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0KCNH4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameKCNH4
DescriptionPotassium voltage-gated channel subfamily h member 4 (voltage-gated potassium channel subunit kv12.3) (ether-a-go-go-like potassium channel 1) (elk channel 1) (elk1) (brain-specific eag-like channel 2) (bec2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008076 voltage-gated potassium channel complex (TAS)
0005249 voltage-gated potassium channel activity (TAS)
0006813 potassium ion transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Potassium channels are the most diverse group of the ion channel family. They are important in shaping the action potential.nd in neuronal excitability and plasticity . The potassium channel family iscomposed of several functionally distinct isoforms.hich can be broadlyseparated into 2 groups : the practically non-inactivating delayed group and the rapidly inactivating transient group.These are all highly similar proteins.ith only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism.hannel 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.ogether with intracellular kinases; and others are regulated by GTP-binding proteins orother second messengers . In eukaryotic cells.+ channelsare involved in neural signalling and generation of the cardiac rhythm.ct 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.hey play a role in themaintenance of ionic homeostasis . All K+ channels discovered so far possess a core of alpha subunits.ach comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG).hich hasbeen termed the K+ selectivity sequence.In families that contain one P-domain.our subunits assemble to form a selective pathway for K+ across the membrane.However.t 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.K and SK). The 2TM domain family comprises inward-rectifying K+ channels. In addition.here are K+ channel alpha-subunits that possess two P-domains. These are usually highly regulated K+ selective leak channels.The first EAG K+ channel was identified in Drosophila melanogaster.ollowing a screen for mutations giving rise to behavioural abnormalities. Disruption of the Eag gene caused an ether-induced.eg-shaking behaviour. Subsequent studies have revealed a conserved multi-gene family of EAG-like K+ channels.hich are present in human and many other species. Based on the varying functional properties of the channels.he family has been divided into 3 subfamilies: EAG.LK and ERG. Interestingly.aenorhabditis elegans appears to lack the ELK type .
  IPR003938:EAG/ELK/ERG potassium channel
InterPro domains unassigned to SynO:
This group of proteins is found in sodium.otassium.nd calcium ion channels proteins. The proteins have 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some Na channels proteins the domain is repeated four times.hereas in others (e.g. K channels) the protein forms a tetramer in the membrane. A bacterial structure of the protein is known for the last two helices but is not included in the Pfam family due to it lacking the first four helices.
  IPR005821:Ion transport
Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues . The best studied of these proteins is the prokaryotic catabolite gene activator (alsoknown as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three alpha-helices anda distinctive eight-stranded.ntiparallel beta-barrel structure. There are six invariant amino acids in this domain.hree of which are glycine residues that are thought to be essential for maintenance of the structural integrity ofthe beta-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclicnucleotide-binding domain. The cAPKs are composed of two different subunits. catalytic chain and a regulatory chain.hich contains both copies of the domain. The cGPKs are single chain enzymes that include the two copies of the domainin their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this domain. Two suchcations channels have been fully characterized.ne is found in rod cells where it plays a role in visual signaltransduction.
  IPR000595:Cyclic nucleotide-binding
The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs . The PAS fold appears in archaea.ubacteria and eukarya. The PAS domain contains a sensory box.r S-box domain that occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL .AD in the redox potential sensor NifL .nd a 4-hydroxycinnamyl chromophore in photoactive yellow protein . Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. This domain has been found in the gene product of the madA gene of the filamentous zygomycete fungus Phycomyces blakesleeanus. It has been shown that MadA encodes a blue-light photoreceptor for phototropism and other light responses. The gene is involved in the phototropic responses associated with sporangiophore growth; they exhibit phototropism by bending toward near-UV and blue wavelengths and away from far-UV wavelengths in a manner that is physiologically similar to plant phototropic responses .
  IPR013655:PAS fold-3
PAC motifs occur C-terminal to a subset of all known PAS motifs (see ). It is proposed to contribute to the PAS domain fold .
  IPR001610:PAC motif
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
  IPR000014:PAS
Potassium channels are the most diverse group of the ion channel family. They are important in shaping the action potential.nd in neuronal excitability and plasticity . The potassium channel family iscomposed of several functionally distinct isoforms.hich can be broadlyseparated into 2 groups : the practically non-inactivating delayed group and the rapidly inactivating transient group.These are all highly similar proteins.ith only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism.hannel 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.ogether with intracellular kinases; and others are regulated by GTP-binding proteins orother second messengers . In eukaryotic cells.+ channelsare involved in neural signalling and generation of the cardiac rhythm.ct 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.hey play a role in themaintenance of ionic homeostasis . All K+ channels discovered so far possess a core of alpha subunits.ach comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG).hich hasbeen termed the K+ selectivity sequence.In families that contain one P-domain.our subunits assemble to form a selective pathway for K+ across the membrane.However.t 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.K and SK). The 2TM domain family comprises inward-rectifying K+ channels. In addition.here are K+ channel alpha-subunits that possess two P-domains. These are usually highly regulated K+ selective leak channels. The first EAG K+ channel was identified in Drosophila melanogaster.ollowing a screen for mutations giving rise to behavioural abnormalities. Disruption of the Eag gene caused an ether-induced.eg-shaking behaviour. Subsequent studies have revealed a conserved multi-gene family of EAG-like K+ channels.hich are present in human and many other species. Based on the varying functional properties of the channels.he family has been divided into 3 subfamilies: EAG.LK and ERG. Interestingly.aenorhabditis elegans appears to lack the ELK type .Little is known about the properties of channels of the ELK subfamily. However.hen expressed in frog oocytes.hey show properties between those of the EAG and ERG subtypes. Included in this family are Bec1 and Bec2.rain-specific genes found in the human telencephalon regions. It is thought that they are involved in cellular excitability of restricted neurons in the human central nervous system. Phylogenetic analysis reveals that these genes constitute a subfamily with Elk within the Eag family . Recently. further Elk subfamily member has been identified in the mouse (Melk). On the basis of sequence similarity.his indicates a distinct subclass within this family .
