Potassium Channels (Homo sapiens)

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Bibliography

1. Meuth SG, Kanyshkov T, Melzer N, Bittner S, Kieseier BC, Budde T, Wiendl H.; ''Altered neuronal expression of TASK1 and TASK3 potassium channels in rodent and human autoimmune CNS inflammation.''; PubMed Europe PMC Scholia
2. Fowler CE, Aryal P, Suen KF, Slesinger PA.; ''Evidence for association of GABA(B) receptors with Kir3 channels and regulators of G protein signalling (RGS4) proteins.''; PubMed Europe PMC Scholia
3. Kim J, Hoffman DA.; ''Potassium channels: newly found players in synaptic plasticity.''; PubMed Europe PMC Scholia
4. Norris AJ, Foeger NC, Nerbonne JM.; ''Neuronal voltage-gated K+ (Kv) channels function in macromolecular complexes.''; PubMed Europe PMC Scholia
5. Hill MA, Yang Y, Ella SR, Davis MJ, Braun AP.; ''Large conductance, Ca2+-activated K+ channels (BKCa) and arteriolar myogenic signaling.''; PubMed Europe PMC Scholia
6. Alesutan I, Föller M, Sopjani M, Dërmaku-Sopjani M, Zelenak C, Fröhlich H, Velic A, Fraser S, Kemp BE, Seebohm G, Völkl H, Lang F.; ''Inhibition of the heterotetrameric K+ channel KCNQ1/KCNE1 by the AMP-activated protein kinase.''; PubMed Europe PMC Scholia
7. Han J, Kang D, Kim D.; ''Functional properties of four splice variants of a human pancreatic tandem-pore K+ channel, TALK-1.''; PubMed Europe PMC Scholia
8. Cramer NP, Best TK, Stoffel M, Siarey RJ, Galdzicki Z.; ''GABAB-GIRK2-mediated signaling in Down syndrome.''; PubMed Europe PMC Scholia
9. MacKinnon R.; ''New insights into the structure and function of potassium channels.''; PubMed Europe PMC Scholia
10. Ohya S, Fujimori T, Kimura T, Yamamura H, Imaizumi Y.; ''Novel spliced variants of large-conductance Ca(2+)-activated K(+)-channel β2-subunit in human and rodent pancreas.''; PubMed Europe PMC Scholia
11. Biel M, Wahl-Schott C, Michalakis S, Zong X.; ''Hyperpolarization-activated cation channels: from genes to function.''; PubMed Europe PMC Scholia
12. Kréneisz O, Benoit JP, Bayliss DA, Mulkey DK.; ''AMP-activated protein kinase inhibits TREK channels.''; PubMed Europe PMC Scholia
13. Theilig F, Goranova I, Hirsch JR, Wieske M, Unsal S, Bachmann S, Veh RW, Derst C.; ''Cellular localization of THIK-1 (K(2P)13.1) and THIK-2 (K(2P)12.1) K channels in the mammalian kidney.''; PubMed Europe PMC Scholia
14. Fallen K, Banerjee S, Sheehan J, Addison D, Lewis LM, Meiler J, Denton JS.; ''The Kir channel immunoglobulin domain is essential for Kir1.1 (ROMK) thermodynamic stability, trafficking and gating.''; PubMed Europe PMC Scholia
15. Baruscotti M, Bottelli G, Milanesi R, DiFrancesco JC, DiFrancesco D.; ''HCN-related channelopathies.''; PubMed Europe PMC Scholia
16. Sheng JZ, Ella S, Davis MJ, Hill MA, Braun AP.; ''Openers of SKCa and IKCa channels enhance agonist-evoked endothelial nitric oxide synthesis and arteriolar vasodilation.''; PubMed Europe PMC Scholia
17. 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.; ''A dominant-negative mutation in the TRESK potassium channel is linked to familial migraine with aura.''; PubMed Europe PMC Scholia
18. Hibino H, Inanobe A, Furutani K, Murakami S, Findlay I, Kurachi Y.; ''Inwardly rectifying potassium channels: their structure, function, and physiological roles.''; PubMed Europe PMC Scholia
19. Dallas ML, Scragg JL, Wyatt CN, Ross F, Hardie DG, Evans AM, Peers C.; ''Modulation of O(2) sensitive K (+) channels by AMP-activated protein kinase.''; PubMed Europe PMC Scholia
