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Q14721 (KCNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
Delayed rectifier potassium channel 1
Short name=DRK1
Short name=h-DRK1
Voltage-gated potassium channel subunit Kv2.1
Gene names
Name:KCNB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length858 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-656 and Ser-720 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 By similarity.

Sequence similarities

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

Sequence caution

The sequence AAA36156.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processenergy reserve metabolic process

Traceable author statement. Source: Reactome

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

regulation of insulin secretion

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentdendrite

Inferred from electronic annotation. Source: Ensembl

dendrite membrane

Inferred from electronic annotation. Source: Ensembl

neuronal cell body membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

voltage-gated potassium channel complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondelayed rectifier potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

outward rectifier potassium channel activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 10484328PubMed 11852086. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 858858Potassium voltage-gated channel subfamily B member 1
PRO_0000054042

Regions

Topological domain1 – 186186Cytoplasmic Potential
Transmembrane187 – 20822Helical; Name=Segment S1; Potential
Transmembrane229 – 25022Helical; Name=Segment S2; Potential
Topological domain251 – 26010Cytoplasmic Potential
Transmembrane261 – 28222Helical; Name=Segment S3; Potential
Transmembrane295 – 31622Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain317 – 33014Cytoplasmic Potential
Transmembrane331 – 35222Helical; Name=Segment S5; Potential
Intramembrane365 – 38521Pore-forming; Name=Segment H5; Potential
Transmembrane393 – 41422Helical; Name=Segment S6; Potential
Topological domain415 – 858444Cytoplasmic Potential
Motif377 – 3826Selectivity filter By similarity
Compositional bias517 – 5204Poly-Ser
Compositional bias701 – 7066Poly-Ala

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 residue6561Phosphoserine By similarity
Modified residue7201Phosphoserine By similarity
Modified residue7721Phosphoserine By similarity
Modified residue8001Phosphoserine By similarity
Modified residue8051Phosphoserine By similarity

Natural variations

Natural variant6161T → N.
Corresponds to variant rs2229006 [ dbSNP | Ensembl ].
VAR_062182
Natural variant6161T → S.
Corresponds to variant rs2229006 [ dbSNP | Ensembl ].
VAR_062183
Natural variant8251P → S.
Corresponds to variant rs34467662 [ dbSNP | Ensembl ].
VAR_034049
Natural variant8571S → N.
Corresponds to variant rs34280195 [ dbSNP | Ensembl ].
VAR_062184

Sequences

Sequence LengthMass (Da)Tools
Q14721 [UniParc].

Last modified October 25, 2002. Version 2.
Checksum: C4B426174ED0DEE4

FASTA85895,878
        10         20         30         40         50         60 
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL 

        70         80         90        100        110        120 
RDCNTHDSLL EVCDDYSLDD 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 NMGKKDKVQD 

       490        500        510        520        530        540 
NHLSPNKWKW TKRTLSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYNKMAKTQ 

       550        560        570        580        590        600 
SQPILNTKES AAQSKPKEEL EMESIPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE 

       610        620        630        640        650        660 
ATRFSHSPLT SLPSKTGGST APEVGWRGAL GASGGRFVEA NPSPDASQHS SFFIESPKSS 

       670        680        690        700        710        720 
MKTNNPLKLR ALKVNFMEGD PSPLLPVLGM YHDPLRNRGS AAAAVAGLEC ATLLDKAVLS 

       730        740        750        760        770        780 
PESSIYTTAS AKTPPRSPEK HTAIAFNFEA GVHQYIDADT DDEGQLLYSV DSSPPKSLPG 

       790        800        810        820        830        840 
STSPKFSTGT RSEKNHFESS PLPTSPKFLR QNCIYSTEAL TGKGPSGQEK CKLENHISPD 

       850 
VRVLPGGGAH GSTRDQSI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a human delayed rectifier potassium channel gene."
Albrecht B., Lorra C., Stocker K., Pongs O.
Recept. Channels 1:99-110(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Heterologous expression of the human potassium channel Kv2.1 in clonal mammalian cells by direct cytoplasmic microinjection of cRNA."
Ikeda S.R., Soler F., Zuhlke R.D., Joho R.H., Lewis D.L.
Pflugers Arch. 422:201-203(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain cortex.
[3]"Identification of potassium channels in human lens epithelium."
Rae J.L., Shepard A.R.
(In) Civan M.M. (eds.); The eye's aqueous humor-from secretion to glaucoma, pp.69-104, Academic Press, San Diego (1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens epithelium.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68302 Genomic DNA. Translation: CAA48374.1.
L02840 mRNA. Translation: AAA36156.1. Different initiation.
AF026005 mRNA. Translation: AAB88808.1.
AL035685 Genomic DNA. Translation: CAB89417.1.
CCDSCCDS13418.1.
PIRS31761.
RefSeqNP_004966.1. NM_004975.2.
XP_006723847.1. XM_006723784.1.
UniGeneHs.84244.

3D structure databases

ProteinModelPortalQ14721.
SMRQ14721. Positions 30-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109947. 16 interactions.
IntActQ14721. 1 interaction.
STRING9606.ENSP00000360806.

Chemistry

ChEMBLCHEMBL2362996.
GuidetoPHARMACOLOGY546.

Protein family/group databases

TCDB1.A.1.2.11. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ14721.

Polymorphism databases

DMDM24418854.

2D gel databases

OGPQ14721.

Proteomic databases

PaxDbQ14721.
PRIDEQ14721.

Protocols and materials databases

DNASU3745.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371741; ENSP00000360806; ENSG00000158445.
GeneID3745.
KEGGhsa:3745.
UCSCuc002xur.1. human.

Organism-specific databases

CTD3745.
GeneCardsGC20M047984.
HGNCHGNC:6231. KCNB1.
HPACAB001979.
MIM600397. gene.
neXtProtNX_Q14721.
PharmGKBPA209.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000113206.
HOVERGENHBG052225.
InParanoidQ14721.
KOK04885.
OMACATDFPE.
OrthoDBEOG7CRTPP.
PhylomeDBQ14721.
TreeFamTF313103.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

BgeeQ14721.
CleanExHS_KCNB1.
GenevestigatorQ14721.

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

GeneWikiKCNB1.
GenomeRNAi3745.
NextBio14655.
PROQ14721.
SOURCESearch...

Entry information

Entry nameKCNB1_HUMAN
AccessionPrimary (citable) accession number: Q14721
Secondary accession number(s): Q14193
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 25, 2002
Last modified: July 9, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM