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Search results 101 to 191 out of 191 for Kcnab1

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0.03s
Type Details Score
GXD Expression  
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3638421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 4A-dorsal
Specimen Label: 4A-dorsal
Detected: true
Specimen Num: 3
GXD Expression  
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3638421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 4A-transverse
Specimen Label: 4A-transverse
Detected: true
Specimen Num: 4
GXD Expression  
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3638421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 4A-longitudinal
Specimen Label: 4A-longitudinal
Detected: true
Specimen Num: 5
GXD Expression
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3638421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 5Bd
Note: Areas of expression include, but are not limited to, the future glans.
Specimen Label: 5Bd
Detected: true
Specimen Num: 6
GXD Expression
Probe: MGI:6696346
Assay Type: RNA in situ
Annotation Date: 2021-05-11
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3638421
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:6705002
Age: embryonic day 13.5
Image: 5Bd'
Note: Areas of expression include, but are not limited to, the future glans.
Specimen Label: 5Bd'
Detected: true
Specimen Num: 7
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
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication  
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication
First Author: Oeschger FM
Year: 2012
Journal: Cereb Cortex
Title: Gene expression analysis of the embryonic subplate.
Volume: 22
Issue: 6
Pages: 1343-59
Publication      
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
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
Publication
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
Publication      
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)
Publication      
First Author: GUDMAP Consortium
Year: 2004
Journal: www.gudmap.org
Title: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Rat to Mouse ISO GO annotation transfer
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication
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
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
Publication
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
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication      
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).
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication
First Author: Gaudet P
Year: 2011
Journal: Brief Bioinform
Title: Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium.
Volume: 12
Issue: 5
Pages: 449-62
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
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
Publication      
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
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication
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
Protein Domain
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.
Allele
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
Allele
Name: transgene insertion 1, Matthew Nystoriak
Allele Type: Transgenic
Attribute String: Inducible, Inserted expressed sequence
Protein
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 300  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 398  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
Publication
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
Strain
Attribute String: coisogenic, mutant strain, transgenic
Publication
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication
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
Publication
First Author: Miller C
Year: 2000
Journal: Genome Biol
Title: An overview of the potassium channel family.
Volume: 1
Issue: 4
Pages: REVIEWS0004
Protein
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: true
Publication
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
Publication
First Author: Desai KK
Year: 2008
Journal: Biochemistry
Title: A metabolic bypass of the triosephosphate isomerase reaction.
Volume: 47
Issue: 31
Pages: 7983-5
Publication
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
Protein Domain
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).
Protein Domain
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).
Protein Domain
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.
Protein Domain
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.
Protein
Organism: Mus musculus/domesticus
Length: 367  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 56  
Fragment?: true