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O00180

- KCNK1_HUMAN

UniProt

O00180 - KCNK1_HUMAN

Protein

Potassium channel subfamily K member 1

Gene

KCNK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Weakly inward rectifying potassium channel.1 Publication

    GO - Molecular functioni

    1. inward rectifier potassium channel activity Source: ProtInc

    GO - Biological processi

    1. potassium ion transport Source: ProtInc
    2. response to nicotine Source: Ensembl
    3. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Potassium

    Enzyme and pathway databases

    ReactomeiREACT_75779. Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium channel subfamily K member 1
    Alternative name(s):
    Inward rectifying potassium channel protein TWIK-1
    Potassium channel KCNO1
    Gene namesi
    Name:KCNK1
    Synonyms:HOHO1, KCNO1, TWIK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6272. KCNK1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. brush border membrane Source: Ensembl
    3. endosome Source: Ensembl
    4. plasma membrane Source: Reactome
    5. voltage-gated potassium channel complex Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611T → A: No effect on channel activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA219.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 336336Potassium channel subfamily K member 1PRO_0000101740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 – 69Interchain1 Publication
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO00180.
    PaxDbiO00180.
    PRIDEiO00180.

    PTM databases

    PhosphoSiteiO00180.

    Expressioni

    Tissue specificityi

    Widely expressed with high levels in heart and brain and lower levels in placenta, lung, liver and kidney.

    Gene expression databases

    ArrayExpressiO00180.
    BgeeiO00180.
    CleanExiHS_KCNK1.
    GenevestigatoriO00180.

    Organism-specific databases

    HPAiCAB022588.
    HPA016049.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    BioGridi109976. 4 interactions.
    DIPiDIP-59532N.
    IntActiO00180. 1 interaction.
    STRINGi9606.ENSP00000355580.

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 6648
    Helixi72 – 8615
    Turni87 – 893
    Helixi104 – 11512
    Helixi128 – 16033
    Turni163 – 1675
    Helixi177 – 19519
    Helixi197 – 20610
    Beta strandi207 – 2093
    Helixi212 – 22312
    Beta strandi236 – 2383
    Helixi242 – 26827
    Helixi271 – 2788

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UKMX-ray3.40A/B/C/D19-288[»]
    ProteinModelPortaliO00180.
    SMRiO00180. Positions 19-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini154 – 17724CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini268 – 33669CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei104 – 13027Pore-forming; Name=Pore-forming 1Sequence AnalysisAdd
    BLAST
    Intramembranei212 – 23827Pore-forming; Name=Pore-forming 2Sequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei133 – 15321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei178 – 19821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei247 – 26721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000286014.
    HOVERGENiHBG052237.
    InParanoidiO00180.
    KOiK04912.
    OMAiKQLRKMF.
    OrthoDBiEOG7TTQ85.
    PhylomeDBiO00180.
    TreeFamiTF313947.

    Family and domain databases

    InterProiIPR003280. 2pore_dom_K_chnl.
    IPR013099. 2pore_dom_K_chnl_dom.
    IPR003092. 2pore_dom_K_chnl_TASK.
    IPR005408. 2pore_dom_K_chnl_TWIK.
    IPR001779. 2pore_dom_K_chnl_TWIK1.
    [Graphical view]
    PfamiPF07885. Ion_trans_2. 2 hits.
    [Graphical view]
    PIRSFiPIRSF038061. K_channel_subfamily_K_type. 1 hit.
    PRINTSiPR01333. 2POREKCHANEL.
    PR01096. TWIK1CHANNEL.
    PR01586. TWIKCHANNEL.

    Sequencei

    Sequence statusi: Complete.

