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O95069

- KCNK2_HUMAN

UniProt

O95069 - KCNK2_HUMAN

Protein

Potassium channel subfamily K member 2

Gene

KCNK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner.3 Publications
    Isoform 4: Does not display channel activity but reduces the channel activity of isoform 1 and isoform 2 and reduces cell surface expression of isoform 2.By similarity

    GO - Molecular functioni

    1. outward rectifier potassium channel activity Source: UniProtKB
    2. potassium channel inhibitor activity Source: UniProtKB
    3. potassium ion leak channel activity Source: UniProtKB

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: Ensembl
    2. potassium ion transmembrane transport Source: UniProtKB
    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_75819. TWIK related potassium channel (TREK).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium channel subfamily K member 2
    Alternative name(s):
    Outward rectifying potassium channel protein TREK-1
    TREK-1 K(+) channel subunit
    Two pore domain potassium channel TREK-1
    Two pore potassium channel TPKC1
    Gene namesi
    Name:KCNK2
    Synonyms:TREK, TREK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6277. KCNK2.

    Subcellular locationi

    Isoform 1 : Cell membrane By similarity; Multi-pass membrane protein By similarity
    Isoform 2 : Cell membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB
    4. voltage-gated potassium channel complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi348 – 3481S → A: Mimics non-phosphorylated state and has no effect on leak channel activity. 1 Publication
    Mutagenesisi348 – 3481S → D: Phosphomimetic mutant which causes switch to voltage-dependent outward rectifier channel activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA30059.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Potassium channel subfamily K member 2PRO_0000101742Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Modified residuei348 – 3481Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-348 controls the reversible conversion from a leak channel to a voltage-dependent channel.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO95069.
    PRIDEiO95069.

    PTM databases

    PhosphoSiteiO95069.

    Expressioni

    Tissue specificityi

    Isoform 4 is detected in kidney, adrenal gland and brain where it is preferentially expressed in the amygdala but not found in thalamus, hypothalamus, hippocampus or substantia nigra.1 Publication

    Gene expression databases

    ArrayExpressiO95069.
    BgeeiO95069.
    CleanExiHS_KCNK2.
    GenevestigatoriO95069.

    Organism-specific databases

    HPAiHPA056054.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    STRINGi9606.ENSP00000394033.

    Structurei

    3D structure databases

    ProteinModelPortaliO95069.
    SMRiO95069. Positions 58-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6161CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini193 – 22331CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini309 – 426118CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei144 – 17027Pore-forming; Name=Pore-forming 1Sequence AnalysisAdd
    BLAST
    Intramembranei253 – 28331Pore-forming; Name=Pore-forming 2Sequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei62 – 8221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei172 – 19221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei224 – 24421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei288 – 30821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni354 – 42673Required for basal channel activityBy similarityAdd
    BLAST
    Regioni378 – 42649Essential for chloroform and halothane sensitivityBy similarityAdd
    BLAST

    Domaini

    The C-terminal region of isoform 4 mediates its intracellular retention.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOVERGENiHBG052234.
    InParanoidiO95069.
    KOiK04913.
    OMAiAINVMKW.
    PhylomeDBiO95069.
    TreeFamiTF313947.

    Family and domain databases

    InterProiIPR003280. 2pore_dom_K_chnl.
    IPR013099. 2pore_dom_K_chnl_dom.
    IPR003976. 2pore_dom_K_chnl_TREK.
    [Graphical view]
    PfamiPF07885. Ion_trans_2. 2 hits.
    [Graphical view]
    PRINTSiPR01333. 2POREKCHANEL.
    PR01499. TREKCHANNEL.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95069-1) [UniParc]FASTAAdd to Basket

    Also known as: TREK-1b

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

    « Hide

    MLPSASRERP GYRAGVAAPD LLDPKSAAQN SKPRLSFSTK PTVLASRVES    50
    DTTINVMKWK TVSTIFLVVV LYLIIGATVF KALEQPHEIS QRTTIVIQKQ 100
    TFISQHSCVN STELDELIQQ IVAAINAGII PLGNTSNQIS HWDLGSSFFF 150
    AGTVITTIGF GNISPRTEGG KIFCIIYALL GIPLFGFLLA GVGDQLGTIF 200
    GKGIAKVEDT FIKWNVSQTK IRIISTIIFI LFGCVLFVAL PAIIFKHIEG 250
    WSALDAIYFV VITLTTIGFG DYVAGGSDIE YLDFYKPVVW FWILVGLAYF 300
    AAVLSMIGDW LRVISKKTKE EVGEFRAHAA EWTANVTAEF KETRRRLSVE 350
    IYDKFQRATS IKRKLSAELA GNHNQELTPC RRTLSVNHLT SERDVLPPLL 400
    KTESIYLNGL TPHCAGEEIA VIENIK 426
    Length:426
    Mass (Da):47,093
    Last modified:April 17, 2007 - v2
    Checksum:iDB10382B1803DA13
    GO
    Isoform 2 (identifier: O95069-2) [UniParc]FASTAAdd to Basket

    Also known as: TREK-1a

    The sequence of this isoform differs from the canonical sequence as follows:
         2-16: Missing.

