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Protein

Potassium channel subfamily K member 2

Gene

KCNK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6277. KCNK2.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6161CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence AnalysisAdd
BLAST
Intramembranei144 – 17027Pore-forming; Name=Pore-forming 1Sequence AnalysisAdd
BLAST
Transmembranei172 – 19221HelicalSequence AnalysisAdd
BLAST
Topological domaini193 – 22331CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei224 – 24421HelicalSequence AnalysisAdd
BLAST
Intramembranei253 – 28331Pore-forming; Name=Pore-forming 2Sequence AnalysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST
Topological domaini309 – 426118CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

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.

Chemistry

DrugBankiDB00204. Dofetilide.
DB04855. Dronedarone.

Polymorphism and mutation databases

BioMutaiKCNK2.

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

BgeeiO95069.
CleanExiHS_KCNK2.
ExpressionAtlasiO95069. baseline and differential.
GenevestigatoriO95069.

Organism-specific databases

HPAiHPA056054.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi9606.ENSP00000394033.

Structurei

Secondary structure

1
426
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 10552Combined sources
Helixi111 – 12717Combined sources
Turni133 – 1375Combined sources
Beta strandi141 – 1433Combined sources
Helixi144 – 15512Combined sources
Helixi168 – 21346Combined sources
Helixi218 – 23720Combined sources
Helixi253 – 26412Combined sources
Helixi287 – 31529Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TWKX-ray2.60A/B41-315[»]
ProteinModelPortaliO95069.
SMRiO95069. Positions 53-317.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118858.
HOGENOMiHOG000137657.
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. AlignAdd to basket

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

        10         20         30         40         50
MLPSASRERP GYRAGVAAPD LLDPKSAAQN SKPRLSFSTK PTVLASRVES
60 70 80 90 100
DTTINVMKWK TVSTIFLVVV LYLIIGATVF KALEQPHEIS QRTTIVIQKQ
110 120 130 140 150
TFISQHSCVN STELDELIQQ IVAAINAGII PLGNTSNQIS HWDLGSSFFF
160 170 180 190 200
AGTVITTIGF GNISPRTEGG KIFCIIYALL GIPLFGFLLA GVGDQLGTIF
210 220 230 240 250
GKGIAKVEDT FIKWNVSQTK IRIISTIIFI LFGCVLFVAL PAIIFKHIEG
260 270 280 290 300
WSALDAIYFV VITLTTIGFG DYVAGGSDIE YLDFYKPVVW FWILVGLAYF
310 320 330 340 350
AAVLSMIGDW LRVISKKTKE EVGEFRAHAA EWTANVTAEF KETRRRLSVE
360 370 380 390 400
IYDKFQRATS IKRKLSAELA GNHNQELTPC RRTLSVNHLT SERDVLPPLL
410 420
KTESIYLNGL TPHCAGEEIA VIENIK
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 (Ref. 3) Curated
Sequence conflicti391 – 3911S → N in AAD47569 (PubMed:10321245).Curated
Sequence conflicti411 – 4111T → A in AAD01203 (Ref. 3) Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TWKX-ray2.60A/B41-315[»]
ProteinModelPortaliO95069.
SMRiO95069. Positions 53-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000394033.

Chemistry

BindingDBiO95069.
ChEMBLiCHEMBL2321615.
DrugBankiDB00204. Dofetilide.
DB04855. Dronedarone.
GuidetoPHARMACOLOGYi514.

PTM databases

PhosphoSiteiO95069.

Polymorphism and mutation databases

BioMutaiKCNK2.

Proteomic databases

PaxDbiO95069.
PRIDEiO95069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi3776.
GeneCardsiGC01P215178.
HGNCiHGNC:6277. KCNK2.
HPAiHPA056054.
MIMi603219. gene.
neXtProtiNX_O95069.
PharmGKBiPA30059.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118858.
HOGENOMiHOG000137657.
HOVERGENiHBG052234.
InParanoidiO95069.
KOiK04913.
OMAiAINVMKW.
PhylomeDBiO95069.
TreeFamiTF313947.

Enzyme and pathway databases

ReactomeiREACT_75819. TWIK related potassium channel (TREK).

Miscellaneous databases

ChiTaRSiKCNK2. human.
GeneWikiiKCNK2.
GenomeRNAii3776.
NextBioi14811.
PROiO95069.
SOURCEiSearch...

Gene expression databases

BgeeiO95069.
CleanExiHS_KCNK2.
ExpressionAtlasiO95069. baseline and differential.
GenevestigatoriO95069.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 466:1559-1570(2014) [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: April 29, 2015
This is version 130 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.