E.; Robinson B.H.;
Am. J. Hum. Genet. 56:558-569(1995)
Cited for: VARIANTS PDHAD CYS-72; LEU-205; GLY-263; ARG-311 DEL AND HIS-378;
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;
Biochemical and molecular analysis of an X-linked case of Leigh syndrome associated with thiamin-responsive pyruvate dehydrogenase deficiency.
Naito E.; Ito M.; Yokota I.; Saijo T.; Matsuda J.; Osaka H.; Kimura S.; Kuroda Y.;
J. Inherit. Metab. Dis. 20:539-548(1997)
Cited for: VARIANT PDHAD GLY-263;
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