    Show »
    Length:411
    Mass (Da):45,495
    Checksum:iFDE40CAB21B42A1C
    GO
    Isoform 3 (identifier: O95069-3) [UniParc]FASTAAdd to Basket

    Also known as: TREK-1c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: MLPSASRERPGYRAGV → MMNPRAKRDFYL

    Show »
    Length:422
    Mass (Da):46,888
    Checksum:i1AD4E0B5C1B6CBE7
    GO
    Isoform 4 (identifier: O95069-4) [UniParc]FASTAAdd to Basket

    Also known as: TREK-1e

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: MLPSASRERPGYRAGV → MMNPRAKRDFYL
         213-232: KWNVSQTKIRIISTIIFILF → VDPILNIWTSISLSCGSGSL
         233-426: Missing.

    Show »
    Length:228
    Mass (Da):24,682
    Checksum:i3BEEDE6F7B5EE839
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3113DWL → RLV in AAD01203. 1 PublicationCurated
    Sequence conflicti391 – 3911S → N in AAD47569. (PubMed:10321245)Curated
    Sequence conflicti411 – 4111T → A in AAD01203. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1616MLPSA…YRAGV → MMNPRAKRDFYL in isoform 3 and isoform 4. 1 PublicationVSP_024428Add
    BLAST
    Alternative sequencei2 – 1615Missing in isoform 2. 4 PublicationsVSP_024429Add
    BLAST
    Alternative sequencei213 – 23220KWNVS…IFILF → VDPILNIWTSISLSCGSGSL in isoform 4. 1 PublicationVSP_047567Add
    BLAST
    Alternative sequencei233 – 426194Missing in isoform 4. 1 PublicationVSP_047568Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129399 mRNA. Translation: AAD47569.1.
    AF171068 mRNA. Translation: AAF89743.1.
    AF004711 mRNA. Translation: AAD01203.1.
    AY552980 mRNA. Translation: AAT49015.2.
    AY552981 mRNA. Translation: AAT49016.1.
    EF165334 mRNA. Translation: ABM47413.1.
    EF165335 mRNA. Translation: ABM47414.1.
    AK291483 mRNA. Translation: BAF84172.1.
    AK315249 mRNA. Translation: BAG37671.1.
    AC092804 Genomic DNA. No translation available.
    AC099675 Genomic DNA. No translation available.
    AL583830 Genomic DNA. No translation available.
    CH471100 Genomic DNA. Translation: EAW93347.1.
    CH471100 Genomic DNA. Translation: EAW93349.1.
    BC069462 mRNA. Translation: AAH69462.1.
    BC101693 mRNA. Translation: AAI01694.1.
    BC101695 mRNA. Translation: AAI01696.1.
    BC143586 mRNA. Translation: AAI43587.1.
    CCDSiCCDS31024.1. [O95069-2]
    CCDS41466.1. [O95069-3]
    CCDS41467.1. [O95069-1]
    RefSeqiNP_001017424.1. NM_001017424.2. [O95069-3]
    NP_001017425.2. NM_001017425.2. [O95069-1]
    NP_055032.1. NM_014217.3. [O95069-2]
    UniGeneiHs.497745.

    Genome annotation databases

    EnsembliENST00000391894; ENSP00000375764; ENSG00000082482. [O95069-2]
    ENST00000391895; ENSP00000375765; ENSG00000082482. [O95069-3]
    ENST00000444842; ENSP00000394033; ENSG00000082482. [O95069-1]
    ENST00000467031; ENSP00000420203; ENSG00000082482. [O95069-4]
    GeneIDi3776.
    KEGGihsa:3776.
    UCSCiuc001hko.3. human. [O95069-3]
    uc001hkq.3. human. [O95069-1]
    uc001hkr.4. human. [O95069-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129399 mRNA. Translation: AAD47569.1 .
    AF171068 mRNA. Translation: AAF89743.1 .
    AF004711 mRNA. Translation: AAD01203.1 .
    AY552980 mRNA. Translation: AAT49015.2 .
    AY552981 mRNA. Translation: AAT49016.1 .
    EF165334 mRNA. Translation: ABM47413.1 .
    EF165335 mRNA. Translation: ABM47414.1 .
    AK291483 mRNA. Translation: BAF84172.1 .
    AK315249 mRNA. Translation: BAG37671.1 .
    AC092804 Genomic DNA. No translation available.
    AC099675 Genomic DNA. No translation available.
    AL583830 Genomic DNA. No translation available.
    CH471100 Genomic DNA. Translation: EAW93347.1 .
    CH471100 Genomic DNA. Translation: EAW93349.1 .
    BC069462 mRNA. Translation: AAH69462.1 .
    BC101693 mRNA. Translation: AAI01694.1 .
    BC101695 mRNA. Translation: AAI01696.1 .
    BC143586 mRNA. Translation: AAI43587.1 .
    CCDSi CCDS31024.1. [O95069-2 ]
    CCDS41466.1. [O95069-3 ]
    CCDS41467.1. [O95069-1 ]
    RefSeqi NP_001017424.1. NM_001017424.2. [O95069-3 ]
    NP_001017425.2. NM_001017425.2. [O95069-1 ]
    NP_055032.1. NM_014217.3. [O95069-2 ]
    UniGenei Hs.497745.

