| Standard Name | PDX1 |
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| Systematic Name | YGR193C |
| Feature Type | ORF, Verified |
| Description | Dihydrolipoamide dehydrogenase (E3)-binding protein (E3BP) of the mitochondrial pyruvate dehydrogenase (PDH) complex, plays a structural role in the complex by binding and positioning E3 to the dihydrolipoamide acetyltransferase (E2) core (1, 2, 3 and see Summary Paragraph) |
| Name Description | Pyruvate Dehydrogenase complex protein X 1 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
Gene Ontology Annotations All PDX1 GO evidence and references
| View Computational GO annotations for PDX1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
Mutant phenotypes All PDX1 Phenotype evidence and references
interactions All PDX1 Interaction evidence and references
| 39 total interaction(s) for 31 unique genes/features. | |
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| Genetic Interactions |
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| Resources |
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Expression Summary
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| Resources |
Protein Information All PDX1 Protein evidence and references
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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Analyze Sequence
| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000003425 |
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SUMMARY PARAGRAPH for PDX1
PDX1 encodes the Protein X (E3-binding) subunit of the mitochondrial pyruvate dehydrogenase multienzyme complex (2). The pyruvate dehydrogenase complex consists of an E2 (Lat1p) core that binds E1 (Pda1p and Pdb1p), E3 (Lpd1p) and Protein X (Pdx1p) subunits (4). E1, E2, and E3 have catalytic activity; Pdx1p appears to be required for binding of the E3 subunit to the central E2 core (1). Cells lacking PDX1 are viable, but the pyruvate dehydrogenase complex is inactive (1). Mutations in the human homolog of PDX1 appear to be responsible for some cases of neonatal lactic acidosis (5).
References cited on this page View Complete Literature Guide for PDX1
| 1) | Lawson JE, et al. (1991) Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex. Biochemistry 30(11):2834-9 |
| 2) | Behal RH, et al. (1989) Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 86(22):8732-6 |
| 3) | Maeng CY, et al. (1994) Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Biochemistry 33(46):13801-7 |
| 4) | Pronk JT, et al. (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12(16):1607-33 |
| 5) | Aral B, et al. (1997) Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis. Am J Hum Genet 61(6):1318-26 |