  IPR003950:ELK potassium channel
Terpenoid cyclases catalyze remarkably complex cyclisation cascades that are initiated by the formation of a highly reactive carbocation in a polyisoprene substrate . The pathways of monoterpene.esquiterpene.nd diterpene biosynthesis are conveniently divided into several stages . The first encompasses the synthesis of isopentenyl diphosphate.somerization to dimethylallyl diphosphate.renyltransferase-catalysed condensation of these two C5-units to geranyl diphosphate (GDP).nd the subsequent 1-4 additions of isopentenyl diphosphate to generate farnesyl (FDP) and geranylgeranyl (GGDP)diphosphate. In the second stage.he prenyl diphosphates undergo a range of cyclisations based on variations on the same mechanistic theme to produce the parent skeletons of each class. Thus.DP (C10) gives rise to monoterpenes.DP (C15) to sesquiterpenes.nd GGDP (C20) to diterpenes. These transformations catalysed by the terpenoid synthases (cyclases) may be followed by a variety of redox modifications of the parent skeletal types to produce the many thousands of different terpenoid metabolites of the essential oils.urpentines.nd resins of plant origin. Terpenoid synthases enzymes provide a template for binding and stabilizing the flexible substrate in the precise orientation required for catalysis.rigger carbocation formation.haperone the conformations of the reactive carbocation intermediates through a unique cyclisation sequence.nd sequester and stabilize carbocations from premature quenching .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008949:Terpenoid synthase
IPR005821:Ion_trans 
Evalue:-24.1426677703857 
Location:265-474IPR000595:cNMP 
Evalue:-11.602059991328 
Location:556-681IPR013655:PAS_3 
Evalue:-6.92081880569458 
Location:42-136IPR003938:EAGCHANLFMLY 
Evalue:0 
Location:221-230IPR003938:EAGCHANLFMLY 
Evalue:0 
Location:520-527IPR003938:EAGCHANLFMLY 
Evalue:0 
Location:239-246IPR000595:CNMP_BINDING_2 
Evalue:0 
Location:0-0
SequencesProtein: KCNH4_HUMAN (1017 aa)
mRNA: NM_012285
Local Annotation
Synapse Ontology
this kind of receptor usually locates at the postsynaptic plasma membranous region.
sdb:0109 ionotropic receptor  (Evidence:domains)
?
sdb:0219 GPCR mediated signaling  (Evidence:domains)
LTP that is not dependent on the function of NMDA receptor.
sdb:0255 NMDA Receptor-independent LTP  (Evidence:domains)
K channel plays an important role in the course of action potential
sdb:0286 K channel  (Evidence:domains)
all kinds of ion channels that play their roles in the synaptic activity.
sdb:0308 ion channels and receptors  (Evidence:domains)
KO assignmentK04907
  Level 3 annotation:
    potassium voltage-gated channel, Eag-related subfamily H, member 4
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 75 residues, 37562438-37562662Exon2: 237 residues, 37565274-37565979Exon3: 26 residues, 37567791-37567865Exon4: 37 residues, 37568771-37568878Exon5: 119 residues, 37569149-37569502Exon6: 15 residues, 37569673-37569712Exon7: 83 residues, 37570992-37571237Exon8: 85 residues, 37571840-37572090Exon9: 68 residues, 37575020-37575220Exon10: 67 residues, 37575650-37575845Exon11: 71 residues, 37577331-37577539Exon12: 54 residues, 37581122-37581280Exon13: 83 residues, 37581597-37581841Exon14: 44 residues, 37583643-37583771Exon15: 51 residues, 37583874-37584021Exon16: 80 residues, 37584336-37584570Exon17: 138 residues, 37586413-37586822Exon18: 2 residues, -Jump to KCNH4_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4288 37562438-37586822 ~-24K 15872(KCNH4)(-)Loci: 4289 37589603-37590996 ~-1K 15873(HCRT)(-)Loci: 3002 37864387-37928122 ~-64K 15882(ATP6V0A1)(+)Loci: 3003 37941476-37949990 ~-9K 15887(NAGLU)(+)Loci: 3004 38064836-38072549 ~-8K 15898(TUBG2)(+)Loci: 3005 38088157-38105358 ~-17K 15903(CNTNAP1)(+)Loci: 4290 38105819-38150574 ~-45K 15904(EZH1)(-)Loci: 3006 38186221-38202605 ~-16K 15907(WNK4)(+)Loci: 4291 38215677-38229807 ~-14K 15912(BECN1)(-)Loci: 3007 38250134-38256248 ~-6K 15916(AOC2)(+)Loci: 3008 38256726-38263664 ~-7K 15917(AOC3)(+)Loci: 4292 38420147-38427921 ~-8K 15927(VAT1)(-)Loci: 4293 38449839-38530657 ~-81K 15931(BRCA1)(-)Loci: 4287 37530523-37560548 ~-30K 15871(RAB5C)(-)Link out to UCSC