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Search results 201 to 277 out of 277 for Kcnq2

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Type Details Score
Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Allele
Kcnq2<tm1Hsa> | MGI:2386963
Name: potassium voltage-gated channel, subfamily Q, member 2; targeted mutation 1, Hitoshi Sasai
Allele Type: Targeted
Attribute String: Null/knockout
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Protein Domain
IPR003947 | K_chnl_volt-dep_KCNQ2
Type: Family
Description: Potassium channels are the most diverse group of the ion channel family [, ]. Theyare important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers []. In eukaryotic cells, K+channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K+selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK) []. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.KCNQ channels (also known as KQT-like channels) differ from other voltage-gated 6 TM helix channels, chiefly in that they possess no tetramerisation domain. Consequently, they rely on interaction with accessory subunits, or form heterotetramers with other members of the family []. Currently, 5 members of the KCNQ family are known. These have been found to be widely distributed within the body, having been shown to be expressed in the heart, brain, pancreas, lung, placenta and ear. They were initially cloned as a result of a search for proteins involved in cardiac arhythmia. Subsequently, mutations in other KCNQ family members have been shown to be responsible for some forms of hereditary deafness []and benign familial neonatal epilepsy [].The KCNQ2 channel subunit is thought to form active channels by hetero- tetramerisation with KCNQ3, although some K+ channel activity does results from the expression of KCNQ2 alone []. Channel function is modulated by phosphorylation, since experiments have demonstrated that an increase in intracellular cAMP concentration can enhance channel activity. Frameshift mutations in both KCNQ2 and KCNQ3 are associated with benign familial neonatal epilepsy [], a disorder where an infant begins to suffer convulsions, within the first three days of life. These symptoms usually disappear after approximately three months, but affected individuals have a higher than average chance of subsequently developing epilepsy (10-15%), in later life [].
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Allele
Kcnq2<em1Smoc> | MGI:7290681
Name: potassium voltage-gated channel, subfamily Q, member 2; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Publication
9872318 | -
First Author: Schroeder BC
Year: 1998
Journal: Nature
Title: Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy.
Volume: 396
Issue: 6712
Pages: 687-90
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Publication
16735477 | -
First Author: Chung HJ
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Polarized axonal surface expression of neuronal KCNQ channels is mediated by multiple signals in the KCNQ2 and KCNQ3 C-terminal domains.
Volume: 103
Issue: 23
Pages: 8870-5
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Strain
MGI:6770879 | C57BL/6-Kcnq2<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Protein
A0A0G2JGA6
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: true
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Allele
Kcnq2<tm1.1Lvi> | MGI:6488172
Name: potassium voltage-gated channel, subfamily Q, member 2; targeted mutation 1.1, Laurent Villard
Allele Type: Targeted
Attribute String: Not Specified
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Protein
F6UC55
Organism: Mus musculus/domesticus
Length: 795  
Fragment?: true
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Protein
B7ZBV9
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein
A0A0G2JFQ2
Organism: Mus musculus/domesticus
Length: 842  
Fragment?: false
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Protein
Q3UY10
Organism: Mus musculus/domesticus
Length: 726  
Fragment?: true
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Protein
B7ZBV3
Organism: Mus musculus/domesticus
Length: 726  
Fragment?: true
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Protein
B7ZBW1
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
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Protein
B7ZBW2
Organism: Mus musculus/domesticus
