PKM

Also known as CTHBP, HEL-S-30, OIP3, PK3, PKM2, TCB, THBP1, pyruvate kinase, muscle

Pyruvate kinase isozymes M1/M2 (PKM1/M2), also known as pyruvate kinase muscle isozyme (PKM), pyruvate kinase type K, cytosolic thyroid hormone-binding protein (CTHBP), thyroid hormone-binding protein 1 (THBP1), or opa-interacting protein 3 (OIP3), is an enzyme that in humans is encoded by the PKM2 gene.

Gene data

PKM

Name: pyruvate kinase M1/2
Type: protein-coding
Position: 72,199,026–72,231,819 (−)
Aliases: CTHBP, HEL-S-30, OIP3, PK3, PKM2, TCB, THBP1, p58
Ensembl: ENSG00000067225
RefSeq RNA: NM_001206796.3, NM_001206797.3, NM_001206798.3, NM_001206799.2, NM_001316318.2
RefSeq protein: NP_001193725.1, NP_001193726.1, NP_001193727.1, NP_001193728.1, NP_001303247.1

This gene encodes a protein involved in glycolysis. The encoded protein is a pyruvate kinase that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP and pyruvate. This protein has been shown to interact with thyroid hormone and may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis. Several alternatively spliced transcript variants encoding a few distinct isoforms have been reported. [provided by RefSeq, May 2011].

Gene Ontology

Biological process

Article

16 sections

Contents

Discovery
Structure
Function
Localization
Tissue
Cellular
Subcellular
Clinical significance
Bi-functional role within tumors
Natural mutations and carcinogenesis
Regulatory circuits
Bacterial pathogenesis
Interactive pathway map
See also
References
External links

PKM2 is an isoenzyme of the glycolytic enzyme pyruvate kinase. Depending upon the different metabolic functions of the tissues, different isoenzymes of pyruvate kinase are expressed. PKM2 is expressed in some differentiated tissues, such as lung, fat tissue, retina, and pancreatic islets, as well as in all cells with a high rate of nucleic acid synthesis, such as normal proliferating cells, embryonic cells, and especially tumor cells.