Search Results
Overview
| Uniprot ID | P30613 |
|---|---|
| Protein Name | Pyruvate kinase PKLR |
| Gene Name | PKLR |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | ERLKEMIKAGMNIAR |
| 290 | VFASFVRKASDVAAV |
| 309 | GPEGHGIKIISKIEN |
| 313 | HGIKIISKIENHEGV |
| 321 | IENHEGVKRFDEILE |
| 419 | NFPVEAVKMQHAIAR |
| 541 | QFGIESGKLRGFLRV |
Function
Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis (PubMed:11960989). Also produces the side product 2-phospholactate which can inhibit fructose-2,6-bisphosphate production (PubMed:27294321). 2-phospholactate can be dephosphorylated by PGP which prevents the inhibition of fructose-2,6-bisphosphate production and allows glycolysis to occur (PubMed:27294321)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016301 | kinase activity |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0048029 | monosaccharide binding |
| Molecular Function | GO:0030955 | potassium ion binding |
| Molecular Function | GO:0004743 | pyruvate kinase activity |
| Biological Process | GO:0071872 | cellular response to epinephrine stimulus |
| Biological Process | GO:0032869 | cellular response to insulin stimulus |
| Biological Process | GO:0006096 | glycolytic process |
| Biological Process | GO:0042866 | pyruvate biosynthetic process |
| Biological Process | GO:0033198 | response to ATP |
| Biological Process | GO:0051591 | response to cAMP |
| Biological Process | GO:0009749 | response to glucose |
| Biological Process | GO:0001666 | response to hypoxia |
| Biological Process | GO:0010038 | response to metal ion |
| Biological Process | GO:0007584 | response to nutrient |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.