Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Potassium voltage-gated channel subfamily A member 1

Gene

KCNA1

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 kidney (PubMed:19903818). Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:17156368). 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). 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:12077175, PubMed:17156368). 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 (PubMed:12077175, PubMed:17156368). 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 KCNA1 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:19912772, PubMed:19968958, PubMed:19307729, PubMed:19903818). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:17156368). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (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) release (By similarity). Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction (By similarity). Required for normal neuromuscular responses (PubMed:11026449, PubMed:17136396). Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli (By similarity). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (By similarity). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (By similarity). Plays a role in the reabsorption of Mg2+ in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential (PubMed:23903368, PubMed:19307729).By similarity11 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 1.1 mM 4-aminopyridine (4-AP) and by 20 mM tetraethylammonium (TEA), but not by charybdotoxin (CTX)(PubMed:19912772). Inhibited by dendrotoxin (DTX) (PubMed:19307729).2 Publications

<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

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.1.2.12 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 1
Alternative name(s):
Voltage-gated K(+) channel HuKI1 Publication
Voltage-gated potassium channel HBK11 Publication
Voltage-gated potassium channel subunit Kv1.1
<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:KCNA1
<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 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000111262.4

Human Gene Nomenclature Database

More...
HGNCi
HGNC:6218 KCNA1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
176260 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q09470

<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 – 164CytoplasmicBy similarityAdd BLAST164
<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>Transmembranei165 – 186Helical; Name=Segment S1By similarityAdd BLAST22
Topological domaini187 – 220ExtracellularBy similarityAdd BLAST34
Transmembranei221 – 242Helical; Name=Segment S2By similarityAdd BLAST22
Topological domaini243 – 253CytoplasmicBy similarityAdd BLAST11
Transmembranei254 – 274Helical; Name=Segment S3By similarityAdd BLAST21
Topological domaini275 – 287ExtracellularBy similarityAdd BLAST13
Transmembranei288 – 308Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST21
Topological domaini309 – 323CytoplasmicBy similarityAdd BLAST15
Transmembranei324 – 345Helical; Name=Segment S5By similarityAdd BLAST22
Topological domaini346 – 359ExtracellularBy 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>Intramembranei360 – 371Helical; Name=Pore helixBy similarityAdd BLAST12
Intramembranei372 – 379By similarity8
Topological domaini380 – 386ExtracellularBy similarity7
Transmembranei387 – 415Helical; Name=Segment S6By similarityAdd BLAST29
Topological domaini416 – 495CytoplasmicBy similarityAdd BLAST80

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Synapse

<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

Episodic ataxia 1 (EA1)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by brief episodes of ataxia and dysarthria. Neurological examination during and between the attacks demonstrates spontaneous, repetitive discharges in the distal musculature (myokymia) that arise from peripheral nerve. Nystagmus is absent.
See also OMIM:160120
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_001508174V → F in EA1. 2 PublicationsCorresponds to variant dbSNP:rs104894349EnsemblClinVar.1
Natural variantiVAR_001509177I → R in EA1. 1 Publication1
Natural variantiVAR_020830184F → C in EA1; alters voltage dependence and kinetics of activation though not of C-type inactivation. 2 PublicationsCorresponds to variant dbSNP:rs104894357EnsemblClinVar.1
Natural variantiVAR_001510226T → A in EA1. 1 PublicationCorresponds to variant dbSNP:rs104894354EnsemblClinVar.1
Natural variantiVAR_020831226T → M in EA1. 1 PublicationCorresponds to variant dbSNP:rs28933383EnsemblClinVar.1
Natural variantiVAR_037101226T → R in EA1; yields currents with a largely reduced amplitude. 1 PublicationCorresponds to variant dbSNP:rs28933383EnsemblClinVar.1
Natural variantiVAR_001511239R → S in EA1. 1 PublicationCorresponds to variant dbSNP:rs104894348EnsemblClinVar.1
Natural variantiVAR_001512249F → I in EA1. 1 PublicationCorresponds to variant dbSNP:rs104894356EnsemblClinVar.1
Natural variantiVAR_020832325E → D in EA1; results in non-functional homomeric channels; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 4 PublicationsCorresponds to variant dbSNP:rs104894353EnsemblClinVar.1
Natural variantiVAR_020833329L → I in EA1. 1 Publication1
Natural variantiVAR_020834342S → I in EA1; phenotype without myokymia. 1 Publication1
Natural variantiVAR_001513404V → I in EA1; results in slower channel activation compared to wild-type; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 3 PublicationsCorresponds to variant dbSNP:rs104894355EnsemblClinVar.1
Natural variantiVAR_001514408V → A in EA1; channels have voltage dependence similar to that of wild-type channels but with faster kinetics and increased C-type inactivation; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 4 PublicationsCorresponds to variant dbSNP:rs104894352EnsemblClinVar.1
Myokymia isolated 1 (MK1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by spontaneous involuntary contraction of muscle fiber groups that can be observed as vermiform movement of the overlying skin. Electromyography typically shows continuous motor unit activity with spontaneous oligo- and multiplet-discharges of high intraburst frequency (myokymic discharges). Isolated spontaneous muscle twitches occur in many persons and have no grave significance.
See also OMIM:160120
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037100226T → K in MK1; induces a reduced efflux of potassium ions during depolarization which results in increased muscle cell activity; coexpression studies of the mutant protein with the wild-type protein produces significantly reduced currents suggesting a severe effect of the mutation. 1 PublicationCorresponds to variant dbSNP:rs28933383EnsemblClinVar.1
Natural variantiVAR_037102242A → P in MK1; 10% reduction of mean peak current amplitudes compared to wil-dtype; mutant and wild-type expression together is consistent with a loss-of-function effect of the mutation. 1 PublicationCorresponds to variant dbSNP:rs28933381EnsemblClinVar.1
Natural variantiVAR_037103244P → H in MK1; does not affect channel activity. 1 PublicationCorresponds to variant dbSNP:rs28933382EnsemblClinVar.1
Natural variantiVAR_072397255N → D in MK1; strongly reduces the activity of homomeric channels with dominant negative effects on wild-type channels. 1 PublicationCorresponds to variant dbSNP:rs121918067EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi35 – 36CC → AA: No effect on palmitoylation, no effect on current kinetics. 1 Publication2
Mutagenesisi177I → N: Slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 1 Publication1
Mutagenesisi243C → A: Strongly decreases palmitoylation and alters current kinetics. 1 Publication1
Mutagenesisi255N → A, H or T: Slightly increases channel activity, but does not affect expression at the cell membrane. 1 Publication1
Mutagenesisi255N → E: Abolishes channel activity, but does not affect expression at the cell membrane. 1 Publication1
Mutagenesisi255N → Q: Strongly reduces channel activity, but does not affect expression at the cell membrane. 1 Publication1
Mutagenesisi255N → V: No effect on channel activity. 1 Publication1
Mutagenesisi446S → A: Impairs phosphorylation by PKA. 1 Publication1
Mutagenesisi446S → E: Impairs expression at the cell membrane. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
3736

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
KCNA1

MalaCards human disease database

More...
MalaCardsi
KCNA1
MIMi160120 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000111262

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

More...
Orphaneti
37612 Episodic ataxia type 1
972 Hereditary continuous muscle fiber activity
199326 Isolated autosomal dominant hypomagnesemia, Glaudemans type
98809 Paroxysmal kinesigenic dyskinesia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30019

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2309

Drug and drug target database

More...
DrugBanki
DB00321 Amitriptyline
DB06637 Dalfampridine
DB01189 Desflurane
DB00228 Enflurane
DB00753 Isoflurane
DB01028 Methoxyflurane
DB01115 Nifedipine
DB01236 Sevoflurane

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
538

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
KCNA1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
223590092

<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_00000539681 – 495Potassium voltage-gated channel subfamily A member 1Add BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei23PhosphoserineBy similarity1
<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>Lipidationi243S-palmitoyl cysteine1 Publication1
Modified residuei322Phosphoserine; by PKASequence analysis1
Modified residuei437PhosphoserineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei446Phosphoserine; by PKA1 Publication1

<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

N-glycosylated.By similarity
Palmitoylated on Cys-243; which may be required for membrane targeting.1 Publication
Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (By similarity). Phosphorylation at Ser-446 regulates channel activity by down-regulating expression at the cell membrane (PubMed:23774215).By similarity1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q09470

