PDHX
entrez
8050
canonical
uniprot
O00330
canonical
ensembl
ENSG00000110435
resolver
ensp
ENSP00000227868
resolver
ensp
ENSP00000389404
resolver
ensp
ENSP00000415695
resolver
enst
ENST00000448838
resolver
genesymbol
PDHX
resolver
genesymbol_syn
PDX1
resolver
hgnc
HGNC:21350
resolver
uniprot
A0A8C8MSB2
resolver
uniprot
B4DW62
resolver
uniprot
D3DR11
resolver
uniprot
E9PB14
resolver
uniprot
E9PBP7
resolver
uniprot
O60221
resolver
uniprot
Q96FV8
resolver
uniprot
Q99783
resolver
uniprot_entry
A0A8C8MSB2_HUMAN
resolver
uniprot_entry
ODPX_HUMAN
resolver
uniprot_sec
B4DW62
resolver
uniprot_sec
D3DR11
resolver
uniprot_sec
E9PB14
resolver
uniprot_sec
E9PBP7
resolver
uniprot_sec
O60221
resolver
uniprot_sec
Q96FV8
resolver
uniprot_sec
Q99783
resolver
amino_acid_sequence
MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA
uniprot
proteins
disease_involvement
DISEASE: Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:245349]: A metabolic disorder characterized by decreased activity of the pyruvate dehydrogenase complex without observable reduction in the activities of enzymes E1, E2, or E3. Clinical features include hypotonia and psychomotor retardation. {ECO:0000269|PubMed:9399911}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
uniprot
proteins
mass_dalton
54122
uniprot
proteins
mutagenesis
MUTAGEN 183; /note="R->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 185; /note="S->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 186; /note="P->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 187; /note="A->M: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 189; /note="R->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 190; /note="N->A: Decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:20160912"; MUTAGEN 190; /note="N->K: Moderately decreased interaction with DLD."; /evidence="ECO:0000269|PubMed:20160912"; MUTAGEN 193; /note="E->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 208; /note="R->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 208; /note="R->D: Decreased interaction with DLD."; /evidence="ECO:0000269|PubMed:20160912"; MUTAGEN 210; /note="I->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 210; /note="I->R: Decreased interaction with DLD."; /evidence="ECO:0000269|PubMed:20160912"; MUTAGEN 210; /note="I->S: Decreased interaction with DLD."; /evidence="ECO:0000269|PubMed:20160912"; MUTAGEN 213; /note="K->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803"; MUTAGEN 214; /note="E->A: Strongly decreased DLD binding."; /evidence="ECO:0000269|PubMed:16442803
uniprot
proteins
post_translational_modification
PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000269|PubMed:25525879}.
uniprot
proteins
protein_family
2-oxoacid dehydrogenase family
uniprot
proteins
pubmed
14638692
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263718
uniprot
proteins
pubmed
16442803
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20160912
uniprot
proteins
pubmed
20361979
uniprot
proteins
pubmed
20385101
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25525879
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
9110174
uniprot
proteins
pubmed
9242632
uniprot
proteins
pubmed
9399911
uniprot
proteins
pubmed
9467010
uniprot
proteins
sequence_length
501
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix.
uniprot
proteins