Potassium voltage-gated channel subfamily B member 1

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Q03717 (KCNB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Potassium voltage-gated channel subfamily B member 1

Alternative name(s):
Voltage-gated potassium channel subunit Kv2.1
mShab

Gene names

Name:

Kcnb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
Protein existence	Evidence 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]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from electronic annotation. Source: InterPro
Cellular_component	dendrite Inferred from electronic annotation. Source: Compara dendrite membrane Inferred from electronic annotation. Source: Compara neuronal cell body membrane Inferred from electronic annotation. Source: Compara postsynaptic membrane Inferred from electronic annotation. Source: Compara voltage-gated potassium channel complex Inferred from electronic annotation. Source: InterPro
Molecular_function	delayed rectifier potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome outward rectifier potassium channel activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 857

857

Potassium voltage-gated channel subfamily B member 1

PRO_0000054043

Regions

Topological domain

1 – 185

185

Cytoplasmic Potential

Transmembrane

186 – 206

Helical; Name=Segment S1; Potential

Transmembrane

229 – 249

Helical; Name=Segment S2; Potential

Topological domain

250 – 259

Cytoplasmic Potential

Transmembrane

260 – 280

Helical; Name=Segment S3; Potential

Transmembrane

295 – 315

Helical; Voltage-sensor; Name=Segment S4; Potential

Topological domain

316 – 330

Cytoplasmic Potential

Transmembrane

331 – 351

Helical; Name=Segment S5; Potential

Intramembrane

365 – 385

Pore-forming; Name=Segment H5; Potential

Transmembrane

393 – 413

Helical; Name=Segment S6; Potential

Topological domain

414 – 857

444

Cytoplasmic Potential

Motif

377 – 382

Selectivity filter By similarity

Compositional bias

517 – 520

Poly-Ser

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine By similarity

Modified residue

128

Phosphotyrosine; by Src By similarity

Modified residue

457

Phosphoserine By similarity

Modified residue

484

Phosphoserine By similarity

Modified residue

496

Phosphoserine By similarity

Modified residue

503

Phosphoserine By similarity

Modified residue

520

Phosphoserine By similarity

Modified residue

541

Phosphoserine By similarity

Modified residue

567

Phosphoserine By similarity

Modified residue

590

Phosphoserine By similarity

Modified residue

607

Phosphoserine By similarity

Modified residue

655

Phosphoserine Ref.5 Ref.6

Modified residue

719

Phosphoserine By similarity

Modified residue

771

Phosphoserine By similarity

Modified residue

799

Phosphoserine By similarity

Modified residue

804

Phosphoserine By similarity

Modified residue

836

Phosphothreonine By similarity

Experimental info

Sequence conflict

701

A → R in AAA40112. Ref.1

Sequence conflict

773

P → L in AAA40112. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q03717 [UniParc].

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

857

95,591

        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' referencesShow '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. 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, MASS SPECTROMETRY. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-655, MASS SPECTROMETRY. 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.
IPI	IPI00135596.
PIR	I56529.
RefSeq	NP_032446.2. NM_008420.4.
UniGene	Mm.205341. Mm.490804.
3D structure databases
ProteinModelPortal	Q03717.
SMR	Q03717. Positions 30-462.
ModBase	Search...
PTM databases
PhosphoSite	Q03717.
Proteomic databases
PaxDb	Q03717.
PRIDE	Q03717.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
GeneID	16500.
KEGG	mmu:16500.
Organism-specific databases
CTD	3745.
MGI	MGI:96666. Kcnb1.
Phylogenomic databases
eggNOG	COG1226.
GeneTree	ENSGT00690000101842.
HOGENOM	HOG000113206.
HOVERGEN	HBG052225.
InParanoid	Q8K0D1.
KO	K04885.
OMA	QLEDMYN.
OrthoDB	EOG4X6C7Q.
Gene expression databases
ArrayExpress	Q03717.
Bgee	Q03717.
Genevestigator	Q03717.
GermOnline	ENSMUSG00000050556. Mus musculus.
Family and domain databases
Gene3D	3.30.710.10. 1 hit.
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. 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. [Graphical view]
PANTHER	PTHR11537. PTHR11537. 1 hit.
Pfam	PF00520. Ion_trans. 1 hit. PF02214. K_tetra. 1 hit. PF03521. Kv2channel. 1 hit. [Graphical view]
PRINTS	PR00169. KCHANNEL. PR01514. KV21CHANNEL. PR01491. KVCHANNEL. PR01495. SHABCHANNEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	KCNB1. mouse.
NextBio	289823.
SOURCE	Search...

Entry information

Entry name

KCNB1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents