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Protein

Potassium voltage-gated channel subfamily A member 2

Gene

KCNA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772, PubMed:8495559, PubMed:11211111, PubMed:23769686). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:8495559, PubMed:20220134). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:19912772, PubMed:23769686). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559). Regulates neuronal excitability and plays a role as pacemaker in the regulation of neuronal action potentials (By similarity). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (By similarity). Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination (By similarity). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (By similarity). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (By similarity). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (By similarity). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (By similarity).By similarityCurated5 Publications

Miscellaneous

The delay or D-type current observed in hippocampus pyramidal neurons is probably mediated by potassium channels containing KCNA2 plus KCNA1 or other family members. It is activated at about -50 mV, i.e. below the action potential threshold, and is characterized by slow inactivation, extremely slow recovery from inactivation, sensitivity to dendrotoxin (DTX) and to 4-aminopyridine (4-AP).1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by 4-aminopyridine (4-AP) and charybdotoxin (CTX), but not by tetraethylammonium (TEA) (PubMed:19912772). Inhibited by dendrotoxin (DTX) (By similarity). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly specific for KCNA2 (By similarity). Inhibited by maurotoxin (By similarity). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-RIIIK; kappaM-RIIIJ has much higher affinity for channels containing KCNA2 than kappaM-RIIIK, with the exception of heterodimers formed by KCNA2 and KCNA7 where the opposite is true (PubMed:20220134).By similarity2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Homotetrameric channels activate rapidly, i.e within a few msec, but inactivation is very slow, with only a marginal decrease in conductance over several seconds. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, post-translational modifications and the presence or absence of ancillary subunits. For the activation of homotetrameric channels expressed in xenopus oocytes, the threshold is at about -30 mV and the midpoint at about -5 mV.1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei252Important for normal, slow channel gatingBy similarity1
      Sitei381Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxinBy similarity1

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      • delayed rectifier potassium channel activity Source: UniProtKB
      • kinesin binding Source: Ensembl
      • outward rectifier potassium channel activity Source: Ensembl
      • potassium channel activity Source: ProtInc
      • voltage-gated potassium channel activity Source: UniProtKB

      GO - Biological processi

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionIon channel, Potassium channel, Voltage-gated channel
      Biological processIon transport, Potassium transport, Transport
      LigandPotassium

      Enzyme and pathway databases

      Reactome - a knowledgebase of biological pathways and processes

      More...
      Reactomei
      R-HSA-1296072 Voltage gated Potassium channels

      Protein family/group databases

      Transport Classification Database

      More...
      TCDBi
      1.A.1.2.10 the voltage-gated ion channel (vic) superfamily

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
      Recommended name:
      Potassium voltage-gated channel subfamily A member 2
      Alternative name(s):
      NGK1
      Voltage-gated K(+) channel HuKIV1 Publication
      Voltage-gated potassium channel HBK5
      Voltage-gated potassium channel subunit Kv1.2
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:KCNA2
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

      Organism-specific databases

      Eukaryotic Pathogen Database Resources

      More...
      EuPathDBi
      HostDB:ENSG00000177301.13

      Human Gene Nomenclature Database

      More...
      HGNCi
      HGNC:6220 KCNA2

      Online Mendelian Inheritance in Man (OMIM)

      More...
      MIMi
      176262 gene

      neXtProt; the human protein knowledge platform

      More...
      neXtProti
      NX_P16389

      <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

      Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

      Topology

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 160CytoplasmicBy similarityAdd BLAST160
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei161 – 182Helical; Name=Segment S1By similarityAdd BLAST22
      Topological domaini183 – 221ExtracellularBy similarityAdd BLAST39
      Transmembranei222 – 243Helical; Name=Segment S2By similarityAdd BLAST22
      Topological domaini244 – 254CytoplasmicBy similarityAdd BLAST11
      Transmembranei255 – 275Helical; Name=Segment S3By similarityAdd BLAST21
      Topological domaini276 – 289ExtracellularBy similarityAdd BLAST14
      Transmembranei290 – 310Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST21
      Topological domaini311 – 325CytoplasmicBy similarityAdd BLAST15
      Transmembranei326 – 347Helical; Name=Segment S5By similarityAdd BLAST22
      Topological domaini348 – 361ExtracellularBy similarityAdd BLAST14
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei362 – 373Helical; Name=Pore helixBy similarityAdd BLAST12
      Intramembranei374 – 381By similarity8
      Topological domaini382 – 388ExtracellularBy similarity7
      Transmembranei389 – 417Helical; Name=Segment S6By similarityAdd BLAST29
      Topological domaini418 – 499CytoplasmicBy similarityAdd BLAST82

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Membrane, Synapse, Synaptosome

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

      Epileptic encephalopathy, early infantile, 32 (EIEE32)2 Publications
      The disease is caused by mutations affecting the gene represented in this entry.
      Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent.
      See also OMIM:616366
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073704263I → T in EIEE32; dominant-negative mutation; loss of channel function. 1 PublicationCorresponds to variant dbSNP:rs786205231EnsemblClinVar.1
      Natural variantiVAR_073705297R → Q in EIEE32; causes a gain of function. 2 PublicationsCorresponds to variant dbSNP:rs786205232EnsemblClinVar.1
      Natural variantiVAR_073706298L → F in EIEE32; causes a gain of function. 1 PublicationCorresponds to variant dbSNP:rs876657390EnsemblClinVar.1
      Natural variantiVAR_073707405P → L in EIEE32; loss of channel function. 1 PublicationCorresponds to variant dbSNP:rs876657389EnsemblClinVar.1

      Keywords - Diseasei

      Disease mutation, Epilepsy

      Organism-specific databases

      DisGeNET

      More...
      DisGeNETi
      3737

      MalaCards human disease database

      More...
      MalaCardsi
      KCNA2
      MIMi616366 phenotype

      Open Targets

      More...
      OpenTargetsi
      ENSG00000177301

      Orphanet; a database dedicated to information on rare diseases and orphan drugs

      More...
      Orphaneti
      442835 Undetermined early-onset epileptic encephalopathy

      The Pharmacogenetics and Pharmacogenomics Knowledge Base

      More...
      PharmGKBi
      PA206

      Chemistry databases

      ChEMBL database of bioactive drug-like small molecules

      More...
      ChEMBLi
      CHEMBL2086

      Drug and drug target database

      More...
      DrugBanki
      DB06637 Dalfampridine

      IUPHAR/BPS Guide to PHARMACOLOGY

      More...
      GuidetoPHARMACOLOGYi
      539

      Polymorphism and mutation databases

      BioMuta curated single-nucleotide variation and disease association database

      More...
      BioMutai
      KCNA2

      Domain mapping of disease mutations (DMDM)

      More...
      DMDMi
      1345813

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000539721 – 499Potassium voltage-gated channel subfamily A member 2Add BLAST499

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi207N-linked (GlcNAc...) asparagineSequence analysis1
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi244S-palmitoyl cysteineSequence analysis1
      <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei429PhosphotyrosineBy similarity1
      Modified residuei434PhosphoserineBy similarity1
      Modified residuei440PhosphoserineBy similarity1
      Modified residuei441PhosphoserineBy similarity1
      Modified residuei449PhosphoserineBy similarity1
      Modified residuei458PhosphotyrosineBy similarity1
      Modified residuei468PhosphoserineBy similarity1

      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

      Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (By similarity). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (By similarity). Phosphorylation on tyrosine residues suppresses ion channel activity (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN. This is probably due to endocytosis of the phosphorylated channel subunits (By similarity). Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (By similarity).By similarity
      N-glycosylated, with complex, sialylated N-glycans.By similarity

      Keywords - PTMi

      Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

      Proteomic databases

      MaxQB - The MaxQuant DataBase

      More...
      MaxQBi
      P16389

      PaxDb, a database of protein abundance averages across all three domains of life

      More...
      PaxDbi
      P16389

      PeptideAtlas

      More...
      PeptideAtlasi
      P16389

      PRoteomics IDEntifications database

      More...
      PRIDEi
      P16389

      ProteomicsDB human proteome resource

      More...
      ProteomicsDBi
      53349
      53350 [P16389-2]