20. Shorter K, Farjo NP, Picksley SM, Randall VA.; ''Human hair follicles contain two forms of ATP-sensitive potassium channels, only one of which is sensitive to minoxidil.''; PubMed Europe PMC Scholia
21. Shin HG, Lu Z.; ''Mechanism of the voltage sensitivity of IRK1 inward-rectifier K+ channel block by the polyamine spermine.''; PubMed Europe PMC Scholia
22. Feliciangeli S, Tardy MP, Sandoz G, Chatelain FC, Warth R, Barhanin J, Bendahhou S, Lesage F.; ''Potassium channel silencing by constitutive endocytosis and intracellular sequestration.''; PubMed Europe PMC Scholia
23. Gestreau C, Heitzmann D, Thomas J, Dubreuil V, Bandulik S, Reichold M, Bendahhou S, Pierson P, Sterner C, Peyronnet-Roux J, Benfriha C, Tegtmeier I, Ehnes H, Georgieff M, Lesage F, Brunet JF, Goridis C, Warth R, Barhanin J.; ''Task2 potassium channels set central respiratory CO2 and O2 sensitivity.''; PubMed Europe PMC Scholia
24. McKeown L, Swanton L, Robinson P, Jones OT.; ''Surface expression and distribution of voltage-gated potassium channels in neurons (Review).''; PubMed Europe PMC Scholia
25. Pongs O, Schwarz JR.; ''Ancillary subunits associated with voltage-dependent K+ channels.''; PubMed Europe PMC Scholia
26. Moroni A, Gorza L, Beltrame M, Gravante B, Vaccari T, Bianchi ME, Altomare C, Longhi R, Heurteaux C, Vitadello M, Malgaroli A, DiFrancesco D.; ''Hyperpolarization-activated cyclic nucleotide-gated channel 1 is a molecular determinant of the cardiac pacemaker current I(f).''; PubMed Europe PMC Scholia
27. Toyoda H, Saito M, Okazawa M, Hirao K, Sato H, Abe H, Takada K, Funabiki K, Takada M, Kaneko T, Kang Y.; ''Protein kinase G dynamically modulates TASK1-mediated leak K+ currents in cholinergic neurons of the basal forebrain.''; PubMed Europe PMC Scholia
28. Krenz M, Oldenburg O, Wimpee H, Cohen MV, Garlid KD, Critz SD, Downey JM, Benoit JN.; ''Opening of ATP-sensitive potassium channels causes generation of free radicals in vascular smooth muscle cells.''; PubMed Europe PMC Scholia
29. Xie K, Allen KL, Kourrich S, Colón-Saez J, Thomas MJ, Wickman K, Martemyanov KA.; ''Gbeta5 recruits R7 RGS proteins to GIRK channels to regulate the timing of neuronal inhibitory signaling.''; PubMed Europe PMC Scholia

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DataNodes

Name	Type	Database reference	Comment
3',5'-Cyclic AMP [cytosol]	Metabolite	CHEBI:17489 (ChEBI)
3',5'-Cyclic AMP	Metabolite	CHEBI:17489 (ChEBI)
ABCC8 [plasma membrane]	Protein	Q09428 (Uniprot-TrEMBL)
ABCC9 [plasma membrane]	Protein	O60706 (Uniprot-TrEMBL)
ATP sensitive K+ channels-inwardly rectifying (SUR1)	Complex	REACT_76659 (Reactome)
ATP sensitive K+ channels-inwardly rectifying (SUR2)	Complex	REACT_111451 (Reactome)
BK channel	Complex	REACT_24118 (Reactome)	BK channels (also called Maxi-K or slo1) are potassium ion channels. They are activated by changes in membrane electrical potential and increases in intracellular [Ca2+]. Opening of BK channels results in cell membrane hyperpolarization. BK channels are tetramers of dimer subunits formed by the association of a pore-forming alpha subunit, always derived from the same gene KCNMA1, and a modulatory beta subunit, dervied from one of 4 human genes KCNMB11-4. Intracellular calcium regulates the physical association between the alpha and beta subunits.
GABA B receptor G-protein beta-gamma and Kir3 channel complex	Complex	REACT_26489 (Reactome)
GABA [extracellular region]	Metabolite	CHEBI:16865 (ChEBI)
GABBR1 [plasma membrane]	Protein	Q9UBS5 (Uniprot-TrEMBL)
GABBR2 [plasma membrane]	Protein	O75899 (Uniprot-TrEMBL)
GNB1 [plasma membrane]	Protein	P62873 (Uniprot-TrEMBL)
GNB2 [plasma membrane]	Protein	P62879 (Uniprot-TrEMBL)
GNB3 [plasma membrane]	Protein	P16520 (Uniprot-TrEMBL)
GNG10 [plasma membrane]	Protein	P50151 (Uniprot-TrEMBL)
GNG12 [plasma membrane]	Protein	Q9UBI6 (Uniprot-TrEMBL)
GNG2 [plasma membrane]	Protein	P59768 (Uniprot-TrEMBL)
GNG3 [plasma membrane]	Protein	P63215 (Uniprot-TrEMBL)
GNG4 [plasma membrane]	Protein	P50150 (Uniprot-TrEMBL)
GNG5 [plasma membrane]	Protein	P63218 (Uniprot-TrEMBL)
GNG7 [plasma membrane]	Protein	O60262 (Uniprot-TrEMBL)
GNG8(2-67) [plasma membrane]	Protein	Q9UK08 (Uniprot-TrEMBL)
GNGT1 [plasma membrane]	Protein	P63211 (Uniprot-TrEMBL)
GNGT2 [plasma membrane]	Protein	O14610 (Uniprot-TrEMBL)
HCN channel bound to cAMP	Complex	REACT_76050 (Reactome)
HCN channels	Complex	REACT_76601 (Reactome)
HCN1 [plasma membrane]	Protein	O60741 (Uniprot-TrEMBL)
HCN2 [plasma membrane]	Protein	Q9UL51 (Uniprot-TrEMBL)
HCN3 [plasma membrane]	Protein	Q9P1Z3 (Uniprot-TrEMBL)
HCN4 [plasma membrane]	Protein	Q9Y3Q4 (Uniprot-TrEMBL)
K+	Metabolite	CHEBI:29103 (ChEBI)
KCNA1 [plasma membrane]	Protein	Q09470 (Uniprot-TrEMBL)
KCNA10 [plasma membrane]	Protein	Q16322 (Uniprot-TrEMBL)
KCNA2 [plasma membrane]	Protein	P16389 (Uniprot-TrEMBL)
KCNA3 [plasma membrane]	Protein	P22001 (Uniprot-TrEMBL)
KCNA4 [plasma membrane]	Protein	P22459 (Uniprot-TrEMBL)
KCNA5 [plasma membrane]	Protein	P22460 (Uniprot-TrEMBL)
KCNA6 [plasma membrane]	Protein	P17658 (Uniprot-TrEMBL)
KCNA7 [plasma membrane]	Protein	Q96RP8 (Uniprot-TrEMBL)
KCNAB1 [plasma membrane]	Protein	Q14722 (Uniprot-TrEMBL)
KCNAB2 [plasma membrane]	Protein	Q13303 (Uniprot-TrEMBL)
KCNAB3 [plasma membrane]	Protein	O43448 (Uniprot-TrEMBL)
KCNB1 [plasma membrane]	Protein	Q14721 (Uniprot-TrEMBL)
KCNB2 [plasma membrane]	Protein	Q92953 (Uniprot-TrEMBL)
KCNC1 [plasma membrane]	Protein	P48547 (Uniprot-TrEMBL)
KCNC2 [plasma membrane]	Protein	Q96PR1 (Uniprot-TrEMBL)
KCNC3 [plasma membrane]	Protein	Q14003 (Uniprot-TrEMBL)
KCNC4 [plasma membrane]	Protein	Q03721 (Uniprot-TrEMBL)
KCND1 [plasma membrane]	Protein	Q9NSA2 (Uniprot-TrEMBL)
KCND2 [plasma membrane]	Protein	Q9NZV8 (Uniprot-TrEMBL)
KCND3 [plasma membrane]	Protein	Q9UK17 (Uniprot-TrEMBL)
KCNF1 [plasma membrane]	Protein	Q9H3M0 (Uniprot-TrEMBL)
KCNG1 [plasma membrane]	Protein	Q9UIX4 (Uniprot-TrEMBL)
KCNG2 [plasma membrane]	Protein	Q9UJ96 (Uniprot-TrEMBL)
KCNG3 [plasma membrane]	Protein	Q8TAE7 (Uniprot-TrEMBL)
KCNG4 [plasma membrane]	Protein	Q8TDN1 (Uniprot-TrEMBL)
KCNH1 [plasma membrane]	Protein	O95259 (Uniprot-TrEMBL)
KCNH2 [plasma membrane]	Protein	Q12809 (Uniprot-TrEMBL)
KCNH3 [plasma membrane]	Protein	Q9ULD8 (Uniprot-TrEMBL)
KCNH4 [plasma membrane]	Protein	Q9UQ05 (Uniprot-TrEMBL)
KCNH5 [plasma membrane]	Protein	Q8NCM2 (Uniprot-TrEMBL)
KCNH6 [plasma membrane]	Protein	Q9H252 (Uniprot-TrEMBL)
KCNH7 [plasma membrane]	Protein	Q9NS40 (Uniprot-TrEMBL)
KCNH8 [plasma membrane]	Protein	Q96L42 (Uniprot-TrEMBL)
KCNJ1 [plasma membrane]	Protein	P48048 (Uniprot-TrEMBL)
KCNJ10 [plasma membrane]	Protein	P78508 (Uniprot-TrEMBL)
KCNJ11 [plasma membrane]	Protein	Q14654 (Uniprot-TrEMBL)
KCNJ12 [plasma membrane]	Protein	Q14500 (Uniprot-TrEMBL)
KCNJ14 [plasma membrane]	Protein	Q9UNX9 (Uniprot-TrEMBL)
KCNJ15 [plasma membrane]	Protein	Q99712 (Uniprot-TrEMBL)
KCNJ16 [plasma membrane]	Protein	Q9NPI9 (Uniprot-TrEMBL)
KCNJ2 [plasma membrane]	Protein	P63252 (Uniprot-TrEMBL)
KCNJ3 [plasma membrane]	Protein	P48549 (Uniprot-TrEMBL)
KCNJ4 [plasma membrane]	Protein	P48050 (Uniprot-TrEMBL)
KCNJ5 [plasma membrane]	Protein	P48544 (Uniprot-TrEMBL)
KCNJ6 [plasma membrane]	Protein	P48051 (Uniprot-TrEMBL)
KCNJ8 [plasma membrane]	Protein	Q15842 (Uniprot-TrEMBL)
KCNJ9 [plasma membrane]	Protein	Q92806 (Uniprot-TrEMBL)
KCNK1 [plasma membrane]	Protein	O00180 (Uniprot-TrEMBL)
KCNK10 [plasma membrane]	Protein	P57789 (Uniprot-TrEMBL)
KCNK13 [plasma membrane]	Protein	Q9HB14 (Uniprot-TrEMBL)
KCNK16 [plasma membrane]	Protein	Q96T55 (Uniprot-TrEMBL)
