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Protein

Potassium voltage-gated channel subfamily B member 1

Gene

Kcnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the voltage-dependent potassium ion permeability of excitable membranes. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient.

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: GO_Central
  2. outward rectifier potassium channel activity Source: Ensembl
  3. voltage-gated potassium channel activity Source: MGI

GO - Biological processi

  1. potassium ion transmembrane transport Source: GO_Central
  2. potassium ion transport Source: MGI
  3. protein homooligomerization Source: InterPro
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_199077. Voltage gated Potassium channels.
REACT_248547. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily B member 1
Alternative name(s):
Voltage-gated potassium channel subunit Kv2.1
mShab
Gene namesi
Name:Kcnb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:96666. Kcnb1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 185185CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei186 – 20621Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei229 – 24921Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Topological domaini250 – 25910CytoplasmicSequence Analysis
Transmembranei260 – 28021Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei295 – 31521Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Topological domaini316 – 33015CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei331 – 35121Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Intramembranei365 – 38521Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Transmembranei393 – 41321Helical; Name=Segment S6Sequence AnalysisAdd
BLAST
Topological domaini414 – 857444CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. dendrite membrane Source: Ensembl
  3. integral component of membrane Source: GO_Central
  4. neuronal cell body membrane Source: Ensembl
  5. postsynaptic membrane Source: Ensembl
  6. voltage-gated potassium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 857857Potassium voltage-gated channel subfamily B member 1PRO_0000054043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei128 – 1281Phosphotyrosine; by SrcBy similarity
Modified residuei457 – 4571PhosphoserineBy similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei496 – 4961PhosphoserineBy similarity
Modified residuei503 – 5031PhosphoserineBy similarity
Modified residuei520 – 5201PhosphoserineBy similarity
Modified residuei541 – 5411PhosphoserineBy similarity
Modified residuei567 – 5671PhosphoserineBy similarity
Modified residuei590 – 5901PhosphoserineBy similarity
Modified residuei607 – 6071PhosphoserineBy similarity
Modified residuei655 – 6551Phosphoserine1 Publication
Modified residuei719 – 7191PhosphoserineBy similarity
Modified residuei771 – 7711PhosphoserineBy similarity
Modified residuei799 – 7991PhosphoserineBy similarity
Modified residuei804 – 8041PhosphoserineBy similarity
Modified residuei836 – 8361PhosphothreonineBy similarity

Post-translational modificationi

Highly phosphorylated on serine residues in the C-terminal. Differential phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are all regulated by calcineurin-mediated dephosphorylation. Particularly, Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/ dephosphorylation activities. Tyr-128 can be dephosphorylated by PTPalpha and cyt-PTPepsilon. Phosphorylation levels on Ser-607 are supersensitive to neuronal activity. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5. Levels then increase to reach adult levels by P14. Phosphorylation levels on Ser-564 and Ser-607 are greatly reduced during seizures, by 40% and 85% respectively.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03717.
PaxDbiQ03717.
PRIDEiQ03717.

PTM databases

PhosphoSiteiQ03717.

Expressioni

Gene expression databases

BgeeiQ03717.
ExpressionAtlasiQ03717. baseline and differential.
GenevestigatoriQ03717.

Interactioni

Subunit structurei

Heteromultimer with KCNG2, KCNG3, KCNG4, KCNS1, KCNS2, KCNS3 and KCNV2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Amigo1Q80ZD84EBI-7511364,EBI-7511393

Protein-protein interaction databases

BioGridi200886. 3 interactions.
IntActiQ03717. 1 interaction.
MINTiMINT-8298631.

Structurei

3D structure databases

ProteinModelPortaliQ03717.
SMRiQ03717. Positions 30-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi377 – 3826Selectivity filterBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi517 – 5204Poly-Ser

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000113206.
HOVERGENiHBG052225.
InParanoidiQ03717.
KOiK04885.
OMAiTEGVIDM.
OrthoDBiEOG7CRTPP.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003973. K_chnl_volt-dep_Kv2.
IPR004350. K_chnl_volt-dep_Kv2.1.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF03521. Kv2channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01514. KV21CHANNEL.
PR01491. KVCHANNEL.
PR01495. SHABCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

