|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 301 to 364 out of 364 for Kcne2

<< First    < Previous  |  Next >    Last >>
0.049s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Publication
- | J:94338
     
First Author: NIH Mouse Knockout Inventory
Year: 2004
Journal: MGI Direct Data Submission
Title: Information obtained from the NIH Mouse Knockout Inventory
•
•
•
•
•
Publication
30973865 | J:274872
First Author: Ingham NJ
Year: 2019
Journal: PLoS Biol
Title: Mouse screen reveals multiple new genes underlying mouse and human hearing loss.
Volume: 17
Issue: 4
Pages: e3000194
•
•
•
•
•
Publication
15226823 | J:93300
First Author: Blackshaw S
Year: 2004
Journal: PLoS Biol
Title: Genomic analysis of mouse retinal development.
Volume: 2
Issue: 9
Pages: E247
•
•
•
•
•
Publication
- | J:80001
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: FANTOM2 Data Curation in Mouse Genome Informatics
•
•
•
•
•
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
•
•
•
•
•
Publication
14681479 | J:122989
First Author: Visel A
Year: 2004
Journal: Nucleic Acids Res
Title: GenePaint.org: an atlas of gene expression patterns in the mouse embryo.
Volume: 32
Issue: Database issue
Pages: D552-6
•
•
•
•
•
Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
•
•
•
•
•
Publication
- | J:155845
     
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
•
•
•
•
•
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
•
•
•
•
•
Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
•
•
•
•
•
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
•
•
•
•
•
Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
•
•
•
•
•
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
•
•
•
•
•
Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
•
•
•
•
•
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
•
•
•
•
•
Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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).
•
•
•
•
•
Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
•
•
•
•
•
Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
•
•
•
•
•
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
•
•
•
•
•
Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
•
•
•
•
•
Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
•
•
•
•
•
Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
•
•
•
•
•
Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
•
•
•
•
•
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
•
•
•
•
•
Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
•
•
•
•
•
Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
•
•
•
•
•
Publication
10219239 | J:64949
First Author: Abbott GW
Year: 1999
Journal: Cell
Title: MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia.
Volume: 97
Issue: 2
Pages: 175-87
•
•
•
•
•
Protein Domain
IPR005425 | K_chnl_volt-dep_bsu_KCNE2
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.Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). KCNE2 subunits associate with the eag-like HERG alpha subunits, which arethe pore-forming subunits of cardiac IKr channels. Channels formed solelyfrom HERG subunits display similar properties to native IKr channels;however, they differ in their gating and single channel conductance. Channels formed from both KCNE2 and HERG exhibit properties that are identical to those seen in native IKr channels. Three mutations in the KCNE2gene are associated with long QT syndrome and ventricular fibrillation. These mutations result in channels that open slower and close more rapidly,the net effect being a reduced K+ current [].
•
•
•
•
•
Allele
Kcne2<em1Smoc> | MGI:7290655
Name: potassium voltage-gated channel, Isk-related subfamily, gene 2; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
•
•
•
•
•
Protein
Q9D808
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J1J2
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
•
•
•
•
•
Strain
MGI:6429034 | C57BL/6J-Kcne2<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
•
•
•
•
•
DO Term
DOID:0110648 | long QT syndrome 6
•
•
•
•
•
Publication
32183852 | J:301905
First Author: Kong Q
Year: 2020
Journal: Mol Brain
Title: Conditional Dnmt3b deletion in hippocampal dCA1 impairs recognition memory.
Volume: 13
Issue: 1
Pages: 42
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
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
•
•
•
•
•
Publication
10493825 | J:57928
First Author: Piccini M
Year: 1999
Journal: Genomics
Title: KCNE1-like gene is deleted in AMME contiguous gene syndrome: identification and characterization of the human and mouse homologs.
Volume: 60
Issue: 3
Pages: 251-7
•
•
•
•
•
Protein
Q9QZ26
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: false
•
•
•
•
•
Protein
Q9WTW3
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
•
•
•
•
•
Protein
Q8JZQ4
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
•
•
•
•
•
Protein
A0A087WQK6
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
•
•
•
•
•
Protein
Q8C1K1
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
•
•
•
•
•
Publication
19219384 | -
First Author: McCrossan ZA
Year: 2009
Journal: J Membr Biol
Title: Regulation of the Kv2.1 potassium channel by MinK and MiRP1.
Volume: 228
Issue: 1
Pages: 1-14
•
•
•
•
•
Publication
11207363 | -
First Author: Abbott GW
Year: 2001
Journal: Cell
Title: MiRP2 forms potassium channels in skeletal muscle with Kv3.4 and is associated with periodic paralysis.
Volume: 104
Issue: 2
Pages: 217-31
•
•
•
•
•
Publication
10646604 | -
First Author: Schroeder BC
Year: 2000
Journal: Nature
Title: A constitutively open potassium channel formed by KCNQ1 and KCNE3.
Volume: 403
Issue: 6766
Pages: 196-9
•
•
•
•
•
Protein Domain
IPR000369 | K_chnl_KCNE
Type: Family
Description: Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). 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.
•
•
•
•
•
Protein Domain
IPR005424 | KCNE1
Type: Family
Description: KCNE1 (Potassium voltage-gated channel subfamily E member 1, also known as Mink) subunits associate with KCNQ1 alpha subunits to form channels that are responsible for the IkS currents that determine the duration of the action potential in cardiac muscle []. Mutations in both of the genes encoding these subunits cause an inherited disorder that increases the risk of death from cardiac arrhythmia (long QT syndrome type 1) and Jervell and Lange-Nielsen syndrome, associated with congenital deafness [].Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). 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.
•
•
•
•
•
Protein Domain
IPR005426 | K_chnl_volt-dep_bsu_KCNE3
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.Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). KCNE3 is known to associate with the pore forming subunits KCNQ1, KCNQ4,HERG and Kv3.4. KCNE3 forms complexes with Kv3.4 in skeletal muscle -KCNE3 mutations have been identified in families with skeletal muscledisorders []. In the intestine, KCNE3 associates with KCNQ1 to formchannels that are stimulated by cAMP and are thought to be involved insecretory diarrhoea and cystic fibrosis [].
•
•
•
•
•
Protein
Q9WTW2
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: false
•
•
•
•
•
Protein
P23299
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: false
•
•
•
•
•
Protein
Q545H9
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: false
•
•
•
•
•
Protein
Q545H6
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: false
•
•
•
•
•




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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom