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Protein

Potassium channel subfamily K member 1

Gene

KCNK1

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

Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed:15820677, PubMed:21653227). Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K+ ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na+ at subphysiological K+ levels and upon acidification of the extracellular medium (PubMed:21653227, PubMed:22431633). The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel (PubMed:8605869, PubMed:8978667, PubMed:15820677, PubMed:21653227, PubMed:22431633, PubMed:23169818, PubMed:25001086). Channel activity is modulated by activation of serotonin receptors (By similarity). Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes (By similarity). Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity (PubMed:23169818). Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane-sensitive currents (PubMed:23169818). Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential (By similarity). Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability (By similarity). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity). Required for normal ion and water transport in the kidney (By similarity). Contributes to the regulation of the resting membrane potential of pancreatic beta cells (By similarity). The low channel activity of homodimeric KCNK1 may be due to sumoylation (PubMed:15820677, PubMed:20498050, PubMed:23169818). The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes (PubMed:19959478).By similarity11 Publications

Miscellaneous

When the external K+ concentration is lowered to subphysiological levels, it takes several minutes till the channel has reached a new, stable state characterized by increased Na+ permeability (PubMed:21653227). Likewise, when the external pH is lowered to values below 6.5, it takes several minutes till the channel has reached a new, stable state characterized by increased Na+ permeability (PubMed:22431633). When raising the K+ concentration back to 5 mM, it takes 40 to 70 minutes for the channel to regain its original selectivity for K+ (PubMed:21653227). Likewise, it takes more that 25 minutes for the channel to regain its original K+ selectivity when the pH is raised back to 7.4 (PubMed:22431633).2 Publications

<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 Ba2+ ions and quinidine (PubMed:8605869). Inhibited by quinine (PubMed:8605869, PubMed:21653227). Is slightly inhibited by 10 mM tetraethylammonium (TEA), and only marginally inhibited by 4-aminopyridine, charybdotoxin and dendrotoxin (PubMed:8605869). Lowering the extracellular pH to below 6.5 transiently activates the channel, and then inhibits channel activity (PubMed:15820677, PubMed:22431633). Inhibited when the intracellular pH is decreased down to pH 6.0, but this may be due to indirect effects (PubMed:8605869).4 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

Has a unit conductance of 34 pS. Both activation and channel closure are very rapid. Is not voltage-gated. The relationship between voltage and current is nearly linear. Has a mean open time of 0.3 msec at a membrane potential of -80 mV, and 1.9 msec at +80 mV (PubMed:8605869).2 Publications

      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>Sitei118Important for increased permeability to Na(+) when K(+) levels are subphysiological1 Publication1
      Sitei146Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability2 Publications1
      Sitei261Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability1 Publication1

      <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

      • identical protein binding Source: IntAct
      • inward rectifier potassium channel activity Source: ProtInc
      • potassium channel activity Source: UniProtKB
      • potassium ion leak channel activity Source: UniProtKB
      • sodium channel activity Source: UniProtKB

      GO - Biological processi

      • cardiac conduction Source: Reactome
      • potassium ion transmembrane transport Source: UniProtKB
      • potassium ion transport Source: ProtInc
      • regulation of resting membrane potential Source: UniProtKB
      • response to nicotine Source: Ensembl
      • sodium ion transmembrane transport Source: UniProtKB
      • stabilization of membrane potential Source: GO_Central

      <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
      Biological processIon transport, Potassium transport, Transport
      LigandPotassium

      Enzyme and pathway databases

      Reactome - a knowledgebase of biological pathways and processes

      More...
      Reactomei
      R-HSA-1299308 Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK)
      R-HSA-5576886 Phase 4 - resting membrane potential

      <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 channel subfamily K member 1
      Alternative name(s):
      Inward rectifying potassium channel protein TWIK-11 Publication
      Potassium channel K2P11 Publication
      Potassium channel KCNO1
      <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:KCNK1
      Synonyms:HOHO11 Publication, KCNO1, TWIK1
      <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:ENSG00000135750.14

      Human Gene Nomenclature Database

      More...
      HGNCi
      HGNC:6272 KCNK1

      Online Mendelian Inheritance in Man (OMIM)

      More...
      MIMi
      601745 gene

      neXtProt; the human protein knowledge platform

      More...
      neXtProti
      NX_O00180

      <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 – 20Cytoplasmic1 PublicationAdd BLAST20
      <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>Transmembranei21 – 41Helical1 PublicationAdd BLAST21
      Topological domaini42 – 103Extracellular1 Publication1 PublicationAdd BLAST62
      <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>Intramembranei104 – 116Helical; Name=Pore helix 11 PublicationAdd BLAST13
      Intramembranei117 – 1221 Publication6
      Topological domaini123 – 132Extracellular1 Publication10
      Transmembranei133 – 156Helical1 PublicationAdd BLAST24
      Topological domaini157 – 181Cytoplasmic1 PublicationAdd BLAST25
      Transmembranei182 – 202Helical1 PublicationAdd BLAST21
      Topological domaini203 – 211Extracellular1 Publication9
      Intramembranei212 – 224Helical; Name=Pore helix 21 PublicationAdd BLAST13
      Intramembranei225 – 2311 Publication7
      Topological domaini232 – 243Extracellular1 PublicationAdd BLAST12
      Transmembranei244 – 267Helical1 PublicationAdd BLAST24
      Topological domaini268 – 336Cytoplasmic1 PublicationAdd BLAST69

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, 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

      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>Mutagenesisi69C → A: Abolishes channel activity and formation of disulfide-linked homodimers. 1 Publication1
      Mutagenesisi95N → A: Abolishes N-glycosylation. 1 Publication1
      Mutagenesisi108 – 109LF → FY: Impairs selectivity for K(+) ions and increases permeability to Na(+) ions, both at pH 7.4 and at pH 6. 1 Publication2
      Mutagenesisi118T → I: Abolishes change in ion selectivity in the presence of subphysiological K(+) levels. 1 Publication1
      Mutagenesisi122H → K: Increases channel activity, and has only a minor effect on the inhibition by acidification of the extracellular medium. 1 Publication1
      Mutagenesisi122H → N: Decreases channel activity and abolishes inhibition by acidification of the extracellular medium. 3 Publications1
      Mutagenesisi146L → A or V: Does not increase the low intrinsic channel activity. 1 Publication1
      Mutagenesisi146L → D: Increases channel activity. 2 Publications1
      Mutagenesisi146L → N or T: Increases channel activity. 1 Publication1
      Mutagenesisi146L → S: Increases channel activity. Strongly increases channel activity; when associated with S-261. 1 Publication1
      Mutagenesisi161T → A: No effect on channel activity. 1 Publication1
      Mutagenesisi228L → F: No effect on selectivity for K(+) ions. 1 Publication1
      Mutagenesisi231Y → F: Strongly decreases activity of homodimeric channels and of heterodimeric channels formed with KCNK3 and with KCNK9. No effect on location at the cell membrane. 1 Publication1
      Mutagenesisi250T → L: Slighly decreases the increased permeability to Na(+) ions at pH 6. 1 Publication1
      Mutagenesisi261L → D or N: Increases channel activity. 1 Publication1
      Mutagenesisi261L → S: Increases channel activity. Strongly increases channel activity; when associated with S-146. 1 Publication1
      Mutagenesisi274K → A, C, D, Q or R: Converts the electrically silent channel that is present at the cell membrane to an active channel. 1 Publication1
      Mutagenesisi274K → E: Converts the electrically silent channel that is present at the cell membrane to an active channel. No effect on retention in recycling endosomes. 6 Publications1
      Mutagenesisi293 – 294II → AA: Strongly increases location at the cell membrane. 1 Publication2
      Mutagenesisi299 – 336Missing : No effect on intracellular retention in recycling endosomes. 1 PublicationAdd BLAST38

      Organism-specific databases

      DisGeNET

      More...
      DisGeNETi
      3775

      Open Targets

      More...
      OpenTargetsi
      ENSG00000135750

      The Pharmacogenetics and Pharmacogenomics Knowledge Base

      More...
      PharmGKBi
      PA219

      Chemistry databases

      Drug and drug target database

      More...
      DrugBanki
      DB00308 Ibutilide
      DB00908 Quinidine
      DB01346 Quinidine barbiturate