Length: 839  
Fragment?: false
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Protein
Q9Z351
Organism: Mus musculus/domesticus
Length: 759  
Fragment?: false
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Protein
B7ZBV7
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: false
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Protein
B7ZBV5
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Protein
B7ZBV6
Organism: Mus musculus/domesticus
Length: 754  
Fragment?: false
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Protein
B7ZBV8
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: false
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Protein
B7ZBV4
Organism: Mus musculus/domesticus
Length: 759  
Fragment?: false
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Genotype
Genotype
Symbol: Kcnq2/Kcnq2<+>
Background: 129-Kcnq2/Lvi
Zygosity: ht
Has Mutant Allele: true
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DO Term
DOID:0080462 | developmental and epileptic encephalopathy 7
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Publication
10838601 | -
First Author: Sanguinetti MC
Year: 2000
Journal: Trends Pharmacol Sci
Title: Maximal function of minimal K+ channel subunits.
Volume: 21
Issue: 6
Pages: 199-201
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Publication
8528244 | -
First Author: Wang Q
Year: 1996
Journal: Nat Genet
Title: Positional cloning of a novel potassium channel gene: KVLQT1 mutations cause cardiac arrhythmias.
Volume: 12
Issue: 1
Pages: 17-23
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Publication
9430594 | -
First Author: Biervert C
Year: 1998
Journal: Science
Title: A potassium channel mutation in neonatal human epilepsy.
Volume: 279
Issue: 5349
Pages: 403-6
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Allele
Tg(Kcnq2-EGFP)FW221Gsat | MGI:4847176
Name: transgene insertion FW221, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
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Strain
MGI:5003686 | STOCK Tg(Kcnq2-EGFP)FW221Gsat/Mmucd
Attribute String: mutant stock, transgenic
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Publication
12716895 | -
First Author: Lemaillet G
Year: 2003
Journal: J Biol Chem
Title: Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits.
Volume: 278
Issue: 30
Pages: 27333-9
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Publication
17311847 | -
First Author: Rasmussen HB
Year: 2007
Journal: J Cell Sci
Title: Requirement of subunit co-assembly and ankyrin-G for M-channel localization at the axon initial segment.
Volume: 120
Issue: Pt 6
Pages: 953-63
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Publication
19112491 | -
First Author: Hill AS
Year: 2008
Journal: PLoS Genet
Title: Ion channel clustering at the axon initial segment and node of Ranvier evolved sequentially in early chordates.
Volume: 4
Issue: 12
Pages: e1000317
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Protein Domain
IPR020969 | Ankyrin-G_BS
Type: Binding_site
Description: Interactions with ankyrin-G are crucial to the localisation of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localise sodium channels to a variety of 'excitable' membrane domains both inside and outside of the nervous system []. This motif has also been identified in the potassium channel 6TM proteins KCNQ2 and KCNQ3 []that correspond to the M channels that exert a crucial influence over neuronal excitability. KCNQ2/KCNQ3 channels are preferentially localised to the surface of axons both at the axonal initial segment and more distally, and this axonal initial segment targeting of surface KCNQ channels is mediated by these ankyrin-G binding motifs of KCNQ2 and KCNQ3 []. KCNQ3 is a major determinant of M channel localisation to the AIS, rather than KCNQ2 []. Phylogenetic analysis reveals that anchor motifs evolved sequentially in chordates (NaV channel) and jawed vertebrates (KCNQ2/3) [].
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Publication
29145442 | J:250373
First Author: Whitmire LE
Year: 2017
Journal: PLoS One
Title: Downregulation of KCNMB4 expression and changes in BK channel subtype in hippocampal granule neurons following seizure activity.
Volume: 12
Issue: 11
Pages: e0188064
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Publication
25649132 | J:221364
 