Q03717-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD
60 70 80 90 100
RLPRTRLGKL RDCNTHDSLL QVCDDYSLED NEYFFDRHPG AFTSILNFYR
110 120 130 140 150
TGRLHMMEEM CALSFSQELD YWGIDEIYLE SCCQARYHQK KEQMNEELKR
160 170 180 190 200
EAETLREREG EEFDNTCCAE KRKKLWDLLE KPNSSVAAKI LAIISIMFIV
210 220 230 240 250
LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF TMEYLLRFLS
260 270 280 290 300
SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
310 320 330 340 350
IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF
360 370 380 390 400
FAEKDEDDTK FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA
410 420 430 440 450
GVLVIALPIP IIVNNFSEFY KEQKRQEKAI KRREALERAK RNGSIVSMNM
460 470 480 490 500
KDAFARSIEM MDIVVEKNGE GVAKKDKVQD NHLSPNKWKW TKRALSETSS
510 520 530 540 550
SKSFETKEQG SPEKARSSSS PQHLNVQQLQ DMYSKMAKTQ SQPILNTKEM
560 570 580 590 600
APQSQPQEEL EMGSMPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
610 620 630 640 650
ATRFSHSPLA SLSGKSGGST APEVGWRGAL GASGGRLMET NPIPEASRSG
660 670 680 690 700
FFVESPRSSM KTHNPMKLRA LKVNFLEGDP TPLLPALGLY HDPLRNRGGA
710 720 730 740 750
AAAVAGLECA SLLDKPVLSP ESSIYTTASA RTPPRSPEKH TAIAFNFEAG
760 770 780 790 800
VHQYIDTDTD DEGQLLYSVD SSPPKSLHGS TSPKFSLGAR TEKNHFESSP
810 820 830 840 850
LPTSPKFLRP NCVYASEGLP GKGPGAQEKC KLENHTSPDV HMLPGGGAHG

STRDQSI
Length:857
Mass (Da):95,591
Last modified:July 27, 2011 - v2
Checksum:i5FE2D80E58E60710
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti701 – 7011A → R in AAA40112. (PubMed:2002364)Curated
Sequence conflicti773 – 7731P → L in AAA40112. (PubMed:2002364)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64228 mRNA. Translation: AAA40112.1.
AL591854, AL591711 Genomic DNA. Translation: CAM13429.1.
AL591711, AL591854 Genomic DNA. Translation: CAM17304.1.
CH466551 Genomic DNA. Translation: EDL06500.1.
BC031776 mRNA. Translation: AAH31776.1.
BC061501 mRNA. Translation: AAH61501.1.
CCDSiCCDS17096.1.
PIRiI56529.
RefSeqiNP_032446.2. NM_008420.4.
UniGeneiMm.205341.
Mm.490804.

Genome annotation databases

EnsembliENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
GeneIDi16500.
KEGGimmu:16500.
UCSCiuc008nzh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64228 mRNA. Translation: AAA40112.1.
AL591854, AL591711 Genomic DNA. Translation: CAM13429.1.
AL591711, AL591854 Genomic DNA. Translation: CAM17304.1.
CH466551 Genomic DNA. Translation: EDL06500.1.
BC031776 mRNA. Translation: AAH31776.1.
BC061501 mRNA. Translation: AAH61501.1.
CCDSiCCDS17096.1.
PIRiI56529.
RefSeqiNP_032446.2. NM_008420.4.
UniGeneiMm.205341.
Mm.490804.

3D structure databases

ProteinModelPortaliQ03717.
SMRiQ03717. Positions 30-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200886. 3 interactions.
IntActiQ03717. 1 interaction.
MINTiMINT-8298631.

Chemistry

GuidetoPHARMACOLOGYi546.

PTM databases

PhosphoSiteiQ03717.

Proteomic databases

MaxQBiQ03717.
PaxDbiQ03717.
PRIDEiQ03717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
GeneIDi16500.
KEGGimmu:16500.
UCSCiuc008nzh.2. mouse.

Organism-specific databases

CTDi3745.
MGIiMGI:96666. Kcnb1.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000113206.
HOVERGENiHBG052225.
InParanoidiQ03717.
KOiK04885.
OMAiTEGVIDM.
OrthoDBiEOG7CRTPP.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_199077. Voltage gated Potassium channels.
REACT_248547. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Miscellaneous databases

ChiTaRSiKcnb1. mouse.
NextBioi289823.
PROiQ03717.
SOURCEiSearch...

Gene expression databases

BgeeiQ03717.
ExpressionAtlasiQ03717. baseline and differential.
GenevestigatoriQ03717.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003973. K_chnl_volt-dep_Kv2.
IPR004350. K_chnl_volt-dep_Kv2.1.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF03521. Kv2channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01514. KV21CHANNEL.
PR01491. KVCHANNEL.
PR01495. SHABCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mouse brain homolog of the Drosophila Shab K+ channel with conserved delayed-rectifier properties."
    Pak M.D., Covarrubias M., Ratcliffe A., Salkoff L.
    J. Neurosci. 11:869-880(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Eye.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.

Entry informationi

Entry nameiKCNB1_MOUSE
AccessioniPrimary (citable) accession number: Q03717
Secondary accession number(s): Q8K0D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibited by tetraethylammonium chloride (TEA).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.