ID   KCNB1_HUMAN             Reviewed;         858 AA.
AC   Q14721; Q14193;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   11-JUL-2012, entry version 106.
DE   RecName: Full=Potassium voltage-gated channel subfamily B member 1;
DE   AltName: Full=Delayed rectifier potassium channel 1;
DE            Short=DRK1;
DE            Short=h-DRK1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv2.1;
GN   Name=KCNB1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94363205; PubMed=8081723;
RA   Albrecht B., Lorra C., Stocker K., Pongs O.;
RT   "Cloning and characterization of a human delayed rectifier potassium
RT   channel gene.";
RL   Recept. Channels 1:99-110(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain cortex;
RX   PubMed=1283219; DOI=10.1007/BF00370422;
RA   Ikeda S.R., Soler F., Zuhlke R.D., Joho R.H., Lewis D.L.;
RT   "Heterologous expression of the human potassium channel Kv2.1 in
RT   clonal mammalian cells by direct cytoplasmic microinjection of cRNA.";
RL   Pflugers Arch. 422:201-203(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens epithelium;
RA   Rae J.L., Shepard A.R.;
RT   "Identification of potassium channels in human lens epithelium.";
RL   (In) Civan M.M. (eds.);
RL   The eye's aqueous humor-from secretion to glaucoma, pp.69-104,
RL   Academic Press, San Diego (1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Channels open or close in
CC       response to the voltage difference across the membrane, letting
CC       potassium ions pass in accordance with their electrochemical
CC       gradient.
CC   -!- SUBUNIT: Heteromultimer with KCNG2, KCNG3, KCNG4, KCNS1, KCNS2,
CC       KCNS3 and KCNV2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments.
CC   -!- PTM: Highly phosphorylated on serine residues in the C-terminal.
CC       Differential phosphorylation on a subset of serines allows graded
CC       activity-dependent regulation of channel gating. Phosphorylation
CC       on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well
CC       as the N-terminal Ser-15 are all regulated by calcineurin-mediated
CC       dephosphorylation. Particularly, Ser-607 and Tyr-128 are
CC       significant sites of voltage-gated regulation through
CC       phosphorylation/ dephosphorylation activities. Tyr-128 can be
CC       dephosphorylated by PTPalpha and cyt-PTPepsilon. Phosphorylation
CC       levels on Ser-607 are supersensitive to neuronal activity.
CC       Phosphorylation on Ser-567 is reduced during postnatal development
CC       with low levels at P2 and P5. Levels then increase to reach adult
CC       levels by P14. Phosphorylation levels on Ser-564 and Ser-607 are
CC       greatly reduced during seizures, by 40% and 85% respectively (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. B (Shab)
CC       (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA36156.1; Type=Erroneous initiation;
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DR   EMBL; X68302; CAA48374.1; -; Genomic_DNA.
DR   EMBL; L02840; AAA36156.1; ALT_INIT; mRNA.
DR   EMBL; AF026005; AAB88808.1; -; mRNA.
DR   EMBL; AL035685; CAB89417.1; -; Genomic_DNA.
DR   IPI; IPI00033019; -.
DR   PIR; S31761; S31761.
DR   RefSeq; NP_004966.1; NM_004975.2.
DR   UniGene; Hs.84244; -.
DR   ProteinModelPortal; Q14721; -.
DR   SMR; Q14721; 30-423.
DR   IntAct; Q14721; 1.
DR   STRING; Q14721; -.
DR   TCDB; 1.A.1.2.11; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; Q14721; -.
DR   DMDM; 24418854; -.
DR   OGP; Q14721; -.
DR   PRIDE; Q14721; -.
DR   DNASU; 3745; -.
DR   Ensembl; ENST00000371741; ENSP00000360806; ENSG00000158445.
DR   GeneID; 3745; -.
DR   KEGG; hsa:3745; -.
DR   UCSC; uc002xur.1; human.
DR   CTD; 3745; -.
DR   GeneCards; GC20M047984; -.
DR   HGNC; HGNC:6231; KCNB1.
DR   HPA; CAB001979; -.
DR   MIM; 600397; gene.
DR   neXtProt; NX_Q14721; -.
DR   PharmGKB; PA209; -.
DR   eggNOG; COG1226; -.
DR   GeneTree; ENSGT00560000076807; -.
DR   HOGENOM; HOG000113206; -.
DR   HOVERGEN; HBG052225; -.
DR   InParanoid; Q14721; -.
DR   KO; K04885; -.
DR   OMA; IHQYIDA; -.
DR   OrthoDB; EOG4X6C7Q; -.
DR   PhylomeDB; Q14721; -.
DR   Reactome; REACT_111217; Metabolism.
DR   Reactome; REACT_13685; Neuronal System.
DR   NextBio; 14655; -.
DR   Bgee; Q14721; -.
DR   CleanEx; HS_KCNB1; -.
DR   Genevestigator; Q14721; -.
DR   GermOnline; ENSG00000158445; Homo sapiens.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003973; K_chnl_volt-dep_Kv2.
DR   InterPro; IPR004350; K_chnl_volt-dep_Kv2.1.
DR   InterPro; IPR003131; T1-type_BTB.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF03521; Kv2channel; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01514; KV21CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01495; SHABCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Ion transport; Ionic channel; Membrane;
KW   Phosphoprotein; Polymorphism; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    858       Potassium voltage-gated channel subfamily
FT                                B member 1.
FT                                /FTId=PRO_0000054042.
FT   TOPO_DOM      1    186       Cytoplasmic (Potential).
FT   TRANSMEM    187    208       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    229    250       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    251    260       Cytoplasmic (Potential).
FT   TRANSMEM    261    282       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    295    316       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    317    330       Cytoplasmic (Potential).
FT   TRANSMEM    331    352       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    365    385       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    393    414       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    415    858       Cytoplasmic (Potential).
FT   MOTIF       377    382       Selectivity filter (By similarity).
FT   COMPBIAS    517    520       Poly-Ser.
FT   COMPBIAS    701    706       Poly-Ala.
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphotyrosine; by Src (By similarity).
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   MOD_RES     484    484       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     503    503       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     590    590       Phosphoserine (By similarity).
FT   MOD_RES     607    607       Phosphoserine (By similarity).
FT   MOD_RES     656    656       Phosphoserine (By similarity).
FT   MOD_RES     720    720       Phosphoserine (By similarity).
FT   MOD_RES     772    772       Phosphoserine (By similarity).
FT   MOD_RES     800    800       Phosphoserine (By similarity).
FT   MOD_RES     805    805       Phosphoserine (By similarity).
FT   VARIANT     616    616       T -> N (in dbSNP:rs2229006).
FT                                /FTId=VAR_062182.
FT   VARIANT     616    616       T -> S (in dbSNP:rs2229006).
FT                                /FTId=VAR_062183.
FT   VARIANT     825    825       P -> S (in dbSNP:rs34467662).
FT                                /FTId=VAR_034049.
FT   VARIANT     857    857       S -> N (in dbSNP:rs34280195).
FT                                /FTId=VAR_062184.
SQ   SEQUENCE   858 AA;  95878 MW;  C4B426174ED0DEE4 CRC64;
     MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL
     RDCNTHDSLL EVCDDYSLDD 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 NMGKKDKVQD
     NHLSPNKWKW TKRTLSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYNKMAKTQ
     SQPILNTKES AAQSKPKEEL EMESIPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
     ATRFSHSPLT SLPSKTGGST APEVGWRGAL GASGGRFVEA NPSPDASQHS SFFIESPKSS
     MKTNNPLKLR ALKVNFMEGD PSPLLPVLGM YHDPLRNRGS AAAAVAGLEC ATLLDKAVLS
     PESSIYTTAS AKTPPRSPEK HTAIAFNFEA GVHQYIDADT DDEGQLLYSV DSSPPKSLPG
     STSPKFSTGT RSEKNHFESS PLPTSPKFLR QNCIYSTEAL TGKGPSGQEK CKLENHISPD
     VRVLPGGGAH GSTRDQSI
//