First Author: Fidzinski P
Year: 2015
Journal: Nat Commun
Title: KCNQ5 K(+) channels control hippocampal synaptic inhibition and fast network oscillations.
Volume: 6
Pages: 6254
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Publication
29861105 | J:269189
First Author: Wang CC
Year: 2018
Journal: Am J Hum Genet
Title: βIV Spectrinopathies Cause Profound Intellectual Disability, Congenital Hypotonia, and Motor Axonal Neuropathy.
Volume: 102
Issue: 6
Pages: 1158-1168
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Publication
35201886 | J:323820
First Author: Li SB
Year: 2022
Journal: Science
Title: Hyperexcitable arousal circuits drive sleep instability during aging.
Volume: 375
Issue: 6583
Pages: eabh3021
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Publication
27466704 | J:235497
   
First Author: Kim HJ
Year: 2016
Journal: Elife
Title: Protein arginine methylation facilitates KCNQ channel-PIP2 interaction leading to seizure suppression.
Volume: 5
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Publication
20534576 | J:195336
First Author: Tzingounis AV
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: The KCNQ5 potassium channel mediates a component of the afterhyperpolarization current in mouse hippocampus.
Volume: 107
Issue: 22
Pages: 10232-7
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Publication
33766732 | J:342653
 
First Author: Stincic TL
Year: 2021
Journal: Mol Metab
Title: CRISPR knockdown of Kcnq3 attenuates the M-current and increases excitability of NPY/AgRP neurons to alter energy balance.
Volume: 49
Pages: 101218
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Publication
28283543 | J:252684
First Author: Neverisky DL
Year: 2017
Journal: FASEB J
Title: KCNQ-SMIT complex formation facilitates ion channel-solute transporter cross talk.
Volume: 31
Issue: 7
Pages: 2828-2838
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Publication
21849543 | J:254146
First Author: Roepke TA
Year: 2011
Journal: J Neurosci
Title: Fasting and 17β-estradiol differentially modulate the M-current in neuropeptide Y neurons.
Volume: 31
Issue: 33
Pages: 11825-35
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Publication
21562284 | J:244567
First Author: Zhang J
Year: 2011
Journal: J Neurosci
Title: AKAP79/150 signal complexes in G-protein modulation of neuronal ion channels.
Volume: 31
Issue: 19
Pages: 7199-211
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Publication
10575255 | J:59642
First Author: Rho JM
Year: 1999
Journal: Dev Neurosci
Title: Developmental seizure susceptibility of kv1.1 potassium channel knockout mice.
Volume: 21
Issue: 3-5
Pages: 320-7
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Publication
11038262 | J:64846
First Author: Jow F
Year: 2000
Journal: Brain Res Mol Brain Res
Title: Cloning and functional expression of rKCNQ2 K(+) channel from rat brain.
Volume: 80
Issue: 2
Pages: 269-78
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Publication
23849776 | J:206687
First Author: Jiang YH
Year: 2013
Journal: Am J Hum Genet
Title: Detection of clinically relevant genetic variants in autism spectrum disorder by whole-genome sequencing.
Volume: 93
Issue: 2
Pages: 249-63
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Publication
2451788 | J:9129
First Author: Tempel BL
Year: 1988
Journal: Nature
Title: Cloning of a probable potassium channel gene from mouse brain.
Volume: 332
Issue: 6167
Pages: 837-9
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Publication
1772658 | -
First Author: Perney TM
Year: 1991
Journal: Curr Opin Cell Biol
Title: The molecular biology of K+ channels.
Volume: 3
Issue: 4
Pages: 663-70
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Publication
1879548 | -
First Author: Luneau C
Year: 1991
Journal: FEBS Lett
Title: Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.
Volume: 288
Issue: 1-2
Pages: 163-7
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Publication
1373731 | J:931
First Author: Attali B
Year: 1992
Journal: J Biol Chem
Title: Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.
Volume: 267
Issue: 12
Pages: 8650-7
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Publication
2448635 | -
First Author: Schwarz TL
Year: 1988
Journal: Nature
Title: Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila.
Volume: 331
Issue: 6152
Pages: 137-42
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Publication
2555158 | -
First Author: Stühmer W
Year: 1989
Journal: EMBO J
Title: Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain.
Volume: 8
Issue: 11
Pages: 3235-44
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Publication
11178249 | -
First Author: Miller C
Year: 2000
Journal: Genome Biol
Title: An overview of the potassium channel family.
Volume: 1
Issue: 4
Pages: REVIEWS0004
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Publication
29265344 | J:273036
First Author: Vanhoof-Villalba SL
Year: 2018
Journal: Epilepsia
Title: Pharmacogenetics of KCNQ channel activation in 2 potassium channelopathy mouse models of epilepsy.
Volume: 59
Issue: 2
Pages: 358-368
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Publication
21267074 | J:169461
First Author: Cifuentes-Diaz C
Year: 2011
Journal: PLoS One
Title: Nodes of ranvier and paranodes in chronic acquired neuropathies.
Volume: 6
Issue: 1
Pages: e14533
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Protein
Q8K3F6
Organism: Mus musculus/domesticus
Length: 873  
Fragment?: false
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Protein
Q14B66
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein Domain
IPR003948 | K_chnl_volt-dep_KCNQ3
Type: Family
Description: Potassium channels are the most diverse group of the ion channel family [, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers []. In eukaryotic cells, K+channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K+selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK) []. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.KCNQ channels (also known as KQT-like channels) differ from other voltage-gated 6 TM helix channels, chiefly in that they possess no tetramerisation domain. Consequently, they rely on interaction with accessory subunits, or form heterotetramers with other members of the family []. Currently, 5 members of the KCNQ family are known. These have been found to be widely distributed within the body, having been shown to be expressed in the heart, brain, pancreas, lung, placenta and ear. They were initially cloned as a result of a search for proteins involved in cardiac arhythmia. Subsequently, mutations in other KCNQ family members have been shown to be responsible for some forms of hereditary deafness []and benign familial neonatal epilepsy [].The KCNQ3 channel subunit is thought to form active channels by hetero- tetramerisation with KCNQ2, although some K+ channel activity does result from the expression of KCNQ3 alone []. Channel function is modulated by phosphorylation; experiments have demonstrated that an increase in intracellular cAMP concentration can enhance channel activity. Frameshift mutations in both KCNQ2 and KCNQ3 are associated with benign familial neonatal epilepsy [], a disorder in which infants suffer convulsions within the first 3 days of life. These symptoms usually disappear after about 3 months, but affected individuals have a higher than average chance of subsequently developing epilepsy (10-15%) in later life [].
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Publication
- | J:100256
     
First Author: The Gene Expression Nervous System Atlas (GENSAT) Project, The Rockefeller University (New York, NY)
Year: 2005
Journal: Database Download
Title: MGI download of GENSAT transgene data
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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