HCN2

From Wikipedia, the free encyclopedia

Hyperpolarization activated cyclic nucleotide-gated potassium channel 2

PDB rendering based on 1q3e.

Available structures: 1q3e, 1q43, 1q5o

Identifiers

Symbol(s)

HCN2; BCNG-2; BCNG2; HAC-1

External IDs

OMIM: 602781 MGI: 1298210 HomoloGene: 31022

Gene ontology
Molecular Function:	• nucleotide binding • voltage-gated potassium channel activity • sodium channel activity • cAMP binding • potassium ion binding • sodium ion binding
Cellular Component:	• membrane fraction • voltage-gated potassium channel complex • membrane • integral to membrane
Biological Process:	• cation transport • potassium ion transport • sodium ion transport • muscle contraction • cell-cell signaling

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001194 (mRNA)
NP_001185 (protein)

XM_985431 (mRNA)
XP_990525 (protein)

Location

Chr 19: 0.54 - 0.57 Mb

Chr 10: 79.12 - 79.14 Mb

Pubmed search

[1]

[2]

Hyperpolarization activated cyclic nucleotide-gated potassium channel 2, also known as HCN2, is a human gene.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Cyclic nucleotide-gated ion channel

[edit] References

^ Entrez Gene: HCN2 hyperpolarization activated cyclic nucleotide-gated potassium channel 2.

[edit] Further reading

Hofmann F, Biel M, Kaupp UB (2006). "International Union of Pharmacology. LI. Nomenclature and structure-function relationships of cyclic nucleotide-regulated channels.". Pharmacol. Rev. 57 (4): 455-62. doi:10.1124/pr.57.4.8. PMID 16382102.
Santoro B, Grant SG, Bartsch D, Kandel ER (1998). "Interactive cloning with the SH3 domain of N-src identifies a new brain specific ion channel protein, with homology to eag and cyclic nucleotide-gated channels.". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14815-20. PMID 9405696.
Santoro B, Liu DT, Yao H, et al. (1998). "Identification of a gene encoding a hyperpolarization-activated pacemaker channel of brain.". Cell 93 (5): 717-29. PMID 9630217.
Kleiderlein JJ, Nisson PE, Jessee J, et al. (1999). "CCG repeats in cDNAs from human brain.". Hum. Genet. 103 (6): 666-73. PMID 9921901.
Ludwig A, Zong X, Stieber J, et al. (1999). "Two pacemaker channels from human heart with profoundly different activation kinetics.". EMBO J. 18 (9): 2323-9. doi:10.1093/emboj/18.9.2323. PMID 10228147.
Vaccari T, Moroni A, Rocchi M, et al. (1999). "The human gene coding for HCN2, a pacemaker channel of the heart.". Biochim. Biophys. Acta 1446 (3): 419-25. PMID 10524219.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788-95. PMID 11076863.
Ulens C, Tytgat J (2001). "Functional heteromerization of HCN1 and HCN2 pacemaker channels.". J. Biol. Chem. 276 (9): 6069-72. doi:10.1074/jbc.C000738200. PMID 11133998.
Proenza C, Tran N, Angoli D, et al. (2002). "Different roles for the cyclic nucleotide binding domain and amino terminus in assembly and expression of hyperpolarization-activated, cyclic nucleotide-gated channels.". J. Biol. Chem. 277 (33): 29634-42. doi:10.1074/jbc.M200504200. PMID 12034718.
Qu J, Altomare C, Bucchi A, et al. (2003). "Functional comparison of HCN isoforms expressed in ventricular and HEK 293 cells.". Pflugers Arch. 444 (5): 597-601. doi:10.1007/s00424-002-0860-7. PMID 12194012.
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.
Sesti F, Rajan S, Gonzalez-Colaso R, et al. (2003). "Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel.". Nat. Neurosci. 6 (4): 353-61. doi:10.1038/nn1028. PMID 12640457.
Stieber J, Thomer A, Much B, et al. (2003). "Molecular basis for the different activation kinetics of the pacemaker channels HCN2 and HCN4.". J. Biol. Chem. 278 (36): 33672-80. doi:10.1074/jbc.M305318200. PMID 12813043.
Bender RA, Soleymani SV, Brewster AL, et al. (2003). "Enhanced expression of a specific hyperpolarization-activated cyclic nucleotide-gated cation channel (HCN) in surviving dentate gyrus granule cells of human and experimental epileptic hippocampus.". J. Neurosci. 23 (17): 6826-36. PMID 12890777.
Much B, Wahl-Schott C, Zong X, et al. (2003). "Role of subunit heteromerization and N-linked glycosylation in the formation of functional hyperpolarization-activated cyclic nucleotide-gated channels.". J. Biol. Chem. 278 (44): 43781-6. doi:10.1074/jbc.M306958200. PMID 12928435.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529-35. doi:10.1038/nature02399. PMID 15057824.
Michels G, Er F, Khan I, et al. (2005). "Single-channel properties support a potential contribution of hyperpolarization-activated cyclic nucleotide-gated channels and If to cardiac arrhythmias.". Circulation 111 (4): 399-404. doi:10.1161/01.CIR.0000153799.65783.3A. PMID 15687126.
Akhavan A, Atanasiu R, Noguchi T, et al. (2005). "Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization.". J. Cell. Sci. 118 (Pt 13): 2803-12. doi:10.1242/jcs.02423. PMID 15961404.
Calloe K, Elmedyb P, Olesen SP, et al. (2006). "Hypoosmotic cell swelling as a novel mechanism for modulation of cloned HCN2 channels.". Biophys. J. 89 (3): 2159-69. doi:10.1529/biophysj.105.063792. PMID 15980171.

[edit] External links

MeSH HCN2+protein,+human

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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

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HCN2

From Wikipedia, the free encyclopedia

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[edit] See also

[edit] References

[edit] Further reading

[edit] External links

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