Search Results
Overview
| Uniprot ID | P35486 |
|---|---|
| Protein Name | Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial |
| Gene Name | Pdha1 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 149 | RGGCAKGKGGSMHMY |
| 18 | VLAGSAQKPASRVLV |
| 244 | AASTDYYKRGDFIPG |
| 277 | AAYCRSGKGPILMEL |
| 313 | EIQEVRSKSDPIMLL |
| 321 | SDPIMLLKDRMVNSN |
| 385 | RGANQWIKFKSVS** |
| 63 | LTREDGLKYYRMMQT |
| 77 | TVRRMELKADQLYKQ |
| 83 | LKADQLYKQKIIRGF |
Function
Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex. The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (By similarity). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed:11708858, PubMed:20841503)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0043209 | myelin sheath |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0045254 | pyruvate dehydrogenase complex |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0004739 | pyruvate dehydrogenase (acetyl-transferring) activity |
| Biological Process | GO:0006006 | glucose metabolic process |
| Biological Process | GO:0006086 | pyruvate decarboxylation to acetyl-CoA |
| Biological Process | GO:0006099 | tricarboxylic acid cycle |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.