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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
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KCNB1_RAT, Rattus norvegicus (Norway rat) Kcnb1 Voltage-gated potassium channel subunit Kv2.1 Functions
wild_type
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Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 Potassium voltage-gated channel subfamily B member 1;
Alternative name(s):
 Delayed rectifier potassium channel 1
Voltage-gated potassium channel subunit Kv2.1
Protein IDs
(Accession numbers)
UniProtKB
 P15387
NCBI RefSeq

NP_037318.1, NM_013186.1.
Organism
Latin Name/
(Common Name)
Rattus norvegicus (Rat).
Taxonomic Identifier (NCBI)
 10116
Gene Names
 Kcnb1 [GenPool]
GeneID

25736
Genome
Annotation (Ensembl)
Protein Sequence
 
SEQUENCE   857 AA;  95637 MW;  B3C5B0839AB15FD0 CRC64;
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL
RDCNTHDSLL QVCDDYSLED NEYFFDRHPG AFTSILNFYR TGRLHMMEEM CALSFSQELD
YWGIDEIYLE SCCQARYHQK KEQMNEELKR EAETLREREG EEFDNTCCAE KRKKLWDLLE
KPNSSVAAKI LAIISIMFIV LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF
TMEYLLRFLS SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF FAEKDEDDTK
FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA GVLVIALPIP IIVNNFSEFY
KEQKRQEKAI KRREALERAK RNGSIVSMNM KDAFARSIEM MDIVVEKNGE SIAKKDKVQD
NHLSPNKWKW TKRALSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYSKMAKTQ
SQPILNTKEM APQSKPPEEL EMSSMPSPVA PLPARTEGVI DMRSMSSIDS FISCATDFPE
ATRFSHSPLA SLSSKAGSST APEVGWRGAL GASGGRLTET NPIPETSRSG FFVESPRSSM
KTNNPLKLRA LKVNFVEGDP TPLLPSLGLY HDPLRNRGGA AAAVAGLECA SLLDKPVLSP
ESSIYTTASA RTPPRSPEKH TAIAFNFEAG VHHYIDTDTD DEGQLLYSVD SSPPKSLHGS
TSPKFSTGAR TEKNHFESSP LPTSPKFLRP NCVYSSEGLT GKGPGAQEKC KLENHTPPDV
HMLPGGGAHG STRDQSI
General annotation
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.
Cofactor
Subunit structure
 Heteromultimer with KCNG2, KCNG3, KCNG4, KCNS1, KCNS2, KCNS3 and KCNV2 (By similarity).
Subcellular location

Membrane; Multi-pass membrane protein.
Tissue specificity
 In the brain, the greatest density occurs in the cerebral cortex, followed by the hippocampus, cerebellum, and olfactory bulb. In peripheral tissues it is most prominent in retina and kidney. Also present in cardiac muscle tissue of the atrium and ventricle and in skeletal muscle.
Induction
Domain
 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 gradedactivity-dependent regulation of channel gating. Phosphorylationon Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as wellas the N-terminal Ser-15 are all regulated by calcineurin-mediateddephosphorylation. Particularly, Ser-607 and Tyr-128 aresignificant sites of voltage-gated regulation throughphosphorylation/ dephosphorylation activities. Tyr-128 can bedephosphorylated by PTPalpha and cyt-PTPepsilon. Phosphorylationlevels on Ser-607 are supersensitive to neuronal activity.Phosphorylation on Ser-567 is reduced during postnatal developmentwith low levels at P2 and P5. Levels then increase to reach adultlevels by P14. Phosphorylation levels on Ser-564 and Ser-607 aregreatly reduced during seizures, by 40% and 85% respectively.
Involvement in disease

References

  • "A novel potassium channel with delayed rectifier properties isolatedfrom rat brain by expression cloning.";,Frech G.C., Vandongen A.M.J., Schuster G., Brown A.M., Joho R.H.;,Nature 340:642-645(1989)., PubMeb:2770868 DOI:10.1038/340642a0

  • Frech G.C.;,Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.

  • "Distinct spatial and temporal expression patterns of K+ channel mRNAsfrom different subfamilies.";,Drewe J.A., Verma S., Frech G.C., Joho R.H.;,J. Neurosci. 12:538-548(1992)., PubMeb:1740690

  • "Phosphorylation of the Kv2.1 K+ channel alters voltage-dependentactivation.";,Murakoshi H., Shi G., Scannevin R.H., Trimmer J.S.;,Mol. Pharmacol. 52:821-828(1997)., PubMeb:9351973

  • "Phosphorylation-dependent regulation of Kv2.1 Channel activity attyrosine 124 by Src and by protein-tyrosine phosphatase epsilon.";,Tiran Z., Peretz A., Attali B., Elson A.;,J. Biol. Chem. 278:17509-17514(2003).,PubMeb:12615930 DOI:10.1074/jbc.M212766200

  • "Bidirectional activity-dependent regulation of neuronal ion channelphosphorylation.";,Misonou H., Menegola M., Mohapatra D.P., Guy L.K., Park K.-S.,Trimmer J.S.;,J. Neurosci. 26:13505-13514(2006).,PubMeb:17192433 DOI:10.1523/JNEUROSCI.3970-06.2006

  • "Graded regulation of the Kv2.1 potassium channel by variablephosphorylation.";,Park K.-S., Mohapatra D.P., Misonou H., Trimmer J.S.;,Science 313:976-979(2006).,PubMeb:16917065 DOI:10.1126/science.1124254

  • "Proteomic analyses of K(v)2.1 channel phosphorylation sitesdetermining cell background specific differences in function.";,Park K.S., Mohapatra D.P., Trimmer J.S.;,Channels 1:59-61(2007).,PubMeb:18690023

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Protein Domain Databases
InterPro

IPR000210, BTB/POZ-like.