    O00180-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLQSLAGSSC VRLVERHRSA WCFGFLVLGY LLYLVFGAVV FSSVELPYED    50
    LLRQELRKLK RRFLEEHECL SEQQLEQFLG RVLEASNYGV SVLSNASGNW 100
    NWDFTSALFF ASTVLSTTGY GHTVPLSDGG KAFCIIYSVI GIPFTLLFLT 150
    AVVQRITVHV TRRPVLYFHI RWGFSKQVVA IVHAVLLGFV TVSCFFFIPA 200
    AVFSVLEDDW NFLESFYFCF ISLSTIGLGD YVPGEGYNQK FRELYKIGIT 250
    CYLLLGLIAM LVVLETFCEL HELKKFRKMF YVKKDKDEDQ VHIIEHDQLS 300
    FSSITDQAAG MKEDQKQNEP FVATQSSACV DGPANH 336
    Length:336
    Mass (Da):38,143
    Last modified:July 1, 1997 - v1
    Checksum:i2A41D9501323215D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33632 mRNA. Translation: AAB01688.1.
    U76996 mRNA. Translation: AAB97878.1.
    U90065 mRNA. Translation: AAB51147.1.
    AL356357 Genomic DNA. Translation: CAI21792.1.
    CH471098 Genomic DNA. Translation: EAW69989.1.
    BC018051 mRNA. Translation: AAH18051.1.
    CCDSiCCDS1599.1.
    PIRiS65566.
    RefSeqiNP_002236.1. NM_002245.3.
    UniGeneiHs.208544.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33632 mRNA. Translation: AAB01688.1 .
    U76996 mRNA. Translation: AAB97878.1 .
    U90065 mRNA. Translation: AAB51147.1 .
    AL356357 Genomic DNA. Translation: CAI21792.1 .
    CH471098 Genomic DNA. Translation: EAW69989.1 .
    BC018051 mRNA. Translation: AAH18051.1 .
    CCDSi CCDS1599.1.
    PIRi S65566.
    RefSeqi NP_002236.1. NM_002245.3.
    UniGenei Hs.208544.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UKM X-ray 3.40 A/B/C/D 19-288 [» ]
    ProteinModelPortali O00180.
    SMRi O00180. Positions 19-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109976. 4 interactions.
    DIPi DIP-59532N.
    IntActi O00180. 1 interaction.
    STRINGi 9606.ENSP00000355580.

    Chemistry

    DrugBanki DB00308. Ibutilide.
    DB00908. Quinidine.

    PTM databases

    PhosphoSitei O00180.

    Proteomic databases

    MaxQBi O00180.
    PaxDbi O00180.
    PRIDEi O00180.

    Protocols and materials databases

    DNASUi 3775.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366621 ; ENSP00000355580 ; ENSG00000135750 .
    GeneIDi 3775.
    KEGGi hsa:3775.
    UCSCi uc010pxo.1. human.

    Organism-specific databases

    CTDi 3775.
    GeneCardsi GC01P233750.
    HGNCi HGNC:6272. KCNK1.
    HPAi CAB022588.
    HPA016049.
    MIMi 601745. gene.
    neXtProti NX_O00180.
    PharmGKBi PA219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000286014.
    HOVERGENi HBG052237.
    InParanoidi O00180.
    KOi K04912.
    OMAi KQLRKMF.
    OrthoDBi EOG7TTQ85.
    PhylomeDBi O00180.
    TreeFami TF313947.

    Enzyme and pathway databases

    Reactomei REACT_75779. Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).

    Miscellaneous databases

    ChiTaRSi KCNK1. human.
    GeneWikii KCNK1.
    GenomeRNAii 3775.
    NextBioi 14807.
    PROi O00180.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00180.
    Bgeei O00180.
    CleanExi HS_KCNK1.
    Genevestigatori O00180.

    Family and domain databases

    InterProi IPR003280. 2pore_dom_K_chnl.
    IPR013099. 2pore_dom_K_chnl_dom.
    IPR003092. 2pore_dom_K_chnl_TASK.
    IPR005408. 2pore_dom_K_chnl_TWIK.
    IPR001779. 2pore_dom_K_chnl_TWIK1.
    [Graphical view ]
    Pfami PF07885. Ion_trans_2. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF038061. K_channel_subfamily_K_type. 1 hit.
    PRINTSi PR01333. 2POREKCHANEL.
    PR01096. TWIK1CHANNEL.
    PR01586. TWIKCHANNEL.
    ProtoNeti Search...

    Publicationsi

    1. "TWIK-1, a ubiquitous human weakly inward rectifying K+ channel with a novel structure."
      Lesage F., Guillemare E., Fink M., Duprat F., Lazdunski M., Romey G., Barhanin J.
      EMBO J. 15:1004-1011(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF THR-161.
      Tissue: Kidney.
    2. "Sequence and function of the two P domain potassium channels: implications of an emerging superfamily."
      Goldstein S.A.N., Wang K.-W., Ilan N., Pausch M.H.
      J. Mol. Med. 76:13-20(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], REVIEW.
      Tissue: Brain.
    3. "Cloning and localization of a double-pore K channel, KCNK1: exclusive expression in distal nephron segments."
      Orias M., Velazquez H., Tung F., Lee G., Desir G.V.
      Am. J. Physiol. 273:F663-F666(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Crystal structure of the human two-pore domain potassium channel K2P1."
      Miller A.N., Long S.B.
      Science 335:432-436(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 23-288, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiKCNK1_HUMAN
    AccessioniPrimary (citable) accession number: O00180
    Secondary accession number(s): Q13307, Q5T5E8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Miscellaneous

    Inhibited by barium, quinine, quinidine and internal acidification. Activated by protein kinase C.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3