KCNJ4
Potassium inwardly-rectifying channel, subfamily J, member 4 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||||
Symbols | KCNJ4 ; HIR; HIRK2; HRK1; IRK3; Kir2.3; MGC142066; MGC142068 | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 3653 | ||||||||||
| |||||||||||
RNA expression pattern | |||||||||||
More reference expression data | |||||||||||
Orthologs | |||||||||||
Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
Potassium inwardly-rectifying channel, subfamily J, member 4, also known as KCNJ4 or Kir2.3, is a human gene.[1]
Several different potassium channels are known to be involved with electrical signaling in the nervous system. One class is activated by depolarization whereas a second class is not. The latter are referred to as inwardly rectifying K+ channels, and they have a greater tendency to allow potassium to flow into the cell rather than out of it. This asymmetry in potassium ion conductance plays a key role in the excitability of muscle cells and neurons. The protein encoded by this gene is an integral membrane protein and member of the inward rectifier potassium channel family. The encoded protein has a small unitary conductance compared to other members of this protein family. Two transcript variants encoding the same protein have been found for this gene.[1]
See also
References
Further reading
- Kubo Y, Adelman JP, Clapham DE; et al. (2006). "International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels". Pharmacol. Rev. 57 (4): 509–26. doi:10.1124/pr.57.4.11. PMID 16382105.
- Budarf ML, Périer F, Barnoski BL; et al. (1995). "Assignment of the human hippocampal inward rectifier potassium channel (HIR) gene to 22q13.1". Genomics. 26 (3): 625–9. PMID 7607694.
- Périer F, Radeke CM, Vandenberg CA (1994). "Primary structure and characterization of a small-conductance inwardly rectifying potassium channel from human hippocampus". Proc. Natl. Acad. Sci. U.S.A. 91 (13): 6240–4. PMID 8016146.
- Tang W, Yang XC (1994). "Cloning a novel human brain inward rectifier potassium channel and its functional expression in Xenopus oocytes". FEBS Lett. 348 (3): 239–43. PMID 8034048.
- Makhina EN, Kelly AJ, Lopatin AN; et al. (1994). "Cloning and expression of a novel human brain inward rectifier potassium channel". J. Biol. Chem. 269 (32): 20468–74. PMID 8051145.
- Cohen NA, Brenman JE, Snyder SH, Bredt DS (1996). "Binding of the inward rectifier K+ channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation". Neuron. 17 (4): 759–67. PMID 8893032.
- Cohen NA, Sha Q, Makhina EN; et al. (1997). "Inhibition of an inward rectifier potassium channel (Kir2.3) by G-protein betagamma subunits". J. Biol. Chem. 271 (50): 32301–5. PMID 8943291.
- Zhu G, Qu Z, Cui N, Jiang C (1999). "Suppression of Kir2.3 activity by protein kinase C phosphorylation of the channel protein at threonine 53". J. Biol. Chem. 274 (17): 11643–6. PMID 10206975.
- Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. PMID 10479680.
- Dunham I, Shimizu N, Roe BA; et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
- Nehring RB, Wischmeyer E, Döring F; et al. (2000). "Neuronal inwardly rectifying K(+) channels differentially couple to PDZ proteins of the PSD-95/SAP90 family". J. Neurosci. 20 (1): 156–62. PMID 10627592.
- Leonoudakis D, Mailliard W, Wingerd K; et al. (2001). "Inward rectifier potassium channel Kir2.2 is associated with synapse-associated protein SAP97". J. Cell. Sci. 114 (Pt 5): 987–98. PMID 11181181.
- Liu Y, Liu D, Heath L; et al. (2001). "Direct activation of an inwardly rectifying potassium channel by arachidonic acid". Mol. Pharmacol. 59 (5): 1061–8. PMID 11306688.
- Perillan PR, Chen M, Potts EA, Simard JM (2002). "Transforming growth factor-beta 1 regulates Kir2.3 inward rectifier K+ channels via phospholipase C and protein kinase C-delta in reactive astrocytes from adult rat brain". J. Biol. Chem. 277 (3): 1974–80. doi:10.1074/jbc.M107984200. PMID 11713246.
- Olsen O, Liu H, Wade JB; et al. (2002). "Basolateral membrane expression of the Kir 2.3 channel is coordinated by PDZ interaction with Lin-7/CASK complex". Am. J. Physiol., Cell Physiol. 282 (1): C183–95. doi:10.1152/ajpcell.00249.2001. PMID 11742811.
- Inanobe A, Fujita A, Ito M; et al. (2002). "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses". Am. J. Physiol., Cell Physiol. 282 (6): C1396–403. doi:10.1152/ajpcell.00615.2001. PMID 11997254.
- Preisig-Müller R, Schlichthörl G, Goerge T; et al. (2002). "Heteromerization of Kir2.x potassium channels contributes to the phenotype of Andersen's syndrome". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7774–9. doi:10.1073/pnas.102609499. PMID 12032359.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Leonoudakis D, Conti LR, Radeke CM; et al. (2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63. doi:10.1074/jbc.M400284200. PMID 14960569.
- Leonoudakis D, Conti LR, Anderson S; et al. (2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.
External links
- KCNJ4+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
Stub icon | This membrane protein–related article is a stub. You can help Wikipedia by expanding it. |
This article incorporates text from the United States National Library of Medicine, which is in the public domain.