    3D structure databases

    ProteinModelPortali O95069.
    SMRi O95069. Positions 58-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000394033.

    Chemistry

    ChEMBLi CHEMBL2321615.
    DrugBanki DB00204. Dofetilide.
    GuidetoPHARMACOLOGYi 514.

    PTM databases

    PhosphoSitei O95069.

    Proteomic databases

    PaxDbi O95069.
    PRIDEi O95069.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000391894 ; ENSP00000375764 ; ENSG00000082482 . [O95069-2 ]
    ENST00000391895 ; ENSP00000375765 ; ENSG00000082482 . [O95069-3 ]
    ENST00000444842 ; ENSP00000394033 ; ENSG00000082482 . [O95069-1 ]
    ENST00000467031 ; ENSP00000420203 ; ENSG00000082482 . [O95069-4 ]
    GeneIDi 3776.
    KEGGi hsa:3776.
    UCSCi uc001hko.3. human. [O95069-3 ]
    uc001hkq.3. human. [O95069-1 ]
    uc001hkr.4. human. [O95069-2 ]

    Organism-specific databases

    CTDi 3776.
    GeneCardsi GC01P215178.
    HGNCi HGNC:6277. KCNK2.
    HPAi HPA056054.
    MIMi 603219. gene.
    neXtProti NX_O95069.
    PharmGKBi PA30059.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1226.
    HOVERGENi HBG052234.
    InParanoidi O95069.
    KOi K04913.
    OMAi AINVMKW.
    PhylomeDBi O95069.
    TreeFami TF313947.

    Enzyme and pathway databases

    Reactomei REACT_75819. TWIK related potassium channel (TREK).

    Miscellaneous databases

    ChiTaRSi KCNK2. human.
    GeneWikii KCNK2.
    GenomeRNAii 3776.
    NextBioi 14811.
    PROi O95069.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95069.
    Bgeei O95069.
    CleanExi HS_KCNK2.
    Genevestigatori O95069.

    Family and domain databases

    InterProi IPR003280. 2pore_dom_K_chnl.
    IPR013099. 2pore_dom_K_chnl_dom.
    IPR003976. 2pore_dom_K_chnl_TREK.
    [Graphical view ]
    Pfami PF07885. Ion_trans_2. 2 hits.
    [Graphical view ]
    PRINTSi PR01333. 2POREKCHANEL.
    PR01499. TREKCHANNEL.
    ProtoNeti Search...

    Publicationsi

    1. "Inhalational anesthetics activate two-pore-domain background K+ channels."
      Patel A.J., Honore E., Lesage F., Fink M., Romey G., Lazdunski M.
      Nat. Neurosci. 2:422-426(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ACTIVATION.
    2. "Cloning, localisation and functional expression of the human orthologue of the TREK-1 potassium channel."
      Meadows H.J., Benham C.D., Cairns W., Gloger I., Jennings C., Medhurst A.D., Murdock P., Chapman C.G.
      Pflugers Arch. 439:714-722(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
      Tissue: Brain.
    3. Price L.A., Hellings S.E., Hayashi J.H., Pausch M.H.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "A splice variant of the two-pore domain potassium channel TREK-1 with only one pore domain reduces the surface expression of full-length TREK-1 channels."
      Rinne S., Renigunta V., Schlichthorl G., Zuzarte M., Bittner S., Meuth S.G., Decher N., Daut J., Preisig-Muller R.
      Pflugers Arch. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    5. Thomas D., Sullivan A.N., Goldstein S.A.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Heart.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 2).
      Tissue: Lung.
    10. "KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel."
      Bockenhauer D., Zilberberg N., Goldstein S.A.
      Nat. Neurosci. 4:486-491(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-348, MUTAGENESIS OF SER-348.

    Entry informationi

    Entry nameiKCNK2_HUMAN
    AccessioniPrimary (citable) accession number: O95069
    Secondary accession number(s): A1Z1V3
    , A8K618, B2RCS4, B7ZL56, D3DTA5, Q5DP47, Q5DP48, Q9NRT2, Q9UNE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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

    Activated by volatile general anesthetics such as chloroform, halothane and isoflurane.

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3