Protein detail

KCNK9

Potassium channel subfamily K member 9 (Acid-sensitive potassium channel protein TASK-3) (TWIK-related acid-sensitive K(+) channel 3) (Two pore potassium channel KT3.2) (Two pore K(+) channel KT3.2)

Entry name
KCNK9
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
4
Protein classification
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Potassium channel subfamily K member 9 (Acid-sensitive potassium channel protein TASK-3) (TWIK-related acid-sensitive K(+) channel 3) (Two pore potassium channel KT3.2) (Two pore K(+) channel KT3.2)
Protein Function
  • Voltage-gated ion channels:Two-P Potassium Channels
  • Transporters:Transporter channels and pores
  • Human disease related genes:Congenital malformations:Other congenital malformations
  • Disease related genes
  • FDA approved drug targets:Small molecule drugs
Transmembrane
9..29; Helical; 108..128; Helical; 159..179; Helical; 219..239; Helical
Transmembrane Count
4
Entrez Gene Symbol
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
KCNK9 fluorescence
Cell SpecificEsophageal apical cellsSingle-Nuclei Brain Specificcentral nervous system macrophage
Function & Pathway
Protein Function
  • Voltage-gated ion channels:Two-P Potassium Channels
  • Transporters:Transporter channels and pores
  • Human disease related genes:Congenital malformations:Other congenital malformations
  • Disease related genes
  • FDA approved drug targets:Small molecule drugs
Canonical Pathways
  • M212 Pid integrin5 pathway
  • M185 Pid alk1 pathway
  • M33 Pid glypican 1pathway
Mediation Categories
Fusion and delivery mediation
Relations & Evidence

Enzyme-Mediated Modification

2 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
KCNK9PRKACAP17612S373phosphorylationPhosphoSite_MIMPMIMPProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:21357689
KCNK9PRKCAP17252T341phosphorylationPhosphoSite

Ligand-Receptor Signaling

24 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transportertransporterOmniPathNoYesNoNoNo
ion_channelion_channelOmniPathNoYesNoNoNo
transmembranetransmembraneUniProt_locationNoNoNoNoNo
transmembranetransmembraneUniProt_topologyNoNoNoNoNo
transmembranetransmembraneUniProt_keywordNoNoNoNoNo
transmembranetransmembraneTopDBNoNoNoNoNo
transmembranetransmembraneRamilowski_locationNoNoNoNoNo
transmembranetransmembraneOmniPathNoNoNoNoNo
peripheralperipheralUniProt_topologyNoNoNoNoNo
peripheralperipheralOmniPathNoNoNoNoNo
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Regulatory Interaction Network

2 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
KAPCAP17612KCNK9Q9NPC2YesYesNoPhosphoSite_MIMPMIMPPhosphoSite_norefSIGNORiPTMnetProtMapperSIGNOR_ProtMapperPhosphoSite_ProtMapperSIGNOR:21357689ProtMapper:21357689
KPCAP17252KCNK9Q9NPC2YesNoNoPhosphoSitePhosphoSite_ProtMapperProtMapperPhosphoSite:17374744

Protein Complex Composition

7 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
EXO1KCNK15KCNK9MAP3K2PDXKRPS6KA1SFNTSC1TSC2YWHABYWHAEYWHAGYWHAHYWHAQYWHAZO00764P27348P31946P31947P49815P61981P62258P63104Q04917Q15418Q92574Q9H427Q9NPC2Q9UQ84Q9Y2U51:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8590
DCAF7DYRK1AEXO1HSPA1BKCNK15KCNK3KCNK9PI4KBSFNYWHABYWHAEYWHAGYWHAHYWHAQYWHAZO14649P0DMV9P27348P31946P31947P61962P61981P62258P63104Q04917Q13627Q9H427Q9NPC2Q9UBF8Q9UQ841:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC6990
EXO1HSPA8KCNK15KCNK3KCNK9MAP3K2MAP3K5MAPK8SFNYWHABYWHAEYWHAGYWHAHYWHAQYWHAZO14649P11142P27348P31946P31947P45983P61981P62258P63104Q04917Q99683Q9H427Q9NPC2Q9UQ84Q9Y2U51:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8687
EXO1IARS2KCNK15KCNK9PI4KBSFNTBC1D13TSC1TSC2YWHABYWHAEYWHAGYWHAHYWHAQYWHAZP27348P31946P31947P49815P61981P62258P63104Q04917Q92574Q9H427Q9NPC2Q9NSE4Q9NVG8Q9UBF8Q9UQ841:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC4411
DCAF7DYRK1AEXO1FBXO8HIPK3KCNK15KCNK9PI4KBSFNYWHABYWHAEYWHAGYWHAHYWHAQYWHAZP27348P31946P31947P61962P61981P62258P63104Q04917Q13627Q9H422Q9H427Q9NPC2Q9NRD0Q9UBF8Q9UQ841:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC5582
KCNK9SFNP31947Q9NPC21:1PDBPDB:6ghpPDB:3smlPDB:3p1sPDB:3p1oPDB:3p1nPDB:3smmPDB:3smkPDB:3p1rPDB:3p1qPDB:3smoPDB:3p1pPDB:3ux0PDB:4fr3PDB:3sp5PDB:3sprPDB:3smn
KCNK9Q9NPC22PDBPDB:8k1zPDB:9g9wPDB:8k1vPDB:8k1qPDB:9g9vPDB:8k1j

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry๏ผ›Western blotting23999659038037300
Sequence, Structure & Domains

Sequences

Length
374
Mass
42,264
Sequence
MKRQNVRTLSLIVCTFTYLLVGAAVFDALESDHEMREEEKLKAEEIRIKGKYNISSEDYRQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTDVSMENMVTVGFFSCMGTLCIGAAAFSQCEEWSFFHAYYYCFITLTTIGFGDYVALQTKGALQKKPLYVAFSFMYILVGLTVIGAFLNLVVLRFLTMNSEDERRDAEERASLAGNRNSMVIHIPEEPRPSRPRYKADVPDLQSVCSCTCYRSQDYGGRSVAPQNSFSAKLAPHYFHSISYKIEEISPSTLKNSLFPSPISSISPGLHSFTDHQRLMKRRKSV

3D Structural Models

Helix
3..52; 56..73; 80..91; 104..146; 156..181; 186..197; 213..216; 218..247; 249..256
Beta Strand
77..79
3D Structure
Electron microscopy (6); X-ray crystallography (16)

Domain & Motif Annotations

Domain (CC)
Each subunit contributes two pore-forming domains 1 and 2 which assemble to form a single pore with M2 and M4 transmembrane helices lining the central cavity and M1 and M3 facing the lipid bilayer. The transmembrane helices are bridged by the selectivity filters 1 and 2 carrying a signature sequence TxTTxG(Y/F)G(D/H) that coordinate the permeant ions. Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation.; DOMAIN: The X-gate is positioned at the distal ends of M4 transmembrane helices forming a two-turn-helical structure with the methyl group of Thr-248 closing the ion conduction pathway.
Region
93..98; Selectivity filter 1; 199..204; Selectivity filter 2; 243..248; X-gate
Protein Families
Two pore domain potassium channel (TC 1.A.1.8) family
Sequence Similarities
Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.
Clinical Relevance