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

More...
PaxDbi
Q09470

PeptideAtlas

More...
PeptideAtlasi
Q09470

PRoteomics IDEntifications database

More...
PRIDEi
Q09470

ProteomicsDB human proteome resource

More...
ProteomicsDBi
58722

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q09470

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

More...
PhosphoSitePlusi
Q09470

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q09470

<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 adjacent to nodes of Ranvier in juxtaparanodal zones in spinal cord nerve fibers, but also in paranodal regions in some myelinated spinal cord axons (at protein level) (PubMed:11086297). Detected in the islet of Langerhans (PubMed:21483673).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000111262 Expressed in 103 organ(s), highest expression level in caudate nucleus

CleanEx database of gene expression profiles

More...
CleanExi
HS_KCNA1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q09470 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q09470 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB022365

<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 KCNA2, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:12077175, PubMed:17156368). Channel activity is regulated by interaction with the beta subunits KCNAB1 and KCNAB2 (PubMed:12077175, PubMed:17156368). Identified in a complex with KCNA2 and KCNAB2 (PubMed:11086297). Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts with LGI1 within a complex containing LGI1, KCNA4 and KCNAB1 (By similarity). Interacts (via N-terminus) with STX1A; this promotes channel inactivation (By similarity). Interacts (via N-terminus) with the heterodimer formed by GNB1 and GNG2; this promotes channel inactivation (By similarity). Can interact simultaneously with STX1A and the heterodimer formed by GNB1 and GNG2 (By similarity). Interacts (via cytoplasmic N-terminal domain) with KCNRG; this inhibits channel activity (PubMed:19968958). Interacts with ANK3; this inhibits channel activity (PubMed:23903368).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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109939, 7 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q09470

Protein interaction database and analysis system

More...
IntActi
Q09470, 15 interactors

Molecular INTeraction database

More...
MINTi
Q09470

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000371985

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q09470

<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
Q09470

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

More...
SMRi
Q09470

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 – 128Tetramerization domainBy similarityAdd BLAST128
Regioni310 – 323S4-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>Motifi372 – 377Selectivity filterBy similarity6
Motifi493 – 495PDZ-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 and for interaction with the beta subunits that promote rapid channel closure.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
ENSGT00940000158576

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231015

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052230

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q09470

KEGG Orthology (KO)

More...
KOi
K04874

Identification of Orthologs from Complete Genome Data

More...
OMAi
IHRIDNT

Database of Orthologous Groups

More...
OrthoDBi
EOG091G10NU

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q09470

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
IPR004048 K_chnl_volt-dep_Kv1.1
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

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
PR01508 KV11CHANNEL
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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q09470-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVMSGENVD EASAAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET
60 70 80 90 100
QLKTLAQFPN TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG
110 120 130 140 150
RLRRPVNVPL DMFSEEIKFY ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ
160 170 180 190 200
RQVWLLFEYP ESSGPARVIA IVSVMVILIS IVIFCLETLP ELKDDKDFTG
210 220 230 240 250
TVHRIDNTTV IYNSNIFTDP FFIVETLCII WFSFELVVRF FACPSKTDFF
260 270 280 290 300
KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
310 320 330 340 350
RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE
360 370 380 390 400
EAESHFSSIP DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI
410 420 430 440 450
ALPVPVIVSN FNYFYHRETE GEEQAQLLHV SSPNLASDSD LSRRSSSTMS
460 470 480 490
KSEYMEIEED MNNSIAHYRQ VNIRTANCTT ANQNCVNKSK LLTDV
Length:495
Mass (Da):56,466
Last modified:February 10, 2009 - 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:i0A1B1AB87BCDDEBA
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1W2PRI2A0A1W2PRI2_HUMAN
Potassium voltage-gated channel sub...
KCNA1
441Annotation 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>
A0A1W2PQM4A0A1W2PQM4_HUMAN
Potassium voltage-gated channel sub...
KCNA1
38Annotation 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 conflicti265Missing no nucleotide entry (PubMed:2128063).Curated1
Sequence conflicti315L → R no nucleotide entry (PubMed:2128063).Curated1
Sequence conflicti452S → Y in AAA36139 (PubMed:19912772).Curated1

<p>This subsection of the ‘Sequence’ section provides information relevant to all types of RNA editing events (conversion, insertion, deletion of nucleotides) that lead to one or more amino acid changes compared to the translation of the non-edited RNA version.<p><a href='/help/rna_editing' target='_top'>More...</a></p>RNA editingi

Edited at position 400.1 Publication
Partially edited. RNA editing varies from 17% in the caudate nucleus to 68% in the spinal cord and to 77% in the medulla.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001508174V → F in EA1. 2 PublicationsCorresponds to variant dbSNP:rs104894349EnsemblClinVar.1
Natural variantiVAR_001509177I → R in EA1. 1 Publication1
Natural variantiVAR_020830184F → C in EA1; alters voltage dependence and kinetics of activation though not of C-type inactivation. 2 PublicationsCorresponds to variant dbSNP:rs104894357EnsemblClinVar.1
Natural variantiVAR_020051204R → H. Corresponds to variant dbSNP:rs2229000EnsemblClinVar.1
Natural variantiVAR_001510226T → A in EA1. 1 PublicationCorresponds to variant dbSNP:rs104894354EnsemblClinVar.1
Natural variantiVAR_037100226T → K in MK1; induces a reduced efflux of potassium ions during depolarization which results in increased muscle cell activity; coexpression studies of the mutant protein with the wild-type protein produces significantly reduced currents suggesting a severe effect of the mutation. 1 PublicationCorresponds to variant dbSNP:rs28933383EnsemblClinVar.1
Natural variantiVAR_020831226T → M in EA1. 1 PublicationCorresponds to variant dbSNP:rs28933383EnsemblClinVar.1
Natural variantiVAR_037101226T → R in EA1; yields currents with a largely reduced amplitude. 1 PublicationCorresponds to variant dbSNP:rs28933383EnsemblClinVar.1
Natural variantiVAR_001511239R → S in EA1. 1 PublicationCorresponds to variant dbSNP:rs104894348EnsemblClinVar.1
Natural variantiVAR_037102242A → P in MK1; 10% reduction of mean peak current amplitudes compared to wil-dtype; mutant and wild-type expression together is consistent with a loss-of-function effect of the mutation. 1 PublicationCorresponds to variant dbSNP:rs28933381EnsemblClinVar.1
Natural variantiVAR_037103244P → H in MK1; does not affect channel activity. 1 PublicationCorresponds to variant dbSNP:rs28933382EnsemblClinVar.1
Natural variantiVAR_001512249F → I in EA1. 1 PublicationCorresponds to variant dbSNP:rs104894356EnsemblClinVar.1
Natural variantiVAR_072397255N → D in MK1; strongly reduces the activity of homomeric channels with dominant negative effects on wild-type channels. 1 PublicationCorresponds to variant dbSNP:rs121918067EnsemblClinVar.1
Natural variantiVAR_020832325E → D in EA1; results in non-functional homomeric channels; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 4 PublicationsCorresponds to variant dbSNP:rs104894353EnsemblClinVar.1
Natural variantiVAR_020833329L → I in EA1. 1 Publication1
Natural variantiVAR_020834342S → I in EA1; phenotype without myokymia. 1 Publication1
Natural variantiVAR_016805400I → V in RNA edited version. 1
Natural variantiVAR_001513404V → I in EA1; results in slower channel activation compared to wild-type; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 3 PublicationsCorresponds to variant dbSNP:rs104894355EnsemblClinVar.1
Natural variantiVAR_078205405P → L Probable disease-associated mutation found in a patient with neonatal onset epileptic encephalopathy. 1 Publication1
Natural variantiVAR_001514408V → A in EA1; channels have voltage dependence similar to that of wild-type channels but with faster kinetics and increased C-type inactivation; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4. 4 PublicationsCorresponds to variant dbSNP:rs104894352EnsemblClinVar.1

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
L02750 mRNA Translation: AAA36139.1
AC006063 Genomic DNA No translation available.
CH471116 Genomic DNA Translation: EAW88833.1
BC101733 mRNA Translation: AAI01734.1
BC112180 mRNA Translation: AAI12181.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS8535.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I57680