      PTM databases

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      P16389

      Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

      More...
      PhosphoSitePlusi
      P16389

      <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

      <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

      Detected in brain cortex (PubMed:16473933). Detected in peroneal nerve in the juxtaparanodal regions of the node of Ranvier; expression is decreased in patients with diabetes mellitus that suffer from axonal neuropathy (PubMed:22649228). Detected in paranodal and juxtanodal zones in myelinated spinal cord (at protein level) (PubMed:11086297).3 Publications

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSG00000177301 Expressed in 126 organ(s), highest expression level in cerebellar vermis

      CleanEx database of gene expression profiles

      More...
      CleanExi
      HS_KCNA2

      ExpressionAtlas, Differential and Baseline Expression

      More...
      ExpressionAtlasi
      P16389 baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      P16389 HS

      Organism-specific databases

      Human Protein Atlas

      More...
      HPAi
      CAB001976

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and KCNA7. Channel activity is regulated by interaction with the beta subunits, including KCNAB1 and KCNAB2. Identified in a complex with KCNA1 and KCNAB2 (PubMed:11086297). Identified in a complex with KCNA5 and KCNAB1 (By similarity). Identified in a complex with KCNA4 and FYN (By similarity). Interacts with the beta subunit KCNAB1 (PubMed:19713757). Interacts with PTK2B (By similarity). Interacts (via C-terminus) with CTTN (By similarity). Interacts (via N-terminal cytoplasmic domain) with RHOA (GTP-bound form); this regulates channel activity by reducing location at the cell surface in response to CHRM1 activation (By similarity). Interacts with DRD2 (By similarity). Interacts with SIGMAR1; cocaine consumption leads to increased interaction (By similarity). Interacts with ADAM22 (By similarity). Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts with CNTNAP2 (PubMed:10624965).By similarityCurated4 Publications

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      WithEntry#Exp.IntActNotes
      CAMLGP490693EBI-10210559,EBI-1748958

      GO - Molecular functioni

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGrid)

      More...
      BioGridi
      109940, 17 interactors

      CORUM comprehensive resource of mammalian protein complexes

      More...
      CORUMi
      P16389

      Protein interaction database and analysis system

      More...
      IntActi
      P16389, 2 interactors

      STRING: functional protein association networks

      More...
      STRINGi
      9606.ENSP00000314520

      Chemistry databases

      BindingDB database of measured binding affinities

      More...
      BindingDBi
      P16389

      <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

      3D structure databases

      Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

      More...
      ProteinModelPortali
      P16389

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...
      SMRi
      P16389

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      Search...

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 125Tetramerization domainBy similarityAdd BLAST125
      Regioni312 – 325S4-S5 linkerBy similarityAdd BLAST14

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi374 – 379Selectivity filterBy similarity6
      Motifi497 – 499PDZ-bindingBy similarity3

      <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

      The cytoplasmic N-terminus is important for tetramerization. Interactions between the different subunits modulate the gating characteristics (By similarity). Besides, the cytoplasmic N-terminal domain mediates interaction with RHOA and thus is required for RHOA-mediated endocytosis (By similarity).By similarity
      The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity

      <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      KOG1545 Eukaryota
      COG1226 LUCA

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000158688

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      HOG000231015

      The HOVERGEN Database of Homologous Vertebrate Genes

      More...
      HOVERGENi
      HBG098049

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      P16389

      KEGG Orthology (KO)

      More...
      KOi
      K04875

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      GMTFHTY

      Database of Orthologous Groups

      More...
      OrthoDBi
      EOG091G10NU

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      P16389

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF313103

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      1.20.120.350, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR000210 BTB/POZ_dom
      IPR005821 Ion_trans_dom
      IPR003968 K_chnl_volt-dep_Kv
      IPR003972 K_chnl_volt-dep_Kv1
      IPR004049 K_chnl_volt-dep_Kv1.2
      IPR011333 SKP1/BTB/POZ_sf
      IPR003131 T1-type_BTB
      IPR028325 VG_K_chnl
      IPR027359 Volt_channel_dom_sf

      The PANTHER Classification System

      More...
      PANTHERi
      PTHR11537 PTHR11537, 1 hit
      PTHR11537:SF23 PTHR11537:SF23, 1 hit

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF02214 BTB_2, 1 hit
      PF00520 Ion_trans, 1 hit

      Protein Motif fingerprint database; a protein domain database

      More...
      PRINTSi
      PR00169 KCHANNEL
      PR01509 KV12CHANNEL
      PR01491 KVCHANNEL
      PR01496 SHAKERCHANEL

      Simple Modular Architecture Research Tool; a protein domain database

      More...
      SMARTi
      View protein in SMART
      SM00225 BTB, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF54695 SSF54695, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

      This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

      This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

      Isoform 1 (identifier: P16389-1) [UniParc]FASTAAdd to basket

      This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

      « Hide
              10         20         30         40         50
      MTVATGDPAD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT
      60 70 80 90 100
      LAQFPETLLG DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR
      110 120 130 140 150
      PVNVPLDIFS EEIRFYELGE EAMEMFREDE GYIKEEERPL PENEFQRQVW
      160 170 180 190 200
      LLFEYPESSG PARIIAIVSV MVILISIVSF CLETLPIFRD ENEDMHGSGV
      210 220 230 240 250
      TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR FFACPSKAGF
      260 270 280 290 300
      FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
      310 320 330 340 350
      VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE
      360 370 380 390 400
      ADERESQFPS IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL
      410 420 430 440 450
      TIALPVPVIV SNFNYFYHRE TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA
      460 470 480 490
      STISKSDYME IQEGVNNSNE DFREENLKTA NCTLANTNYV NITKMLTDV
      Length:499
      Mass (Da):56,717
      Last modified:February 1, 1996 - v2
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4B03F1B46A826C39
      GO
      Isoform 2 (identifier: P16389-2) [UniParc]FASTAAdd to basket

      The sequence of this isoform differs from the canonical sequence as follows:
           299-499: VRVFRIFKLS...VNITKMLTDV → ERRPLQSQKS...PAVTTLHRMY

      Note: No experimental confirmation available.
      Show »
      Length:356
      Mass (Da):40,966
      Checksum:i9917ABBFCCCF7411
      GO

      <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

      There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      Gene namesLengthAnnotation
      A0A1W2PPN8A0A1W2PPN8_HUMAN
      Potassium voltage-gated channel sub...
      KCNA2
      377Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A1W2PRY2A0A1W2PRY2_HUMAN
      Potassium voltage-gated channel sub...
      KCNA2
      305Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A1W2PPM7A0A1W2PPM7_HUMAN
      Potassium voltage-gated channel sub...
      KCNA2
      245Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A1W2PP65A0A1W2PP65_HUMAN
      Potassium voltage-gated channel sub...
      KCNA2
      59Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A1W2PR01A0A1W2PR01_HUMAN
      Potassium voltage-gated channel sub...
      KCNA2
      113Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti230I → V in BAF82750 (PubMed:14702039).Curated1

      Natural variant

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_073704263I → T in EIEE32; dominant-negative mutation; loss of channel function. 1 PublicationCorresponds to variant dbSNP:rs786205231EnsemblClinVar.1
      Natural variantiVAR_073705297R → Q in EIEE32; causes a gain of function. 2 PublicationsCorresponds to variant dbSNP:rs786205232EnsemblClinVar.1
      Natural variantiVAR_073706298L → F in EIEE32; causes a gain of function. 1 PublicationCorresponds to variant dbSNP:rs876657390EnsemblClinVar.1
      Natural variantiVAR_078206324S → T Probable disease-associated mutation found in a patient with drug-resistant epilepsy. 1 Publication1
      Natural variantiVAR_073707405P → L in EIEE32; loss of channel function. 1 PublicationCorresponds to variant dbSNP:rs876657389EnsemblClinVar.1

      Alternative sequence

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043077299 – 499VRVFR…MLTDV → ERRPLQSQKSKRGRQHLNTS HDCTLGINLVAGMTVQWTRA SGPDDRQTPAVTTLHRMY in isoform 2. 1 PublicationAdd BLAST201

