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Protein

Potassium channel subfamily K member 17

Gene

KCNK17

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

Functioni

Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K+ currents.

GO - Molecular functioni

  1. potassium channel activity Source: UniProtKB
  2. voltage-gated ion channel activity Source: UniProtKB-KW

GO - Biological processi

  1. potassium ion transport Source: UniProtKB
  2. synaptic transmission Source: Reactome
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_75850. TWIK-related alkaline pH activated K+ channel (TALK).

Protein family/group databases

TCDBi1.A.1.9.6. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel subfamily K member 17
Alternative name(s):
2P domain potassium channel Talk-2
Acid-sensitive potassium channel protein TASK-4
TWIK-related acid-sensitive K(+) channel 4
TWIK-related alkaline pH-activated K(+) channel 2
Short name:
TALK-2
Gene namesi
Name:KCNK17
Synonyms:TALK2, TASK4
ORF Names:UNQ5816/PRO19634
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:14465. KCNK17.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei21 – 4323HelicalSequence AnalysisAdd
BLAST
Intramembranei106 – 12419Pore-forming; Name=Pore-forming 1Sequence AnalysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Topological domaini149 – 17931CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence AnalysisAdd
BLAST
Intramembranei211 – 23020Pore-forming; Name=Pore-forming 2Sequence AnalysisAdd
BLAST
Transmembranei244 – 26421HelicalSequence AnalysisAdd
BLAST
Topological domaini265 – 33268CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Potassium channel subfamily K member 17PRO_0000101768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ96T54.
PRIDEiQ96T54.

Expressioni

Gene expression databases

BgeeiQ96T54.
CleanExiHS_KCNK17.
GenevestigatoriQ96T54.

Organism-specific databases

HPAiHPA043892.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

BioGridi124608. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ96T54.
SMRiQ96T54. Positions 36-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG317582.
GeneTreeiENSGT00760000118858.
HOGENOMiHOG000074161.
HOVERGENiHBG052240.
InParanoidiQ96T54.
KOiK04925.
OMAiSMGRWEF.
OrthoDBiEOG77M8NK.
PhylomeDBiQ96T54.
TreeFamiTF313947.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR013099. 2pore_dom_K_chnl_dom.
IPR003092. 2pore_dom_K_chnl_TASK.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PIRSFiPIRSF038061. K_channel_subfamily_K_type. 1 hit.
PRINTSiPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96T54-3) [UniParc]FASTAAdd to basket

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
MYRPRARAAP EGRVRGCAVP STVLLLLAYL AYLALGTGVF WTLEGRAAQD
60 70 80 90 100
SSRSFQRDKW ELLQNFTCLD RPALDSLIRD VVQAYKNGAS LLSNTTSMGR
110 120 130 140 150
WELVGSFFFS VSTITTIGYG NLSPNTMAAR LFCIFFALVG IPLNLVVLNR
160 170 180 190 200
LGHLMQQGVN HWASRLGGTW QDPDKARWLA GSGALLSGLL LFLLLPPLLF
210 220 230 240 250
SHMEGWSYTE GFYFAFITLS TVGFGDYVIG MNPSQRYPLW YKNMVSLWIL
260 270 280 290 300
FGMAWLALII KLILSQLETP GRVCSCCHHS SKEDFKSQSW RQGPDREPES
310 320 330
HSPQQGCYPE GPMGIIQHLE PSAHAAGCGK DS
Length:332
Mass (Da):36,895
Last modified:December 1, 2001 - v1
Checksum:i1848DBC06E078158
GO
Isoform 2 (identifier: Q96T54-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-332: GMNPSQRYPL...AHAAGCGKDS → ASCLISDTRK...FLAGHGGSHL

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:271
Mass (Da):29,972
Checksum:iA6FD5ECA6E494D5D
GO

Sequence cautioni

The sequence AAK28551.1 differs from that shown. Reason: Frameshift at position 260. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211S → G.2 Publications
Corresponds to variant rs10947804 [ dbSNP | Ensembl ].
VAR_032362
Natural varianti253 – 2531M → L.
Corresponds to variant rs35677794 [ dbSNP | Ensembl ].
VAR_032363
Natural varianti296 – 2961R → Q.
Corresponds to variant rs2758910 [ dbSNP | Ensembl ].
VAR_024683

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei230 – 332103GMNPS…CGKDS → ASCLISDTRKPNRDWQTLER TSKSSGGLLKYRFLAGHGGS HL in isoform 2. CuratedVSP_047354Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF358910 mRNA. Translation: AAK49533.1.
AF339912 mRNA. Translation: AAK28551.1. Frameshift.
AY358853 mRNA. Translation: AAQ89212.1.
AL136087 Genomic DNA. Translation: CAI19536.1.
BC025726 mRNA. Translation: AAH25726.1.
CCDSiCCDS47419.1. [Q96T54-4]
CCDS4842.1. [Q96T54-3]
RefSeqiNP_001128583.1. NM_001135111.1. [Q96T54-4]
NP_113648.2. NM_031460.3. [Q96T54-3]
UniGeneiHs.162282.