NCBI Reference Sequences

More...
RefSeqi
NP_000208.2, NM_000217.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.416139

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000382545; ENSP00000371985; ENSG00000111262

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3736

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3736

UCSC genome browser

More...
UCSCi
uc001qnh.4 human

Keywords - Coding sequence diversityi

Polymorphism, RNA editing

<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
L02750 mRNA Translation: AAA36139.1
AC006063 Genomic DNA No translation available.
CH471116 Genomic DNA Translation: EAW88833.1
BC101733 mRNA Translation: AAI01734.1
BC112180 mRNA Translation: AAI12181.1
CCDSiCCDS8535.1
PIRiI57680
RefSeqiNP_000208.2, NM_000217.2
UniGeneiHs.416139

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AFLmodel-A/B/C/D326-407[»]
ProteinModelPortaliQ09470
SMRiQ09470
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109939, 7 interactors
CORUMiQ09470
IntActiQ09470, 15 interactors
MINTiQ09470
STRINGi9606.ENSP00000371985

Chemistry databases

BindingDBiQ09470
ChEMBLiCHEMBL2309
DrugBankiDB00321 Amitriptyline
DB06637 Dalfampridine
DB01189 Desflurane
DB00228 Enflurane
DB00753 Isoflurane
DB01028 Methoxyflurane
DB01115 Nifedipine
DB01236 Sevoflurane
GuidetoPHARMACOLOGYi538

Protein family/group databases

TCDBi1.A.1.2.12 the voltage-gated ion channel (vic) superfamily

PTM databases

iPTMnetiQ09470
PhosphoSitePlusiQ09470
SwissPalmiQ09470

Polymorphism and mutation databases

BioMutaiKCNA1
DMDMi223590092

Proteomic databases

MaxQBiQ09470
PaxDbiQ09470
PeptideAtlasiQ09470
PRIDEiQ09470
ProteomicsDBi58722

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382545; ENSP00000371985; ENSG00000111262
GeneIDi3736
KEGGihsa:3736
UCSCiuc001qnh.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3736
DisGeNETi3736
EuPathDBiHostDB:ENSG00000111262.4

GeneCards: human genes, protein and diseases

More...
GeneCardsi
KCNA1
GeneReviewsiKCNA1
HGNCiHGNC:6218 KCNA1
HPAiCAB022365
MalaCardsiKCNA1
MIMi160120 phenotype
176260 gene
neXtProtiNX_Q09470
OpenTargetsiENSG00000111262
Orphaneti37612 Episodic ataxia type 1
972 Hereditary continuous muscle fiber activity
199326 Isolated autosomal dominant hypomagnesemia, Glaudemans type
98809 Paroxysmal kinesigenic dyskinesia
PharmGKBiPA30019

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1545 Eukaryota
COG1226 LUCA
GeneTreeiENSGT00940000158576
HOGENOMiHOG000231015
HOVERGENiHBG052230
InParanoidiQ09470
KOiK04874
OMAiIHRIDNT
OrthoDBiEOG091G10NU
PhylomeDBiQ09470
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
KCNA1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Kv1.1

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

More...
GenomeRNAii
3736

Protein Ontology

More...
PROi
PR:Q09470

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000111262 Expressed in 103 organ(s), highest expression level in caudate nucleus
CleanExiHS_KCNA1
ExpressionAtlasiQ09470 baseline and differential
GenevisibleiQ09470 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
IPR004048 K_chnl_volt-dep_Kv1.1
IPR011333 SKP1/BTB/POZ_sf
IPR003131 T1-type_BTB
IPR028325 VG_K_chnl
IPR027359 Volt_channel_dom_sf
PANTHERiPTHR11537 PTHR11537, 1 hit
PfamiView protein in Pfam
PF02214 BTB_2, 1 hit
PF00520 Ion_trans, 1 hit
PRINTSiPR00169 KCHANNEL
PR01508 KV11CHANNEL
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 nameiKCNA1_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: Q09470
Secondary accession number(s): A6NM83, Q3MIQ9
<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: November 1, 1995
Last sequence update: February 10, 2009
Last modified: December 5, 2018
This is version 192 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again