KCNJ12

From Wikipedia, the free encyclopedia

Potassium inwardly-rectifying channel, subfamily J, member 12

Identifiers

KCNJ12; IRK2; KCNJN1; Kir2.2; Kir2.2v; hIRK; hIRK1; hkir2.2x; kcnj12x

External IDs

OMIM: 602323 MGI: 108495 HomoloGene: 7793

Gene ontology
Molecular Function:	• inward rectifier potassium channel activity • voltage-gated ion channel activity • ion channel inhibitor activity • potassium channel regulator activity • potassium ion binding
Cellular Component:	• membrane fraction • integral to plasma membrane • membrane • integral to membrane
Biological Process:	• ion transport • potassium ion transport • muscle contraction • regulation of heart contraction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

XM_939575 (mRNA)
XP_944668 (protein)

NM_010603 (mRNA)
NP_034733 (protein)

Location

Chr 17: 21.22 - 21.26 Mb

Chr 11: 60.84 - 60.89 Mb

Pubmed search

[1]

[2]

Potassium inwardly-rectifying channel, subfamily J, member 12, also known as KCNJ12 or K_ir2.2, is a human gene.^[1]

This gene encodes an inwardly rectifying K+ channel which may be blocked by divalent cations. This protein is thought to be one of multiple inwardly rectifying channels which contribute to the cardiac inward rectifier current (IK1). The gene is located within the Smith-Magenis syndrome region on chromosome 17.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Inward-rectifier potassium ion channel

[edit] References

^ ^a ^b Entrez Gene: KCNJ12 potassium inwardly-rectifying channel, subfamily J, member 12.

[edit] 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.
Mukherjee A, Varma SK, Natarajan K (1972). "Ankle joint instability in poliomyelitis.". Indian journal of pediatrics 39 (289): 37–8. PMID 5024025.
Wible BA, De Biasi M, Majumder K, et al. (1995). "Cloning and functional expression of an inwardly rectifying K+ channel from human atrium.". Circ. Res. 76 (3): 343–50. PMID 7859381.
Namba N, Inagaki N, Gonoi T, et al. (1996). "Kir2.2v: a possible negative regulator of the inwardly rectifying K+ channel Kir2.2.". FEBS Lett. 386 (2-3): 211–4. PMID 8647284.
Hugnot JP, Pedeutour F, Le Calvez C, et al. (1997). "The human inward rectifying K+ channel Kir 2.2 (KCNJ12) gene: gene structure, assignment to chromosome 17p11.1, and identification of a simple tandem repeat polymorphism.". Genomics 39 (1): 113–6. doi:10.1006/geno.1996.4450. PMID 9027495.
Gallagher PG, Forget BG (1998). "An alternate promoter directs expression of a truncated, muscle-specific isoform of the human ankyrin 1 gene.". J. Biol. Chem. 273 (3): 1339–48. PMID 9430667.
Namba N, Mori R, Tanaka H, et al. (1998). "The inwardly rectifying potassium channel subunit Kir2.2v (KCNJN1) maps to 17p11.2-->p11.1.". Cytogenet. Cell Genet. 79 (1-2): 85–7. PMID 9533018.
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.
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.
Chen L, Kawano T, Bajic S, et al. (2002). "A glutamate residue at the C terminus regulates activity of inward rectifier K+ channels: implication for Andersen's syndrome.". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 8430–5. doi:10.1073/pnas.122682899. PMID 12034888.
Kaibara M, Ishihara K, Doi Y, et al. (2002). "Identification of human Kir2.2 (KCNJ12) gene encoding functional inward rectifier potassium channel in both mammalian cells and Xenopus oocytes.". FEBS Lett. 531 (2): 250–4. PMID 12417321.
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.
Karkanis T, Li S, Pickering JG, Sims SM (2003). "Plasticity of KIR channels in human smooth muscle cells from internal thoracic artery.". Am. J. Physiol. Heart Circ. Physiol. 284 (6): H2325–34. doi:10.1152/ajpheart.00559.2002. PMID 12598232.
Stonehouse AH, Grubb BD, Pringle JH, et al. (2003). "Nuclear immunostaining in rat neuronal cells using two anti-Kir2.2 ion channel polyclonal antibodies.". J. Mol. Neurosci. 20 (2): 189–94. PMID 12794312.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Fang Y, Schram G, Romanenko VG, et al. (2005). "Functional expression of Kir2.x in human aortic endothelial cells: the dominant role of Kir2.2.". Am. J. Physiol., Cell Physiol. 289 (5): C1134–44. doi:10.1152/ajpcell.00077.2005. PMID 15958527.
Kiesecker C, Zitron E, Scherer D, et al. (2006). "Regulation of cardiac inwardly rectifying potassium current IK1 and Kir2.x channels by endothelin-1.". J. Mol. Med. 84 (1): 46–56. doi:10.1007/s00109-005-0707-8. PMID 16258766.

[edit] External links

MeSH Kir2.2+channel

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v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel