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Search results 101 to 195 out of 195 for Kcnab1

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Type Details Score
GXD Expression
GXD Expression
   
Probe: MGI:5001349
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Male
Emaps: EMAPS:3151021
Stage: TS21
Assay Id: MGI:5541904
Age: embryonic day 13.5
Image: GUDMAP:11765
Specimen Label: GUDMAP:11765
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:5001349
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Male
Emaps: EMAPS:3150421
Stage: TS21
Assay Id: MGI:5541904
Age: embryonic day 13.5
Image: GUDMAP:11765
Specimen Label: GUDMAP:11765
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:5001349
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Female
Emaps: EMAPS:2896121
Stage: TS21
Assay Id: MGI:5541904
Age: embryonic day 13.5
Image: GUDMAP:11766
Specimen Label: GUDMAP:11766
Detected: false
Specimen Num: 2
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GXD Expression
GXD Expression
   
Probe: MGI:5001349
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Female
Emaps: EMAPS:2894521
Stage: TS21
Assay Id: MGI:5541904
Age: embryonic day 13.5
Image: GUDMAP:11766
Specimen Label: GUDMAP:11766
Detected: false
Specimen Num: 2
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GXD Expression
GXD Expression
   
Probe: MGI:5001349
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Female
Emaps: EMAPS:1796221
Stage: TS21
Assay Id: MGI:5541904
Age: embryonic day 13.5
Image: GUDMAP:11766
Specimen Label: GUDMAP:11766
Detected: false
Specimen Num: 2
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GXD Expression
GXD Expression
 
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3817821
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 5Bd
Specimen Label: 5Bd
Detected: true
Specimen Num: 6
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GXD Expression
GXD Expression
 
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3817821
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 5Bd'
Specimen Label: 5Bd'
Detected: true
Specimen Num: 7
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Publication
15720404 | J:106453
First Author: Connor JX
Year: 2005
Journal: Genes Brain Behav
Title: Genetic modifiers of the Kv beta2-null phenotype in mice.
Volume: 4
Issue: 2
Pages: 77-88
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Publication
27986658 | J:240115
First Author: Tur J
Year: 2017
Journal: Am J Physiol Heart Circ Physiol
Title: KvĪ²1.1 (AKR6A8) senses pyridine nucleotide changes in the mouse heart and modulates cardiac electrical activity.
Volume: 312
Issue: 3
Pages: H571-H583
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Publication
19780818 | J:157803
First Author: Bunse S
Year: 2009
Journal: FEBS J
Title: The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials.
Volume: 276
Issue: 21
Pages: 6258-70
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Publication
10536234 | J:58306
First Author: Downen M
Year: 1999
Journal: Brain Res Dev Brain Res
Title: Developmental expression of voltage-gated potassium channel beta subunits.
Volume: 117
Issue: 1
Pages: 71-80
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Publication
8824288 | J:36040
First Author: Fink M
Year: 1996
Journal: J Biol Chem
Title: A new K+ channel beta subunit to specifically enhance Kv2.2 (CDRK) expression.
Volume: 271
Issue: 42
Pages: 26341-8
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Publication
15662035 | J:106860
First Author: Aimond F
Year: 2005
Journal: Circ Res
Title: Accessory Kvbeta1 subunits differentially modulate the functional expression of voltage-gated K+ channels in mouse ventricular myocytes.
Volume: 96
Issue: 4
Pages: 451-8
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Publication
34368133 | J:313609
 
First Author: DĆ­az Del Moral S
Year: 2021
Journal: Front Cell Dev Biol
Title: Deletion of the Wilms' Tumor Suppressor Gene in the Cardiac Troponin-T Lineage Reveals Novel Functions of WT1 in Heart Development.
Volume: 9
Pages: 683861
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Publication
25707359 | J:230557
First Author: Chen N
Year: 2015
Journal: Biochim Biophys Acta
Title: Interaction proteomics of canonical Caspr2 (CNTNAP2) reveals the presence of two Caspr2 isoforms with overlapping interactomes.
Volume: 1854
Issue: 7
Pages: 827-33
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Publication
37869988 | J:348859
   
