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KCNJ6

Protein-coding gene in the species Homo sapiens


Protein-coding gene in the species Homo sapiens

G protein-activated inward rectifier potassium channel 2 is a protein that in humans is encoded by the KCNJ6 gene. Mutation in KCNJ6 gene has been proposed to be the cause of Keppen-Lubinsky Syndrome (KPLBS).

Function

Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and may be involved in the regulation of insulin secretion by glucose. It associates with two other G-protein-activated potassium channels to form a heteromultimeric pore-forming complex.

Interactions

KCNJ6 has been shown to interact with KCNJ9 and DLG1.

References

References

  1. (August 1995). "Characterization and variation of a human inwardly-rectifying-K-channel gene (KCNJ6): a putative ATP-sensitive K-channel subunit". FEBS Letters.
  2. (December 2005). "International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels". Pharmacological Reviews.
  3. "Entrez Gene: KCNJ6 potassium inwardly-rectifying channel, subfamily J, member 6".
  4. (2015-02-05). "Keppen-Lubinsky Syndrome Is Caused by Mutations in the Inwardly Rectifying K+ Channel Encoded by KCNJ6". American Journal of Human Genetics.
  5. (November 2000). "Functional and biochemical evidence for G-protein-gated inwardly rectifying K+ (GIRK) channels composed of GIRK2 and GIRK3". Journal of Biological Chemistry.
  6. (November 2002). "G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase". Journal of Biological Chemistry.
  7. (January 2000). "Anchoring proteins confer G protein sensitivity to an inward-rectifier K(+) channel through the GK domain". The EMBO Journal.
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