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      L02752 mRNA Translation: AAA36141.1
      AK290061 mRNA Translation: BAF82750.1
      AL365361 Genomic DNA No translation available.
      CH471122 Genomic DNA Translation: EAW56455.1
      CH471122 Genomic DNA Translation: EAW56456.1
      BC043564 mRNA Translation: AAH43564.1

      The Consensus CDS (CCDS) project

      More...
      CCDSi
      CCDS55625.1 [P16389-2]
      CCDS827.1 [P16389-1]

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      I77466

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_001191198.1, NM_001204269.1 [P16389-2]
      NP_004965.1, NM_004974.3 [P16389-1]
      XP_011539698.1, XM_011541396.2 [P16389-1]
      XP_011539699.1, XM_011541397.2 [P16389-1]
      XP_011539700.1, XM_011541398.2 [P16389-1]
      XP_011539701.1, XM_011541399.2 [P16389-1]
      XP_011539702.1, XM_011541400.2 [P16389-1]
      XP_016856702.1, XM_017001213.1 [P16389-1]

      UniGene gene-oriented nucleotide sequence clusters

      More...
      UniGenei
      Hs.248139
      Hs.657199
      Hs.731191

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENST00000316361; ENSP00000314520; ENSG00000177301 [P16389-1]
      ENST00000369770; ENSP00000358785; ENSG00000177301 [P16389-2]
      ENST00000485317; ENSP00000433109; ENSG00000177301 [P16389-1]
      ENST00000633222; ENSP00000487785; ENSG00000177301 [P16389-1]
      ENST00000638532; ENSP00000491613; ENSG00000177301 [P16389-1]
      ENST00000638616; ENSP00000491977; ENSG00000177301 [P16389-1]

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      3737

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      hsa:3737

      UCSC genome browser

      More...
      UCSCi
      uc009wfv.2 human [P16389-1]

      Keywords - Coding sequence diversityi

      Alternative splicing

      <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      L02752 mRNA Translation: AAA36141.1
      AK290061 mRNA Translation: BAF82750.1
      AL365361 Genomic DNA No translation available.
      CH471122 Genomic DNA Translation: EAW56455.1
      CH471122 Genomic DNA Translation: EAW56456.1
      BC043564 mRNA Translation: AAH43564.1
      CCDSiCCDS55625.1 [P16389-2]
      CCDS827.1 [P16389-1]
      PIRiI77466
      RefSeqiNP_001191198.1, NM_001204269.1 [P16389-2]
      NP_004965.1, NM_004974.3 [P16389-1]
      XP_011539698.1, XM_011541396.2 [P16389-1]
      XP_011539699.1, XM_011541397.2 [P16389-1]
      XP_011539700.1, XM_011541398.2 [P16389-1]
      XP_011539701.1, XM_011541399.2 [P16389-1]
      XP_011539702.1, XM_011541400.2 [P16389-1]
      XP_016856702.1, XM_017001213.1 [P16389-1]
      UniGeneiHs.248139
      Hs.657199
      Hs.731191

      3D structure databases

      ProteinModelPortaliP16389
      SMRiP16389
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi109940, 17 interactors
      CORUMiP16389
      IntActiP16389, 2 interactors
      STRINGi9606.ENSP00000314520

      Chemistry databases

      BindingDBiP16389
      ChEMBLiCHEMBL2086
      DrugBankiDB06637 Dalfampridine
      GuidetoPHARMACOLOGYi539

      Protein family/group databases

      TCDBi1.A.1.2.10 the voltage-gated ion channel (vic) superfamily

      PTM databases

      iPTMnetiP16389
      PhosphoSitePlusiP16389

      Polymorphism and mutation databases

      BioMutaiKCNA2
      DMDMi1345813

      Proteomic databases

      MaxQBiP16389
      PaxDbiP16389
      PeptideAtlasiP16389
      PRIDEiP16389
      ProteomicsDBi53349
      53350 [P16389-2]

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENST00000316361; ENSP00000314520; ENSG00000177301 [P16389-1]
      ENST00000369770; ENSP00000358785; ENSG00000177301 [P16389-2]
      ENST00000485317; ENSP00000433109; ENSG00000177301 [P16389-1]
      ENST00000633222; ENSP00000487785; ENSG00000177301 [P16389-1]
      ENST00000638532; ENSP00000491613; ENSG00000177301 [P16389-1]
      ENST00000638616; ENSP00000491977; ENSG00000177301 [P16389-1]
      GeneIDi3737
      KEGGihsa:3737
      UCSCiuc009wfv.2 human [P16389-1]

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...
      CTDi
      3737
      DisGeNETi3737
      EuPathDBiHostDB:ENSG00000177301.13

      GeneCards: human genes, protein and diseases

      More...
      GeneCardsi
      KCNA2
      HGNCiHGNC:6220 KCNA2
      HPAiCAB001976
      MalaCardsiKCNA2
      MIMi176262 gene
      616366 phenotype
      neXtProtiNX_P16389
      OpenTargetsiENSG00000177301
      Orphaneti442835 Undetermined early-onset epileptic encephalopathy
      PharmGKBiPA206

      GenAtlas: human gene database

      More...
      GenAtlasi
      Search...

      Phylogenomic databases

      eggNOGiKOG1545 Eukaryota
      COG1226 LUCA
      GeneTreeiENSGT00940000158688
      HOGENOMiHOG000231015
      HOVERGENiHBG098049
      InParanoidiP16389
      KOiK04875
      OMAiGMTFHTY
      OrthoDBiEOG091G10NU
      PhylomeDBiP16389
      TreeFamiTF313103

      Enzyme and pathway databases

      ReactomeiR-HSA-1296072 Voltage gated Potassium channels

      Miscellaneous databases

      ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

      More...
      ChiTaRSi
      KCNA2 human

      The Gene Wiki collection of pages on human genes and proteins

      More...
      GeneWikii
      KCNA2

      Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

      More...
      GenomeRNAii
      3737

      Protein Ontology

      More...
      PROi
      PR:P16389

      The Stanford Online Universal Resource for Clones and ESTs

      More...
      SOURCEi
      Search...

      Gene expression databases

      BgeeiENSG00000177301 Expressed in 126 organ(s), highest expression level in cerebellar vermis
      CleanExiHS_KCNA2
      ExpressionAtlasiP16389 baseline and differential
      GenevisibleiP16389 HS

      Family and domain databases

      Gene3Di1.20.120.350, 1 hit
      InterProiView protein in InterPro
      IPR000210 BTB/POZ_dom
      IPR005821 Ion_trans_dom
      IPR003968 K_chnl_volt-dep_Kv
      IPR003972 K_chnl_volt-dep_Kv1
      IPR004049 K_chnl_volt-dep_Kv1.2
      IPR011333 SKP1/BTB/POZ_sf
      IPR003131 T1-type_BTB
      IPR028325 VG_K_chnl
      IPR027359 Volt_channel_dom_sf
      PANTHERiPTHR11537 PTHR11537, 1 hit
      PTHR11537:SF23 PTHR11537:SF23, 1 hit
      PfamiView protein in Pfam
      PF02214 BTB_2, 1 hit
      PF00520 Ion_trans, 1 hit
      PRINTSiPR00169 KCHANNEL
      PR01509 KV12CHANNEL
      PR01491 KVCHANNEL
      PR01496 SHAKERCHANEL
      SMARTiView protein in SMART
      SM00225 BTB, 1 hit
      SUPFAMiSSF54695 SSF54695, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
      Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKCNA2_HUMAN
      <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16389
      Secondary accession number(s): A0A024R0D3, A8K1Z6, Q86XG6
      <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
      Last sequence update: February 1, 1996
      Last modified: December 5, 2018
      This is version 186 of the entry and version 2 of the sequence. See complete history.
      <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program
      DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

      <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. Human chromosome 1
        Human chromosome 1: entries, gene names and cross-references to MIM
      2. SIMILARITY comments
        Index of protein domains and families
      3. Human polymorphisms and disease mutations
        Index of human polymorphisms and disease mutations
      4. Human entries with polymorphisms or disease mutations
        List of human entries with polymorphisms or disease mutations
      5. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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