First Author: Lee Y
Year: 2023
Journal: Elife
Title: Transcriptional control of motor pool formation and motor circuit connectivity by the LIM-HD protein Isl2.
Volume: 12
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Publication
10767319 | J:61779
First Author: Tarantino LM
Year: 2000
Journal: Hum Mol Genet
Title: Dissection of behavior and psychiatric disorders using the mouse as a model.
Volume: 9
Issue: 6
Pages: 953-65
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Publication
20510229 | J:165759
First Author: Chiu HS
Year: 2010
Journal: Dev Biol
Title: Comparative gene expression analysis of genital tubercle development reveals a putative appendicular Wnt7 network for the epidermal differentiation.
Volume: 344
Issue: 2
Pages: 1071-87
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Publication
25979088 | J:242531
First Author: Bedogni F
Year: 2016
Journal: Cereb Cortex
Title: Defects During Mecp2 Null Embryonic Cortex Development Precede the Onset of Overt Neurological Symptoms.
Volume: 26
Issue: 6
Pages: 2517-2529
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Publication
16985003 | J:119550
First Author: Harrell MD
Year: 2007
Journal: Physiol Genomics
Title: Large-scale analysis of ion channel gene expression in the mouse heart during perinatal development.
Volume: 28
Issue: 3
Pages: 273-83
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Publication
21862448 | J:198109
First Author: Oeschger FM
Year: 2012
Journal: Cereb Cortex
Title: Gene expression analysis of the embryonic subplate.
Volume: 22
Issue: 6
Pages: 1343-59
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Publication
- | J:238766
     
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
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Publication
- | J:342608
       
First Author: GO Central curators, GOA curators, Rhea curators
Year: 2020
Title: Automatic Gene Ontology annotation based on Rhea mapping
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Publication
- | J:94790
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
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Publication
- | J:346132
       
First Author: The Gene Ontology Consortium
Year: 2016
Title: Automatic assignment of GO terms using logical inference, based on on inter-ontology links
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Publication
24952961 | J:215487
First Author: Thompson CL
Year: 2014
Journal: Neuron
Title: A high-resolution spatiotemporal atlas of gene expression of the developing mouse brain.
Volume: 83
Issue: 2
Pages: 309-323
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Publication
- | J:171409
     
