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O95279 (KCNK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium channel subfamily K member 5
Alternative name(s):
Acid-sensitive potassium channel protein TASK-2
TWIK-related acid-sensitive K(+) channel 2
Gene names
Name:KCNK5
Synonyms:TASK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

pH-dependent, voltage insensitive, outwardly rectifying potassium channel. Outward rectification is lost at high external K+ concentrations.

Subunit structure

Homodimer; disulfide-linked. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Abundant expression in kidney, also detected in liver, placenta and small intestine. In the kidney, expression is restricted to the distal tubules and collecting ducts. Not expressed in proximal tubules or glomeruli.

Miscellaneous

Inhibited by quinine, quinidine and external acidification.

Sequence similarities

Belongs to the two pore domain potassium channel (TC 1.A.1.8) family. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processexcretion

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentintegral to plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionpotassium channel activity

Traceable author statement Ref.1. Source: ProtInc

voltage-gated ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Potassium channel subfamily K member 5
PRO_0000101749

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2619Helical; Potential
Intramembrane85 – 11228Pore-forming; Name=Pore-forming 1; Potential
Transmembrane113 – 13321Helical; Potential
Topological domain134 – 15724Cytoplasmic Potential
Transmembrane158 – 18023Helical; Potential
Intramembrane190 – 21526Pore-forming; Name=Pore-forming 2; Potential
Transmembrane230 – 25021Helical; Potential
Topological domain251 – 32575Cytoplasmic Potential

Amino acid modifications

Modified residue3711Phosphoserine Ref.7
Glycosylation771N-linked (GlcNAc...) Potential
Disulfide bond51Interchain Ref.6

Natural variations

Natural variant4651P → T.
Corresponds to variant rs9462487 [ dbSNP | Ensembl ].
VAR_052425

Sequences

Sequence LengthMass (Da)Tools
O95279 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E871A7A4823DDA00

FASTA49955,130
        10         20         30         40         50         60 
MVDRGPLLTS AIIFYLAIGA AIFEVLEEPH WKEAKKNYYT QKLHLLKEFP CLGQEGLDKI 

        70         80         90        100        110        120 
LEVVSDAAGQ GVAITGNQTF NNWNWPNAMI FAATVITTIG YGNVAPKTPA GRLFCVFYGL 

       130        140        150        160        170        180 
FGVPLCLTWI SALGKFFGGR AKRLGQFLTK RGVSLRKAQI TCTVIFIVWG VLVHLVIPPF 

       190        200        210        220        230        240 
VFMVTEGWNY IEGLYYSFIT ISTIGFGDFV AGVNPSANYH ALYRYFVELW IYLGLAWLSL 

       250        260        270        280        290        300 
FVNWKVSMFV EVHKAIKKRR RRRKESFESS PHSRKALQVK GSTASKDVNI FSFLSKKEET 

       310        320        330        340        350        360 
YNDLIKQIGK KAMKTSGGGE TGPGPGLGPQ GGGLPALPPS LVPLVVYSKN RVPTLEEVSQ 

       370        380        390        400        410        420 
TLRSKGHVSR SPDEEAVARA PEDSSPAPEV FMNQLDRISE ECEPWDAQDY HPLIFQDASI 

       430        440        450        460        470        480 
TFVNTEAGLS DEETSKSSLE DNLAGEESPQ QGAEAKAPLN MGEFPSSSES TFTSTESELS 

       490 
VPYEQLMNEY NKANSPKGT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a novel pH-sensitive two pore domain K+ channel from human kidney."
Reyes R., Duprat F., Lesage F., Fink M., Salinas M., Farman N., Lazdunski M.
J. Biol. Chem. 273:30863-30869(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Regulation of two-pore-domain (K2P) potassium leak channels by the tyrosine kinase inhibitor genistein."
Gierten J., Ficker E., Bloehs R., Schlomer K., Kathofer S., Scholz E., Zitron E., Kiesecker C., Bauer A., Becker R., Katus H.A., Karle C.A., Thomas D.
Br. J. Pharmacol. 154:1680-1690(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Placenta.
[6]"Extracellular conserved cysteine forms an intersubunit disulphide bridge in the KCNK5 (TASK-2) K+ channel without having an essential effect upon activity."
Niemeyer M.I., Cid L.P., Valenzuela X., Paeile V., Sepulveda F.V.
Mol. Membr. Biol. 20:185-191(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084830 mRNA. Translation: AAC79458.1.
EU978936 mRNA. Translation: ACH86095.1.
AL451185 Genomic DNA. Translation: CAH70466.1.
CH471081 Genomic DNA. Translation: EAX03979.1.
BC060793 mRNA. Translation: AAH60793.1.
BC069573 mRNA. Translation: AAH69573.1.
IPIIPI00029507.
RefSeqNP_003731.1. NM_003740.3.
UniGeneHs.444448.

3D structure databases

ProteinModelPortalO95279.
ModBaseSearch...

Protein-protein interaction databases

IntActO95279. 1 interaction.

Protein family/group databases

TCDB1.A.1.8.2. voltage-gated ion channel (VIC) superfamily.

PTM databases

PhosphoSiteO95279.

Proteomic databases

PaxDbO95279.
PRIDEO95279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359534; ENSP00000352527; ENSG00000164626.
GeneID8645.
KEGGhsa:8645.
UCSCuc003oon.3. human.

Organism-specific databases

CTD8645.
GeneCardsGC06M039203.
HGNCHGNC:6280. KCNK5.
MIM603493. gene.
neXtProtNX_O95279.
PharmGKBPA30062.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323264.
HOGENOMHOG000113211.
HOVERGENHBG052236.
InParanoidO95279.
KOK04916.
OMAPYEQLMN.
OrthoDBEOG44J2HX.
PhylomeDBO95279.

Gene expression databases

BgeeO95279.
CleanExHS_KCNK5.
GenevestigatorO95279.
GermOnlineENSG00000164626. Homo sapiens.

Family and domain databases

InterProIPR003280. 2pore_dom_K_chnl.
IPR003092. 2pore_dom_K_chnl_TASK.
IPR013099. Ion_trans_2.
[Graphical view]
PfamPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PRINTSPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.
ProtoNetSearch...

Other

ChiTaRSKCNK5. human.
GenomeRNAi8645.
NextBio32411.
SOURCESearch...

Entry information

Entry nameKCNK5_HUMAN
AccessionPrimary (citable) accession number: O95279
Secondary accession number(s): B5TJL2, Q5VV76
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families