      Polymorphism and mutation databases

      BioMuta curated single-nucleotide variation and disease association database

      More...
      BioMutai
      KCNK1

      <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_00001017401 – 336Potassium channel subfamily K member 1Add BLAST336

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi69Interchain2 Publications
      <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>Glycosylationi95N-linked (GlcNAc...) asparagine1 Publication1
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
      <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 residuei326PhosphoserineBy 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

      Sumoylation is controversial. Sumoylated by UBE2I (PubMed:15820677). Not sumoylated when expressed in xenopus oocytes or mammalian cells (PubMed:17693262). Sumoylation inactivates the channel, but does not interfere with expression at the cell membrane (PubMed:15820677). Sumoylation of a single subunit is sufficient to silence the dimeric channel (PubMed:20498050, PubMed:23169818). Sumoylation of KCNK1 is sufficient to silence heterodimeric channels formed by KCNK1 and KCNK3 or KCNK9 (PubMed:23169818). Desumoylated by SENP1; this activates the channel (PubMed:15820677, PubMed:20498050, PubMed:23169818). Desumoylated by SENP1; this strongly increases halothane-mediated activation of heterodimeric channels formed with KCNK9 (PubMed:23169818). SENP1 treatment has no effect (PubMed:17693262).4 Publications

      Keywords - PTMi

      Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...
      EPDi
      O00180

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      O00180

      MaxQB - The MaxQuant DataBase

      More...
      MaxQBi
      O00180

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

      More...
      PaxDbi
      O00180

      PeptideAtlas

      More...
      PeptideAtlasi
      O00180

      PRoteomics IDEntifications database

      More...
      PRIDEi
      O00180

      ProteomicsDB human proteome resource

      More...
      ProteomicsDBi
      47763

      PTM databases

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      O00180

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

      More...
      PhosphoSitePlusi
      O00180

      <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 bronchial epithelial cells (PubMed:21964404). Detected in heart left atrium and left ventricle (PubMed:17478540). Detected in cardiac myocytes (at protein level) (PubMed:21653227). Widely expressed with high levels in heart, brain and kidney, and lower levels in colon, ovary, placenta, lung and liver (PubMed:8605869, PubMed:9362344). Highly expressed in cerebellum, and detected at lower levels in amygdala, caudate nucleus, brain cortex, hippocampus, putamen, substantia nigra, thalamus, dorsal root ganglion, spinal cord, pituitary, heart, kidney, lung, placenta, pancreas, stomach, small intestine, uterus and prostate (PubMed:11165377). Detected in right and left heart ventricle and atrium, and in heart Purkinje fibers (PubMed:17478540). Detected in bronchial epithelial cells (PubMed:21964404).6 Publications

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSG00000135750 Expressed in 221 organ(s), highest expression level in cerebellum

      CleanEx database of gene expression profiles

      More...
      CleanExi
      HS_KCNK1

      ExpressionAtlas, Differential and Baseline Expression

      More...
      ExpressionAtlasi
      O00180 baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      O00180 HS

      Organism-specific databases

      Human Protein Atlas

      More...
      HPAi
      CAB022588
      HPA016049

      <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

      Homodimer; disulfide-linked (PubMed:8978667, PubMed:22282804). Heterodimer with KCNK2; disulfide-linked (By similarity). In astrocytes, forms mostly heterodimeric potassium channels with KCNK2, with only a minor proportion of functional channels containing homodimeric KCNK1 (By similarity). Interacts with KCNK3 and KCNK9, forming functional heterodimeric channels (PubMed:23169818). Interacts with GNG4 (By similarity). Identified in a complex with PSD and ARF6; interacts only with PSD that is bound to ARF6 (By similarity). Interacts with UBE2I (PubMed:15820677).By similarity4 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
      109976, 6 interactors

      Database of interacting proteins

      More...
      DIPi
      DIP-59532N

      Protein interaction database and analysis system

      More...
      IntActi
      O00180, 10 interactors

      STRING: functional protein association networks

      More...
      STRINGi
      9606.ENSP00000355580

      <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

      Secondary structure

      1336
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      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
      3UKMX-ray3.40A/B/C/D19-288[»]

      Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

      More...
      ProteinModelPortali
      O00180

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

      More...
      SMRi
      O00180

      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>Regioni117 – 122Selectivity filter 11 Publication1 Publication6
      Regioni225 – 230Selectivity filter 21 Publication6
      Regioni293 – 299Important for intracellular retention in recycling endosomes1 Publication7

      <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
      KOG1418 Eukaryota
      COG1226 LUCA

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000155293

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      HOG000286014

      The HOVERGEN Database of Homologous Vertebrate Genes

      More...
      HOVERGENi
      HBG052237

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      O00180

      KEGG Orthology (KO)

      More...
      KOi
      K04912

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      VQRVTIH

      Database of Orthologous Groups

      More...
      OrthoDBi
      1211599at2759

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      O00180

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF313947

      Family and domain databases

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR003280 2pore_dom_K_chnl
      IPR003092 2pore_dom_K_chnl_TASK
      IPR005408 2pore_dom_K_chnl_TWIK
      IPR001779 2pore_dom_K_chnl_TWIK1
      IPR013099 K_chnl_dom

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF07885 Ion_trans_2, 2 hits

      PIRSF; a whole-protein classification database

      More...
      PIRSFi
      PIRSF038061 K_channel_subfamily_K_type, 1 hit

      Protein Motif fingerprint database; a protein domain database

      More...
      PRINTSi
      PR01333 2POREKCHANEL
      PR01096 TWIK1CHANNEL
      PR01586 TWIKCHANNEL

      <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 1 potential isoform that is computationally mapped.Show allAlign All

      O00180-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MLQSLAGSSC VRLVERHRSA WCFGFLVLGY LLYLVFGAVV FSSVELPYED
      60 70 80 90 100
      LLRQELRKLK RRFLEEHECL SEQQLEQFLG RVLEASNYGV SVLSNASGNW
      110 120 130 140 150
      NWDFTSALFF ASTVLSTTGY GHTVPLSDGG KAFCIIYSVI GIPFTLLFLT
      160 170 180 190 200
      AVVQRITVHV TRRPVLYFHI RWGFSKQVVA IVHAVLLGFV TVSCFFFIPA
      210 220 230 240 250
      AVFSVLEDDW NFLESFYFCF ISLSTIGLGD YVPGEGYNQK FRELYKIGIT
      260 270 280 290 300
      CYLLLGLIAM LVVLETFCEL HELKKFRKMF YVKKDKDEDQ VHIIEHDQLS
      310 320 330
      FSSITDQAAG MKEDQKQNEP FVATQSSACV DGPANH
      Length:336
      Mass (Da):38,143
      Last modified:July 1, 1997 - v1
      <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:i2A41D9501323215D
      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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      Gene namesLengthAnnotation
      Q5T5E6Q5T5E6_HUMAN
      Potassium channel subfamily K membe...
      KCNK1
      242Annotation score:

      Annotation score:2 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>

      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
      U33632 mRNA Translation: AAB01688.1
      U76996 mRNA Translation: AAB97878.1
      U90065 mRNA Translation: AAB51147.1
      AL356357 Genomic DNA No translation available.
      CH471098 Genomic DNA Translation: EAW69989.1
      BC018051 mRNA Translation: AAH18051.1

      The Consensus CDS (CCDS) project

      More...
      CCDSi
      CCDS1599.1

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      S65566

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_002236.1, NM_002245.3

      UniGene gene-oriented nucleotide sequence clusters

      More...
      UniGenei
      Hs.208544

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENST00000366621; ENSP00000355580; ENSG00000135750

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      3775

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      hsa:3775

      UCSC genome browser

      More...
      UCSCi
      uc010pxo.1 human

      <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
      U33632 mRNA Translation: AAB01688.1
      U76996 mRNA Translation: AAB97878.1
      U90065 mRNA Translation: AAB51147.1
      AL356357 Genomic DNA No translation available.
      CH471098 Genomic DNA Translation: EAW69989.1
      BC018051 mRNA Translation: AAH18051.1
      CCDSiCCDS1599.1
      PIRiS65566
      RefSeqiNP_002236.1, NM_002245.3
      UniGeneiHs.208544

