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Q03717 (KCNB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily B member 1
Alternative name(s):
Voltage-gated potassium channel subunit Kv2.1
mShab
Gene names
Name:Kcnb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

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.

Post-translational modification

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.

Miscellaneous

Inhibited by tetraethylammonium chloride (TEA).

Sequence similarities

Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Amigo1Q80ZD84EBI-7511364,EBI-7511393

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Potassium voltage-gated channel subfamily B member 1
PRO_0000054043

Regions

Topological domain1 – 185185Cytoplasmic Potential
Transmembrane186 – 20621Helical; Name=Segment S1; Potential
Transmembrane229 – 24921Helical; Name=Segment S2; Potential
Topological domain250 – 25910Cytoplasmic Potential
Transmembrane260 – 28021Helical; Name=Segment S3; Potential
Transmembrane295 – 31521Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain316 – 33015Cytoplasmic Potential
Transmembrane331 – 35121Helical; Name=Segment S5; Potential
Intramembrane365 – 38521Pore-forming; Name=Segment H5; Potential
Transmembrane393 – 41321Helical; Name=Segment S6; Potential
Topological domain414 – 857444Cytoplasmic Potential
Motif377 – 3826Selectivity filter By similarity
Compositional bias517 – 5204Poly-Ser

Amino acid modifications

Modified residue151Phosphoserine By similarity
Modified residue1281Phosphotyrosine; by Src By similarity
Modified residue4571Phosphoserine By similarity
Modified residue4841Phosphoserine By similarity
Modified residue4961Phosphoserine By similarity
Modified residue5031Phosphoserine By similarity
Modified residue5201Phosphoserine By similarity
Modified residue5411Phosphoserine By similarity
Modified residue5671Phosphoserine By similarity
Modified residue5901Phosphoserine By similarity
Modified residue6071Phosphoserine By similarity
Modified residue6551Phosphoserine Ref.5
Modified residue7191Phosphoserine By similarity
Modified residue7711Phosphoserine By similarity
Modified residue7991Phosphoserine By similarity
Modified residue8041Phosphoserine By similarity
Modified residue8361Phosphothreonine By similarity

Experimental info

Sequence conflict7011A → R in AAA40112. Ref.1
Sequence conflict7731P → L in AAA40112. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03717 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 5FE2D80E58E60710

FASTA85795,591
        10         20         30         40         50         60 
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL 

        70         80         90        100        110        120 
RDCNTHDSLL QVCDDYSLED NEYFFDRHPG AFTSILNFYR TGRLHMMEEM CALSFSQELD 

       130        140        150        160        170        180 
YWGIDEIYLE SCCQARYHQK KEQMNEELKR EAETLREREG EEFDNTCCAE KRKKLWDLLE 

       190        200        210        220        230        240 
KPNSSVAAKI LAIISIMFIV LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF 

       250        260        270        280        290        300 
TMEYLLRFLS SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR 

       310        320        330        340        350        360 
IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF FAEKDEDDTK 

       370        380        390        400        410        420 
FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA GVLVIALPIP IIVNNFSEFY 

       430        440        450        460        470        480 
KEQKRQEKAI KRREALERAK RNGSIVSMNM KDAFARSIEM MDIVVEKNGE GVAKKDKVQD 

       490        500        510        520        530        540 
NHLSPNKWKW TKRALSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLQ DMYSKMAKTQ 

       550        560        570        580        590        600 
SQPILNTKEM APQSQPQEEL EMGSMPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE 

       610        620        630        640        650        660 
ATRFSHSPLA SLSGKSGGST APEVGWRGAL GASGGRLMET NPIPEASRSG FFVESPRSSM 

       670        680        690        700        710        720 
KTHNPMKLRA LKVNFLEGDP TPLLPALGLY HDPLRNRGGA AAAVAGLECA SLLDKPVLSP 

       730        740        750        760        770        780 
ESSIYTTASA RTPPRSPEKH TAIAFNFEAG VHQYIDTDTD DEGQLLYSVD SSPPKSLHGS 

       790        800        810        820        830        840 
TSPKFSLGAR TEKNHFESSP LPTSPKFLRP NCVYASEGLP GKGPGAQEKC KLENHTSPDV 

       850 
HMLPGGGAHG STRDQSI 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI56529.
RefSeqNP_032446.2. NM_008420.4.
UniGeneMm.205341.
Mm.490804.

3D structure databases

ProteinModelPortalQ03717.
SMRQ03717. Positions 2-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200886. 3 interactions.
IntActQ03717. 1 interaction.
MINTMINT-8298631.

Chemistry

GuidetoPHARMACOLOGY546.

PTM databases

PhosphoSiteQ03717.

Proteomic databases

PaxDbQ03717.
PRIDEQ03717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
GeneID16500.
KEGGmmu:16500.
UCSCuc008nzh.2. mouse.

Organism-specific databases

CTD3745.
MGIMGI:96666. Kcnb1.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000114905.
HOGENOMHOG000113206.
HOVERGENHBG052225.
InParanoidQ8K0D1.
KOK04885.
OMAKWKWTKR.
OrthoDBEOG7CRTPP.
TreeFamTF313103.

Gene expression databases

ArrayExpressQ03717.
BgeeQ03717.
GenevestigatorQ03717.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. 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]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF03521. Kv2channel. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01514. KV21CHANNEL.
PR01491. KVCHANNEL.
PR01495. SHABCHANNEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

ChiTaRSKCNB1. mouse.
NextBio289823.
PROQ03717.
SOURCESearch...

Entry information

Entry nameKCNB1_MOUSE
AccessionPrimary (citable) accession number: Q03717
Secondary accession number(s): Q8K0D1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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