Genome annotation databases

EnsembliENST00000373231; ENSP00000362328; ENSG00000124780. [Q96T54-3]
ENST00000453413; ENSP00000401271; ENSG00000124780. [Q96T54-4]
GeneIDi89822.
KEGGihsa:89822.
UCSCiuc003ooo.3. human. [Q96T54-3]

Polymorphism databases

DMDMi24636280.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF358910 mRNA. Translation: AAK49533.1.
AF339912 mRNA. Translation: AAK28551.1. Frameshift.
AY358853 mRNA. Translation: AAQ89212.1.
AL136087 Genomic DNA. Translation: CAI19536.1.
BC025726 mRNA. Translation: AAH25726.1.
CCDSiCCDS47419.1. [Q96T54-4]
CCDS4842.1. [Q96T54-3]
RefSeqiNP_001128583.1. NM_001135111.1. [Q96T54-4]
NP_113648.2. NM_031460.3. [Q96T54-3]
UniGeneiHs.162282.

3D structure databases

ProteinModelPortaliQ96T54.
SMRiQ96T54. Positions 36-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124608. 1 interaction.

Protein family/group databases

TCDBi1.A.1.9.6. the voltage-gated ion channel (vic) superfamily.

Polymorphism databases

DMDMi24636280.

Proteomic databases

PaxDbiQ96T54.
PRIDEiQ96T54.

Protocols and materials databases

DNASUi89822.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373231; ENSP00000362328; ENSG00000124780. [Q96T54-3]
ENST00000453413; ENSP00000401271; ENSG00000124780. [Q96T54-4]
GeneIDi89822.
KEGGihsa:89822.
UCSCiuc003ooo.3. human. [Q96T54-3]

Organism-specific databases

CTDi89822.
GeneCardsiGC06M039266.
HGNCiHGNC:14465. KCNK17.
HPAiHPA043892.
MIMi607370. gene.
neXtProtiNX_Q96T54.
PharmGKBiPA30058.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG317582.
GeneTreeiENSGT00760000118858.
HOGENOMiHOG000074161.
HOVERGENiHBG052240.
InParanoidiQ96T54.
KOiK04925.
OMAiSMGRWEF.
OrthoDBiEOG77M8NK.
PhylomeDBiQ96T54.
TreeFamiTF313947.

Enzyme and pathway databases

ReactomeiREACT_75850. TWIK-related alkaline pH activated K+ channel (TALK).

Miscellaneous databases

GeneWikiiKCNK17.
GenomeRNAii89822.
NextBioi76303.
PROiQ96T54.
SOURCEiSearch...

Gene expression databases

BgeeiQ96T54.
CleanExiHS_KCNK17.
GenevestigatoriQ96T54.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR013099. 2pore_dom_K_chnl_dom.
IPR003092. 2pore_dom_K_chnl_TASK.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PIRSFiPIRSF038061. K_channel_subfamily_K_type. 1 hit.
PRINTSiPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic and functional characteristics of novel human pancreatic 2P domain K(+) channels."
    Girard C., Duprat F., Terrenoire C., Tinel N., Fosset M., Romey G., Lazdunski M., Lesage F.
    Biochem. Biophys. Res. Commun. 282:249-256(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  2. "Characterization of TASK-4, a novel member of the pH-sensitive, two-pore domain potassium channel family."
    Decher N., Maier M., Dittrich W., Gassenhuber J., Brueggemann A., Busch A.E., Steinmeyer K.
    FEBS Lett. 492:84-89(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-21.
    Tissue: Adrenal gland.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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.
    , 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].
  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], VARIANT GLY-21.
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiKCNKH_HUMAN
AccessioniPrimary (citable) accession number: Q96T54
Secondary accession number(s): E9PB46
, Q5TCF4, Q8TAW4, Q9BXD1, Q9H592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: December 1, 2001
Last modified: January 7, 2015
This is version 122 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 Ba2+, quinidine, chloroform and halothane. Activated at alkaline pH. Activated by quinine and isoflurane.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.