IPR011333, BTB/POZ_fold.

IPR005821, Ion_trans.

IPR003091, K_chnl.

IPR003968, K_chnl_volt-dep_Kv.

IPR003973, K_chnl_volt-dep_Kv2.

IPR004350, K_chnl_volt-dep_Kv2.1.

IPR003131, K_chnl_volt-dep_Kv_tetra.
Gene3D

G3DSA:3.30.710.10, BTB/POZ_fold; 1.
PANTHER
Pfam

PF00520, Ion_trans; 1.

PF02214, K_tetra; 1.

PF03521, Kv2channel; 1.
PRINTS

PR00169, KCHANNEL.

PR01514, KV21CHANNEL.

PR01491, KVCHANNEL.

PR01495, SHABCHANNEL.
SUPFAM

SSF54695, BTB/POZ_fold; 1.
PROSITE
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
3LNM X-ray 2.90 A B/D 274-305 [>>]
Sequence
Annotation
Feature key
Position(s)
Length
Description
Polypeptide chain 1 - 857 857 Potassium voltage-gated channel subfamily /FTId=PRO_0000054046.
Topological domain 1 - 186 186 Cytoplasmic (Potential).
Topological domain 251 - 260 10 Cytoplasmic (Potential).
Topological domain 317 - 330 14 Cytoplasmic (Potential).
Topological domain 415 - 857 443 Cytoplasmic (Potential).
Transmembrane region 187 - 208 22 Helical; Name=Segment S1; (Potential).
Transmembrane region 229 - 250 22 Helical; Name=Segment S2; (Potential).
Transmembrane region 261 - 282 22 Helical; Name=Segment S3; (Potential).
Transmembrane region 295 - 316 22 Helical; Voltage-sensor; Name=Segment S4;
Transmembrane region 331 - 352 22 Helical; Name=Segment S5; (Potential).
Transmembrane region 393 - 414 22 Helical; Name=Segment S6; (Potential).
Located in a membrane without crossing it 365 - 385 21 Pore-forming; Name=Segment H5;
Sequence motif 377 - 382 6 Selectivity filter (By similarity).
Compositionally biased region 517 - 520 4 Poly-Ser.
Compositionally biased region 700 - 705 6 Poly-Ala.
Posttranslational modification of a residue 12 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 15 1 Phosphoserine.
Posttranslational modification of a residue 128 1 Phosphotyrosine; by Src.
Posttranslational modification of a residue 457 1 Phosphoserine.
Posttranslational modification of a residue 484 1 Phosphoserine.
Posttranslational modification of a residue 496 1 Phosphoserine.
Posttranslational modification of a residue 503 1 Phosphoserine.
Posttranslational modification of a residue 520 1 Phosphoserine.
Posttranslational modification of a residue 541 1 Phosphoserine.
Posttranslational modification of a residue 567 1 Phosphoserine.
Posttranslational modification of a residue 590 1 Phosphoserine.
Posttranslational modification of a residue 607 1 Phosphoserine.
Posttranslational modification of a residue 655 1 Phosphoserine.
Posttranslational modification of a residue 719 1 Phosphoserine.
Posttranslational modification of a residue 771 1 Phosphoserine.
Posttranslational modification of a residue 799 1 Phosphoserine.
Posttranslational modification of a residue 804 1 Phosphoserine.
Posttranslational modification of a residue 836 1 Phosphothreonine.
Mutagenesis 15 1 S->A: Shift in voltage-dependent gating
Mutagenesis 15 1 S->D: Resists voltage-dependent gating on
Mutagenesis 128 1 Y->F: Significant loss of Src-mediated
Mutagenesis 444 1 S->A: No effect on Src-mediated
Mutagenesis 457 1 S->A: Shift in voltage-dependent gating
Mutagenesis 457 1 S->D: Resists voltage-dependent gating on
Mutagenesis 484 1 S->A: No change in calcineurin-dependent
Mutagenesis 484 1 S->D: Resists voltage-dependent gating on
Mutagenesis 496 1 S->A: No effect on Src-mediated
Mutagenesis 541 1 S->A: Shift in voltage-dependent gating
Mutagenesis 541 1 S->D: Resists voltage-dependent gating on
Mutagenesis 567 1 S->A: Shift in voltage-dependent gating
Mutagenesis 567 1 S->D: Resists voltage-dependent gating on
Mutagenesis 607 1 S->A: Shift in voltage-dependent gating
Mutagenesis 607 1 S->D: Resists voltage-dependent gating on
Mutagenesis 655 1 S->A: Shift in voltage-dependent gating
Mutagenesis 655 1 S->D: Resists voltage-dependent gating on
Mutagenesis 719 1 S->A: Shift in voltage-dependent gating
Mutagenesis 771 1 S->A: No change in calcineurin-dependent
Mutagenesis 771 1 S->D: Resists voltage-dependent gating on
Mutagenesis 804 1 S->A: No change in calcineurin-dependent
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG052225
InParanoid
OMA
OrthoDB
Proteomics
Database (PRIDE)

P15387
Comparative
Toxicogenomics
Database (CTD)

3745
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