Search Results
Overview
| Uniprot ID | P09411 |
|---|---|
| Protein Name | Phosphoglycerate kinase 1 |
| Gene Name | Pgk1 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 131 | FHVEEEGKGKDASGN |
| 146 | KVKAEPAKIDAFRAS |
| 192 | AGGFLMKKELNYFAK |
| 30 | VDFNVPMKNNQITNN |
| 361 | SLMDEVVKATSRGCI |
Function
Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). Acts as a protein kinase when localized to the mitochondrion where it phosphorylates pyruvate dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex activity and suppress the formation of acetyl-coenzyme A from pyruvate, and consequently inhibit oxidative phosphorylation and promote glycolysis. May play a role in sperm motility
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0045121 | membrane raft |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Molecular Function | GO:0043531 | ADP binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0004618 | phosphoglycerate kinase activity |
| Molecular Function | GO:0106310 | protein serine kinase activity |
| Molecular Function | GO:0004674 | protein serine/threonine kinase activity |
| Molecular Function | GO:0047134 | protein-disulfide reductase [NAD(P)H] activity |
| Molecular Function | GO:0044325 | transmembrane transporter binding |
| Biological Process | GO:0061621 | canonical glycolysis |
| Biological Process | GO:0071456 | cellular response to hypoxia |
| Biological Process | GO:0030855 | epithelial cell differentiation |
| Biological Process | GO:0006094 | gluconeogenesis |
| Biological Process | GO:0046166 | glyceraldehyde-3-phosphate biosynthetic process |
| Biological Process | GO:0006096 | glycolytic process |
| Biological Process | GO:0016525 | negative regulation of angiogenesis |
| Biological Process | GO:0160218 | negative regulation of pyruvate decarboxylation to acetyl-CoA |
| Biological Process | GO:0031639 | plasminogen activation |
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.