First Author: GUDMAP Consortium
Year: 2004
Journal: www.gudmap.org
Title: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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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
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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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
- | 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: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:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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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: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: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: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:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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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: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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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: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
10399921 | -
First Author: Gulbis JM
Year: 1999
Journal: Cell
Title: Structure of a voltage-dependent K+ channel beta subunit.
Volume: 97
Issue: 7
Pages: 943-52
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Protein Domain
IPR005400 | K_chnl_volt-dep_bsu_KCNAB1
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.The KCNAB family (also known as the Kvbeta family) of voltage-dependent potassium channel beta subunits form complexes with the alpha subunits which can modify the properties of the channel. Four of these soluble beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions. These subunits belong to the family of are NADPH-dependent aldo-keto reductases, and bind NADPH-cofactors in their active sites. Changes in the oxidoreductase activity appear to markedly influence the gating mode of Kv channels, since mutations to the catalytic residues in the active site lessen the inactivating activity of KCNAB []. The KCNAB family is further divided into 3 subfamilies: KCNAB1 (Kvbeta1), KCNAB2 (Kvbeta2) and KCNAB3 (Kvbeta3).KCNAB1 associates with Kv1.4 and Kv1.5 alpha subunits and appears to have an N-terminal sequence that is similar to the Kv1 channel inactivation gate.Thus, when KCNAB1 subunits associate, their N-termini appear to be able to substitute for alpha subunit inactivation gates []. Three isoforms of KCNAB1 exist, which are produced by alternative splicing of the N-terminal90 amino acids. KCNAB1 channels are expressed in brain (caudate nucleus,hippocampus, amygdala, subthalamic nucleus and thalamus) and heart.
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Allele
Kcnab1<em1Smoc> | MGI:7290649
Name: potassium voltage-gated channel, shaker-related subfamily, beta member 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Strain
MGI:6429031 | C57BL/6JSmoc-Kcnab1<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Allele
Tg(tetO-Kcnab1)1Nyst | MGI:7408233
Name: transgene insertion 1, Matthew Nystoriak
Allele Type: Transgenic
Attribute String: Inducible, Inserted expressed sequence
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Protein
P63143
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
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Protein
Q3U6C5
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
E0CXZ9
Organism: Mus musculus/domesticus
Length: 300  
Fragment?: false
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Protein
A0A571BF54
Organism: Mus musculus/domesticus
Length: 398  
Fragment?: false
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Protein
Q9D5E9
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
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Protein
Q8CD65
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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Protein
A0A5F8MPK0
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
A0A571BEM7
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
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Protein
A0A5F8MPA4
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
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Publication
11294861 | -
First Author: BƤhring R
Year: 2001
Journal: J Biol Chem
Title: Coupling of voltage-dependent potassium channel inactivation and oxidoreductase active site of Kvbeta subunits.
Volume: 276
Issue: 25
Pages: 22923-9
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Strain
MGI:7408235 | FVB/N-Tg(tetO-Kcnab1)1Nyst/J
Attribute String: coisogenic, mutant strain, transgenic
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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: StĆ¼hmer 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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Protein
E0CYS2
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: true
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Publication
12583903 | -
First Author: Grant AW
Year: 2003
Journal: FEMS Microbiol Lett
Title: A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity.
Volume: 218
Issue: 1
Pages: 93-9
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Publication
18620424 | -
First Author: Desai KK
Year: 2008
Journal: Biochemistry
Title: A metabolic bypass of the triosephosphate isomerase reaction.
Volume: 47
Issue: 31
Pages: 7983-5
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Publication
9857044 | J:51601
First Author: Leicher T
Year: 1998
Journal: J Biol Chem
Title: Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium channel.
Volume: 273
Issue: 52
Pages: 35095-101
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Protein Domain
IPR005399 | K_chnl_volt-dep_bsu_KCNAB-rel
Type: Family
Description: This entry consists of the voltage-dependent potassium channel beta subunit KCNAB and related proteins. The bacterial proteins in this entry lack apparent alpha subunit partners and predicted to function as soluble aldo/keto reductase enzymes [, ].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.The KCNAB family (also known as the Kvbeta family) of voltage-dependent potassium channel beta subunits form complexes with the alpha subunits which can modify the properties of the channel. Four of these soluble beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions. These subunits belong to the family of are NADPH-dependent aldo-keto reductases, and bind NADPH-cofactors in their active sites. Changes in the oxidoreductase activity appear to markedly influence the gating mode of Kv channels, since mutations to the catalytic residues in the active site lessen the inactivating activity of KCNAB []. The KCNAB family is further divided into 3 subfamilies: KCNAB1 (Kvbeta1), KCNAB2 (Kvbeta2) and KCNAB3 (Kvbeta3).
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Protein Domain
IPR005983 | K_chnl_volt-dep_bsu_KCNAB
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.The KCNAB family (also known as the Kvbeta family) of voltage-dependent potassium channel beta subunits form complexes with the alpha subunits which can modify the properties of the channel. Four of these soluble beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions. These subunits belong to the family of are NADPH-dependent aldo-keto reductases, and bind NADPH-cofactors in their active sites. Changes in the oxidoreductase activity appear to markedly influence the gating mode of Kv channels, since mutations to the catalytic residues in the active site lessen the inactivating activity of KCNAB []. The KCNAB family is further divided into 3 subfamilies: KCNAB1 (Kvbeta1), KCNAB2 (Kvbeta2) and KCNAB3 (Kvbeta3).
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Protein Domain
IPR005402 | K_chnl_volt-dep_bsu_KCNAB3
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. Thefunctional 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.The KCNAB family (also known as the Kvbeta family) of voltage-dependent potassium channel beta subunits form complexes with the alpha subunits which can modify the properties of the channel. Four of these soluble beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions. These subunits belong to the family of are NADPH-dependent aldo-keto reductases, and bind NADPH-cofactors in their active sites. Changes in the oxidoreductase activity appear to markedly influence the gating mode of Kv channels, since mutations to the catalytic residues in the active site lessen the inactivating activity of KCNAB []. The KCNAB family is further divided into 3 subfamilies: KCNAB1 (Kvbeta1), KCNAB2 (Kvbeta2) and KCNAB3 (Kvbeta3).KCNAB3 associates with Kv1.5 alpha subunits, resulting in a much faster inactivation than is observed in kv1.5 channels formed from alpha subunitsalone []. KCNAB3 channels are expressed specifically in the brain, with most prominent expression in the cerebellum. Weaker expression is observed in the cortex, occipital lobe, frontal lobe and temporal lobe.
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Protein Domain
IPR005401 | K_chnl_volt-dep_bsu_KCNAB2
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.The KCNAB family (also known as the Kvbeta family) of voltage-dependent potassium channel beta subunits form complexes with the alpha subunits which can modify the properties of the channel. Four of these soluble beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions. These subunits belong to the family of are NADPH-dependent aldo-keto reductases, and bind NADPH-cofactors in their active sites. Changes in the oxidoreductase activity appear to markedly influence the gating mode of Kv channels, since mutations to the catalytic residues in the active site lessen the inactivating activity of KCNAB []. The KCNAB family is further divided into 3 subfamilies: KCNAB1 (Kvbeta1), KCNAB2 (Kvbeta2) and KCNAB3 (Kvbeta3).KCNAB2 associates with Kv1.4 alpha subunits; however, association has onlyvery modest effects on the gating of this channel []. Two isoforms of KCNAB2exist, which are produced by alternative splicing of amino acids 26-39.
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Protein
P62482
Organism: Mus musculus/domesticus
Length: 367  
Fragment?: false
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Protein
P97382
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
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Protein
Q3UPV6
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
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Protein
Q3U7L1
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
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Protein
Q8C439
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
A0A571BGH0
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
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Protein
Q3U0B0
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: true
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Protein
Q8BQX9
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q8C7S9
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q8VD73
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
E0CXI4
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
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Protein
A0A571BFX6
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Protein
A0A571BE49
Organism: Mus musculus/domesticus
Length: 56  
Fragment?: true
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