KCNK18 Identifiers Aliases KCNK18 External IDs OMIM : 613655 MGI : 2685627 HomoloGene : 133808 GeneCards : KCNK18 Gene location (Human ) Chr. Chromosome 10 (human) [1] Band 10q25.3 Start 117,197,489 bp [1] End 117,210,299 bp [1]
Gene location (Mouse ) Chr. Chromosome 19 (mouse)[2] Band 19|19 D3 Start 59,207,646 bp [2] End 59,225,806 bp [2]
Gene ontology Molecular function Cellular component Biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez Ensembl UniProt RefSeq (mRNA) RefSeq (protein) Location (UCSC) Chr 10: 117.2 – 117.21 Mb Chr 19: 59.21 – 59.23 Mb PubMed search[3] [4] Wikidata
Potassium channel subfamily K member 18 (KCNK18), also known as TWIK-related spinal cord potassium channel (TRESK) or K2P 18.1 is a protein that in humans is encoded by the KCNK18 gene . K2P 18.1 is a potassium channel containing two pore-forming P domains.[5]
A flaw in this gene could help trigger migraine headaches. If the gene does not work properly, environmental factors can more easily trigger pain centres in the brain and cause a severe headache.[6]
See also [ ] Tandem pore domain potassium channel References [ ]
^ a b c GRCh38: Ensembl release 89: ENSG00000186795 - Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040901 - Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ Goldstein SA, Bayliss DA, Kim D, Lesage F, Plant LD, Rajan S (December 2005). "International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels" . Pharmacol. Rev . 57 (4): 527–40. doi :10.1124/pr.57.4.12 . PMID 16382106 . S2CID 7356601 . ^ Lafrenière RG, Cader MZ, Poulin JF, Andres-Enguix I, Simoneau M, Gupta N, Boisvert K, Lafrenière F, McLaughlan S, Dubé MP, Marcinkiewicz MM, Ramagopalan S, Ansorge O, Brais B, Sequeiros J, Pereira-Monteiro JM, Griffiths LR, Tucker SJ, Ebers G, Rouleau GA (September 2010). "A dominant-negative mutation in the TRESK potassium channel is linked to familial migraine with aura". Nature Medicine . 16 (10): 1157–1160. doi :10.1038/nm.2216 . PMID 20871611 . S2CID 205387180 . Lay summary – BBC News (2010-09-27).
Further reading [ ]
Andres-Enguix I, Shang L, Stansfeld PJ, Morahan JM, Sansom MS, Lafrenière RG, Roy B, Griffiths LR, Rouleau GA, Ebers GC, Cader MZ, Tucker SJ (2012). "Functional analysis of missense variants in the TRESK (KCNK18) K+ channel" . Scientific Reports . 2 . article number 237. doi :10.1038/srep00237 . PMC 3266952 PMID 22355750 . Czirják G, Tóth ZE, Enyedi P (2004). "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin" . J. Biol. Chem . 279 (18): 18550–8. doi :10.1074/jbc.M312229200 PMID 14981085 . Kang D, Mariash E, Kim D (2004). "Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family" . J. Biol. Chem . 279 (27): 28063–70. doi :10.1074/jbc.M402940200 PMID 15123670 . Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science . 307 (5715): 1621–5. doi :10.1126/science.1105776 . PMID 15761153 . S2CID 39457788 . Czirják G, Vuity D, Enyedi P (2008). "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation" . J. Biol. Chem . 283 (23): 15672–80. doi :10.1074/jbc.M800712200 PMC 3259650 PMID 18397886 . Pottosin II, Bonales-Alatorre E, Valencia-Cruz G, et al. (2008). "TRESK-like potassium channels in leukemic T cells". Pflügers Arch . 456 (6): 1037–48. doi :10.1007/s00424-008-0481-x . PMID 18506476 . S2CID 3245155 . Sano Y, Inamura K, Miyake A, et al. (2003). "A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord" . J. Biol. Chem . 278 (30): 27406–12. doi :10.1074/jbc.M206810200 PMID 12754259 .
External links [ ]
Ligand-gated Voltage-gated
α2 δ-subunits
β-subunits
γ-subunits
Na+ : Sodium channel
Constitutively active
Epithelial sodium channel
Proton -gated
Amiloride-sensitive cation channel
Voltage-gated
Nav α
1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Nav β
K+ : Potassium channel
Calcium-activated Inward-rectifier Tandem pore domain Voltage-gated
Miscellaneous
Cl− :Chloride channel
Calcium-activated chloride channels
Anoctamin
Bestrophin
Chloride Channel Accessory
CFTR CLCN
CLIC
CLNS
H+ :Proton channel M+ :CNG cation channel M+ :TRP cation channel H2 O (+ solutes ):Porin Cytoplasm :Gap junction
see also disorders
