PKM

Cancer-related genes, Enzymes, Metabolic proteins, Plasma proteins

Intracellular

Cell type enhanced (Basal respiratory cells, Late spermatids)

Low immune cell specificity

Low cell line specificity

[Isoform M2]: Monomer and homotetramer; exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). The monomeric form binds 3,3',5-triiodo-L-thyronine (T3) (PubMed:15996096). Tetramer formation induces pyruvate kinase activity (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). FBP stimulates the formation of tetramers from dimers (PubMed:15996096, 18298799, 18337815, 1854723, 23064226, 2813362). Homodimer; exists in a dimeric form in tumor cells and the dimeric form has less affinity for the phosphoenolpyruvate substrate (PubMed:22306293, 24120661). The homodimer converts into a protein kinase (PubMed:22306293, 24120661). Interacts with HERC1, POU5F1 and PML (PubMed:12650930, 18191611). Interacts with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A (PubMed:21620138, 21483450). Interacts with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (PubMed:21620138). Interacts with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (PubMed:25263439). Interacts with JMJD8 (PubMed:27199445). Interacts with TRAF4 (PubMed:32268273). Interacts with (phosphorylated) CTNNB1; leading to activate transcription (PubMed:22056988). (Microbial infection) Binding to certain oncoproteins such as HPV-16 E7 oncoprotein promotes homodimerization.

Allosteric enzyme, Kinase, Transferase