      3D structure databases

      Select the link destinations:
      PDBei
      RCSB PDBi
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      3UKMX-ray3.40A/B/C/D19-288[»]
      ProteinModelPortaliO00180
      SMRiO00180
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi109976, 6 interactors
      DIPiDIP-59532N
      IntActiO00180, 10 interactors
      STRINGi9606.ENSP00000355580

      Chemistry databases

      DrugBankiDB00308 Ibutilide
      DB00908 Quinidine
      DB01346 Quinidine barbiturate

      PTM databases

      iPTMnetiO00180
      PhosphoSitePlusiO00180

      Polymorphism and mutation databases

      BioMutaiKCNK1

      Proteomic databases

      EPDiO00180
      jPOSTiO00180
      MaxQBiO00180
      PaxDbiO00180
      PeptideAtlasiO00180
      PRIDEiO00180
      ProteomicsDBi47763

      Protocols and materials databases

      The DNASU plasmid repository

      More...
      DNASUi
      3775
      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENST00000366621; ENSP00000355580; ENSG00000135750
      GeneIDi3775
      KEGGihsa:3775
      UCSCiuc010pxo.1 human

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...
      CTDi
      3775
      DisGeNETi3775
      EuPathDBiHostDB:ENSG00000135750.14

      GeneCards: human genes, protein and diseases

      More...
      GeneCardsi
      KCNK1
      HGNCiHGNC:6272 KCNK1
      HPAiCAB022588
      HPA016049
      MIMi601745 gene
      neXtProtiNX_O00180
      OpenTargetsiENSG00000135750
      PharmGKBiPA219

      GenAtlas: human gene database

      More...
      GenAtlasi
      Search...

      Phylogenomic databases

      eggNOGiKOG1418 Eukaryota
      COG1226 LUCA
      GeneTreeiENSGT00940000155293
      HOGENOMiHOG000286014
      HOVERGENiHBG052237
      InParanoidiO00180
      KOiK04912
      OMAiVQRVTIH
      OrthoDBi1211599at2759
      PhylomeDBiO00180
      TreeFamiTF313947

      Enzyme and pathway databases

      ReactomeiR-HSA-1299308 Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK)
      R-HSA-5576886 Phase 4 - resting membrane potential

      Miscellaneous databases

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

      More...
      ChiTaRSi
      KCNK1 human

      The Gene Wiki collection of pages on human genes and proteins

      More...
      GeneWikii
      KCNK1

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

      More...
      GenomeRNAii
      3775

      Protein Ontology

      More...
      PROi
      PR:O00180

      The Stanford Online Universal Resource for Clones and ESTs

      More...
      SOURCEi
      Search...

      Gene expression databases

      BgeeiENSG00000135750 Expressed in 221 organ(s), highest expression level in cerebellum
      CleanExiHS_KCNK1
      ExpressionAtlasiO00180 baseline and differential
      GenevisibleiO00180 HS

      Family and domain databases

      InterProiView protein in InterPro
      IPR003280 2pore_dom_K_chnl
      IPR003092 2pore_dom_K_chnl_TASK
      IPR005408 2pore_dom_K_chnl_TWIK
      IPR001779 2pore_dom_K_chnl_TWIK1
      IPR013099 K_chnl_dom
      PfamiView protein in Pfam
      PF07885 Ion_trans_2, 2 hits
      PIRSFiPIRSF038061 K_channel_subfamily_K_type, 1 hit
      PRINTSiPR01333 2POREKCHANEL
      PR01096 TWIK1CHANNEL
      PR01586 TWIKCHANNEL

      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 nameiKCNK1_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: O00180
      Secondary accession number(s): Q13307, Q5T5E8
      <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: February 21, 2001
      Last sequence update: July 1, 1997
      Last modified: January 16, 2019
      This is version 171 of the entry and version 1 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. SIMILARITY comments
        Index of protein domains and families
      2. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
      3. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      4. Human chromosome 1
        Human chromosome 1: entries, gene names and cross-references to MIM
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