Search Results
Overview
| Uniprot ID | P16617 |
|---|---|
| Protein Name | Phosphoglycerate kinase 1 |
| Gene Name | Pgk1 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 11 | SNKLTLDKLDVKGKR |
| 131 | FHVEEEGKGKDASGN |
| 146 | KVKAEPAKIDAFRAS |
| 156 | AFRASLSKLGDVYVN |
| 184 | VGVNLPQKAGGFLMK |
| 192 | AGGFLMKKELNYFAK |
| 216 | LAILGGAKVADKIQL |
| 220 | GGAKVADKIQLINNM |
| 267 | EEGAKIVKDLMAKAE |
| 30 | VDFNVPMKNNQITNN |
| 323 | CGTESSKKYAEAVAR |
| 353 | EAFARGTKSLMDEVV |
| 361 | SLMDEVVKATSRGCI |
| 41 | ITNNQRIKAAVPSIK |
| 6 | **MSLSNKLTLDKLD |
| 91 | ELKSLLGKDVLFLKD |
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: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: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] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.
[2] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.
[3] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.