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Pkm - pyruvate kinase M1/2 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-14
Description
Enables several functions, including ADP binding activity; pyruvate kinase activity; and thyroid hormone binding activity. Involved in several processes, including protein homotetramerization; pyruvate metabolic process; and response to insulin. Part of pyruvate kinase complex. Biomarker of hypertension. Orthologous to human PKM (pyruvate kinase M1/2).

1 Names and Identifiers

1.1 Synonyms

  • PK
  • PKM12
  • Pk3
  • Pkm2
  • pyruvate kinase PKM
  • M2 pyruvate kinase
  • pyruvate kinase isozymes M1/M2
  • pyruvate kinase muscle isozyme
  • pyruvate kinase, muscle
  • threonine-protein kinase PKM2
  • tyrosine-protein kinase PKM2

1.1.1 MeSH Entry Terms

  • 3,5,3'-triiodothyronine-Binding Protein
  • Cytosolic Thyroid Hormone-Binding Protein
  • Pyruvate Kinase, M1 Isozyme
  • Pyruvate Kinase Muscle Isozyme
  • T3-Binding Protein p55
  • T4-Binding Protein p55
  • Thyroid Hormone-Binding Protein
  • Thyroid Hormone-Binding Protein p55
  • Thyroid Hormone-Binding Protein p58
  • Triiodothyronine-Binding Protein p55

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 Enzyme Commission (EC) Number

1.2.5 RGD ID

1.2.6 VEuPathDB ID

1.2.7 Wikidata

3 Proteins

3.1 Protein Function

Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.

Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity. In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase. Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase. Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription. Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (By similarity). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages. May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (By similarity).

Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth. In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity.

3.2 Protein Isoforms

Isoform
Isoform M1
UniProt ID
RefSeq Accession
Isoform
Isoform M2
UniProt ID
RefSeq Accession

3.3 Protein 3D Structures

3.3.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

3.4 Protein Targets

4 Chemicals and Bioactivities

4.1 Tested Compounds

5 BioAssays

5.1 Small-Molecule BioAssays

6 Interactions and Pathways

6.1 Interactions

6.2 Pathways

7 Biochemical Reactions

8 Expression

9 Literature

9.1 Consolidated References

9.2 NLM Curated PubMed Citations

9.3 Gene-Chemical Co-Occurrences in Literature

9.4 Gene-Gene Co-Occurrences in Literature

9.5 Gene-Disease Co-Occurrences in Literature

10 Patents

10.1 Gene-Chemical Co-Occurrences in Patents

10.2 Gene-Gene Co-Occurrences in Patents

10.3 Gene-Disease Co-Occurrences in Patents

11 Classification

11.1 MeSH Tree

11.2 Gene Ontology: Biological Process

11.3 Gene Ontology: Cellular Component

11.4 Gene Ontology: Molecular Function

11.5 ChEMBL Target Tree

11.6 Enzyme Classification

12 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Medical Subject Headings (MeSH)
    LICENSE
    Works produced by the U.S. government are not subject to copyright protection in the United States. Any such works found on National Library of Medicine (NLM) Web sites may be freely used or reproduced without permission in the U.S.
    https://www.nlm.nih.gov/copyright.html
  4. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  5. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  6. STRING: functional protein association networks
  7. NCBI Gene Expression Omnibus (GEO)
  8. Rat Genome Database (RGD)
    LICENSE
    Creative Commons Attribution 4.0 International license (CC BY 4.0)
    https://creativecommons.org/licenses/by/4.0/
  9. Swiss Institute of Bioinformatics Bgee
    LICENSE
    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  10. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  11. VEuPathDB: The Eukaryotic Pathogen, Vector and Host Informatics Resource
    LICENSE
    All data on VEuPathDB websites are provided freely for public use.
    https://veupathdb.org/veupathdb/app/static-content/about.html
  12. Wikidata
  13. ChEMBL
    LICENSE
    Access to the web interface of ChEMBL is made under the EBI's Terms of Use (http://www.ebi.ac.uk/Information/termsofuse.html). The ChEMBL data is made available on a Creative Commons Attribution-Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-sa/3.0/).
    http://www.ebi.ac.uk/Information/termsofuse.html
  14. Swiss Institute of Bioinformatics ENZYME
    LICENSE
    Copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution (CC BY 4.0) License (https://creativecommons.org/licenses/by/4.0/).
    https://enzyme.expasy.org/enzyme.get
    Enzyme Classification
    https://enzyme.expasy.org/
  15. Gene Ontology (GO)
    LICENSE
    Gene Ontology Consortium data and data products are licensed under the Creative Commons Attribution 4.0 Unported License (https://creativecommons.org/licenses/by/4.0/legalcode)
    http://geneontology.org/docs/go-citation-policy/
  16. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  17. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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