KCNK17 [plasma membrane]	Protein	Q96T54 (Uniprot-TrEMBL)
KCNK18 [plasma membrane]	Protein	Q7Z418 (Uniprot-TrEMBL)
KCNK2 [plasma membrane]	Protein	O95069 (Uniprot-TrEMBL)
KCNK3 [plasma membrane]	Protein	O14649 (Uniprot-TrEMBL)
KCNK4 [plasma membrane]	Protein	Q9NYG8 (Uniprot-TrEMBL)
KCNK6 [plasma membrane]	Protein	Q9Y257 (Uniprot-TrEMBL)
KCNK7 [plasma membrane]	Protein	Q9Y2U2 (Uniprot-TrEMBL)
KCNK9 [plasma membrane]	Protein	Q9NPC2 (Uniprot-TrEMBL)
KCNMA1 [plasma membrane]	Protein	Q12791 (Uniprot-TrEMBL)
KCNMB1 [plasma membrane]	Protein	Q16558 (Uniprot-TrEMBL)
KCNMB2 [plasma membrane]	Protein	Q9Y691 (Uniprot-TrEMBL)
KCNMB3 [plasma membrane]	Protein	Q9NPA1 (Uniprot-TrEMBL)
KCNMB4 [plasma membrane]	Protein	Q86W47 (Uniprot-TrEMBL)
KCNN1 [plasma membrane]	Protein	Q92952 (Uniprot-TrEMBL)
KCNN2 [plasma membrane]	Protein	Q9H2S1 (Uniprot-TrEMBL)
KCNN3 [plasma membrane]	Protein	Q9UGI6 (Uniprot-TrEMBL)
KCNN4	Protein	O15554 (Uniprot-TrEMBL)
KCNQ1 [plasma membrane]	Protein	P51787 (Uniprot-TrEMBL)
KCNQ2 [plasma membrane]	Protein	O43526 (Uniprot-TrEMBL)
KCNQ3 [plasma membrane]	Protein	O43525 (Uniprot-TrEMBL)
KCNQ4 [plasma membrane]	Protein	P56696 (Uniprot-TrEMBL)
KCNQ5 [plasma membrane]	Protein	Q9NR82 (Uniprot-TrEMBL)
KCNS1 [plasma membrane]	Protein	Q96KK3 (Uniprot-TrEMBL)
KCNS2 [plasma membrane]	Protein	Q9ULS6 (Uniprot-TrEMBL)
KCNS3 [plasma membrane]	Protein	Q9BQ31 (Uniprot-TrEMBL)
KCNV1 [plasma membrane]	Protein	Q6PIU1 (Uniprot-TrEMBL)
KCNV2 [plasma membrane]	Protein	Q8TDN2 (Uniprot-TrEMBL)
Octamer of Voltage gated K+ channels	Complex	REACT_76615 (Reactome)
Potassium transport channels (Kir 1.1 and Kir 4.1/5.1)	Complex	REACT_76764 (Reactome)
Small conductance Ca2+ activated potassium channel	Complex	REACT_76180 (Reactome)
TALK 1and 2	Complex	REACT_76406 (Reactome)
TASK	Complex	REACT_76290 (Reactome)
THIK1 homodimers	Complex	REACT_76759 (Reactome)
TREK homodimers	Complex	REACT_76233 (Reactome)
TRESK homodimer	Complex	REACT_76459 (Reactome)
TWIK channels	Complex	REACT_76670 (Reactome)
kir2x heteroteramer	Complex	REACT_76901 (Reactome)	Kir 2 channels form heterotetramers of any two of the four subunits.

