Protein detail

KCNB2

Potassium voltage-gated channel subfamily B member 2 (Voltage-gated potassium channel subunit Kv2.2)

Entry name
KCNB2
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
6
Protein classification
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Potassium voltage-gated channel subfamily B member 2 (Voltage-gated potassium channel subunit Kv2.2)
Protein Function
  • Transporters:Transporter channels and pores
  • Voltage-gated ion channels:Voltage-Gated Potassium Channels
  • FDA approved drug targets:Small molecule drugs
Transmembrane
191..212; Helical; Name=Segment S1; 233..254; Helical; Name=Segment S2; 266..284; Helical; Name=Segment S3; 297..317; Helical; Voltage-sensor; Name=Segment S4; 333..354; Helical; Name=Segment S5; 396..424; Helical; Name=Segment S6
Transmembrane Count
6
Entrez Gene Symbol
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Tissue SpecificbrainCell SpecificBrain excitatory neurons
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

25 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
voltage_gatedion_channelAlmen2009NoYesNoNoNo
transportertransporterOmniPathNoYesNoNoNo
ion_channelion_channelOmniPathNoYesNoNoNo
transmembranetransmembraneUniProt_locationNoNoNoNoNo
transmembranetransmembraneUniProt_topologyNoNoNoNoNo
transmembranetransmembraneUniProt_keywordNoNoNoNoNo
transmembranetransmembraneLOCATENoNoNoNoNo
transmembranetransmembraneRamilowski_locationNoNoNoNoNo
transmembranetransmembraneOmniPathNoNoNoNoNo
peripheralperipheralUniProt_topologyNoNoNoNoNo
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Regulatory Interaction Network

2 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
KCNB2Q92953VAPAQ9P0L0YesYesNoSIGNORSIGNOR:29941597
KCNB2Q92953VAPBO95292YesYesNoSIGNORSIGNOR:29941597

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry;Western blotting;Immunoelectron Microscopy439766158399409232898658527894104
Sequence, Structure & Domains

Sequences

Length
911
Mass
102,563
Sequence
MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPDKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQETDEFGQLNDNRQLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSADDNHLSPSRWKWARKALSETSSNKSFENKYQEVSQKDSHEQLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEKPERPSAYEEEIEMEEVVCPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTEEHQRARGPPFLTLSREKGPAARDGTLEYAPVDITVNLDASGSQCGLHSPLQSDNATDSPKSSLKGSNPLKSRSLKVNFKENRGSAPQTPPSTARPLPVTTADFSLTTPQHISTILLEETPSQGDRPLLGTEVSAPCQGPSKGLSPRFPKQKLFPFSSRERRSFTEIDTGDDEDFLELPGAREEKQVDSSPNCFADKPSDGRDPLREEGSVGSSSPQDTGHNCRQDIYHAVSEVKKDSSQEGCKMENHLFAPEIHSNPGDTGYCPTRETSM

3D Structural Models

Domain & Motif Annotations

Compositional Bias
508..522; Basic and acidic residues; 523..534; Polar residues; 560..569; Basic and acidic residues; 685..711; Polar residues; 837..849; Basic and acidic residues; 851..860; Polar residues
Motif
381..386; Selectivity filter; 605..611; FFAT
Domain (CC)
The transmembrane segment S4 functions as a voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.; DOMAIN: The FFAT motif is involved in the interaction with VAPA and VAPB and its phosphorylation regulates these interactions.
Region
1..22; Disordered; 503..534; Disordered; 549..571; Disordered; 637..665; Disordered; 685..739; Disordered; 760..865; Disordered; 892..911; Disordered
Protein Families
  • Potassium channel family
  • B (Shab) (TC 1.A.1.2) subfamily
  • Kv2.2/KCNB2 sub-subfamily
Sequence Similarities
Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily.
Clinical Relevance