Annotated Interactions

Source	Target	Type	Database reference	Comment
3',5'-Cyclic AMP			REACT_75751 (Reactome)
ATP sensitive K+ channels-inwardly rectifying (SUR1)		mim-catalysis	REACT_75911 (Reactome)
ATP sensitive K+ channels-inwardly rectifying (SUR2)		mim-catalysis	REACT_111144 (Reactome)
BK channel		mim-catalysis	REACT_75757 (Reactome)
GABA B receptor G-protein beta-gamma and Kir3 channel complex		mim-catalysis	REACT_25066 (Reactome)
	HCN channel bound to cAMP	Arrow	REACT_75751 (Reactome)
HCN channel bound to cAMP		mim-catalysis	REACT_75788 (Reactome)
HCN channels			REACT_75751 (Reactome)
	K+	Arrow	REACT_111144 (Reactome)
	K+	Arrow	REACT_25066 (Reactome)
	K+	Arrow	REACT_75749 (Reactome)
	K+	Arrow	REACT_75757 (Reactome)
	K+	Arrow	REACT_75758 (Reactome)
	K+	Arrow	REACT_75772 (Reactome)
	K+	Arrow	REACT_75788 (Reactome)
	K+	Arrow	REACT_75793 (Reactome)
	K+	Arrow	REACT_75806 (Reactome)
	K+	Arrow	REACT_75810 (Reactome)
	K+	Arrow	REACT_75830 (Reactome)
	K+	Arrow	REACT_75846 (Reactome)
	K+	Arrow	REACT_75857 (Reactome)
	K+	Arrow	REACT_75865 (Reactome)
	K+	Arrow	REACT_75911 (Reactome)
	K+	Arrow	REACT_75935 (Reactome)
K+			REACT_111144 (Reactome)
K+			REACT_25066 (Reactome)
K+			REACT_75749 (Reactome)
K+			REACT_75757 (Reactome)
K+			REACT_75758 (Reactome)
K+			REACT_75772 (Reactome)
K+			REACT_75788 (Reactome)
K+			REACT_75793 (Reactome)
K+			REACT_75806 (Reactome)
K+			REACT_75810 (Reactome)
K+			REACT_75830 (Reactome)
K+			REACT_75846 (Reactome)
K+			REACT_75857 (Reactome)
K+			REACT_75865 (Reactome)
K+			REACT_75911 (Reactome)
K+			REACT_75935 (Reactome)
KCNN4		mim-catalysis	REACT_75793 (Reactome)
Octamer of Voltage gated K+ channels		mim-catalysis	REACT_75857 (Reactome)
Potassium transport channels (Kir 1.1 and Kir 4.1/5.1)		mim-catalysis	REACT_75810 (Reactome)
			REACT_111144 (Reactome)	In muscle cells such as cardiac, skeletal, vascular and nonvascular smooth muscle, ATP sensitive K+ channels assemble as octamers of four Kir 6.x subunits and four low-affinity sulfonyl urea receptor 2 subunits (SUR2). The human gene encoding SUR2 gives rise to two splice variants, SUR2A and SUR2B. These channels are blocked by excess intracellular levels of ATP. When the ATP is low, ATP dissociates and the channel opens to allow K+ efflux ().
			REACT_25066 (Reactome)	Binding of G beta gamma activates the GIRK/Kir3 channels that allow the efflux of K+ out of the cell resulting in a hyperpolarized membrane potential. This negative membrane potential prevents the activation of voltage dependent Ca2+ channels.
			REACT_75749 (Reactome)	TALK is activated by increase in pH alkalinity in the extracellular fluid. Potassium is pumped out into the extracellular fluid.
			REACT_75751 (Reactome)	HCN channels require cAMP binding and hyperpolarization of membrane potential for channel opening.
			REACT_75757 (Reactome)	Increase in intracellular concentration of Ca2+ ions and membrane depolarization cooperatively activates BKca, which exhibit large unitary conductance. Ca2+ activated potassium channels. Activation leads to K+ efflux which changes the membrane potential, which leads to inactivation voltage activated Ca2+ channels. BKca are involved in regulation of smooth muscle tone, microbial killing in leukocytes and modulation of neurotransmitter release. Activation of BKca channel with increase in intracellular concentration of Ca2+ leads to efflux of K+ into the extracellular space, which contributes to hyperpolarization of the membrane potential.
			REACT_75758 (Reactome)	Activation of classical kir channels results in K+ efflux which contributes to repolarization and resetting of the membrane potential.
			REACT_75772 (Reactome)	THIK subfamily has 2 members, THIK1 and THIK 2. THIK 1 forms functional homodimers whereas THIK2 function has not been demonstrated. THIK1 channels are inhibited by halothane. THICK1 channels form K+ leak channels and are not regulated by acidity or alkalanity changes.
			REACT_75788 (Reactome)	HCN channels are activated upon hyperpolarization of membrane potential and cAMP binding leading to K+ efflux.
			REACT_75793 (Reactome)	Intermediate conductance K+ channels are restricted to non neuronal tissues like epithelia, blood cells and are activated by intracellular Ca2+ ion concentration. Activation of Ca2+ activated K+ channels with intermediate conductance leads to K+ efflux in to the extracellular space.
			REACT_75806 (Reactome)	Activation of TWIK channels results in low outward K+ currents.
			REACT_75810 (Reactome)	Homotetramers of Kir 1.1 function as inwardly rectifying potassium transport channels. Ki 1.1 are found on the apical side of the cells in the ascending limp of loop of henle and upon activation transport K+ into the extracellular space. Heterotetramers of Kir 4.1 and Ki 5.1 are found on the basolateral side of cells in the distal convoluted tube. Activation of kir 4.1 and 5.1 heterotetramers leads to efflux of K+ into the extracellular space.
			REACT_75830 (Reactome)	Small conductance Ca2+ activated potassium channels (SKca) are solely activated by intracellular Ca2+ concentration. SKca channels form functional tetramers. SKca channels control the contractility of uterus, maintian vascular tone, modulate hormone secretion, control cell volume in red blood cells and activation of microglia and lymphocytes. Actiavtion of SKca channels is triggered by increase in the intracellular Ca2+ ion concentration. Activation of Skca channels leads to relatively small K+ ion effluxes.
			REACT_75846 (Reactome)	TREK channels are activated by mechanical stretch, pH temperature and arachidonic acid which leads to efflux of K+ into the extracellular space resulting in membrane hyperpolarization.
			REACT_75857 (Reactome)	Activation of voltage gated potassium channel is triggered by membrane potential changes that is sensed by the channel assembly. Activation of voltage-gated potassium channel leads to selective outward current of K+ ions.
			REACT_75865 (Reactome)	TRESK is expressed in spinal cord and brain and is involved in K+ efflux. TRESK activation may be mediated by calcineurin.
			REACT_75911 (Reactome)	In neuroendocrine cells such as pancreatic alpha-, beta-, and delta-cells and in the brain, ATP sensitive K+ channels assemble as octamers of four Kir 6.1, 6.2 subunits and four high-affinity sulfonyl urea receptor 1 subunits (SUR1). These channels are blocked by excess intracellular levels of ATP. When the ATP is low, ATP dissociates and the channel opens to allow K+ efflux.
			REACT_75935 (Reactome)	TASK are tandem repeat K+ channels that are sensitive to extracellular pH. Activation of TASK results in efflux of K+ into the extracellular space.
Small conductance Ca2+ activated potassium channel		mim-catalysis	REACT_75830 (Reactome)
TALK 1and 2		mim-catalysis	REACT_75749 (Reactome)
TASK		mim-catalysis	REACT_75935 (Reactome)
THIK1 homodimers		mim-catalysis	REACT_75772 (Reactome)
TREK homodimers		mim-catalysis	REACT_75846 (Reactome)
TRESK homodimer		mim-catalysis	REACT_75865 (Reactome)
TWIK channels		mim-catalysis	REACT_75806 (Reactome)
kir2x heteroteramer		mim-catalysis	REACT_75758 (Reactome)