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Protein

Potassium voltage-gated channel subfamily B member 1

Gene

Kcnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain (PubMed:14684365, PubMed:19383458, PubMed:24494598). Plays also a role in the regulation of exocytosis independently of its electrical function (By similarity). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:22056818). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (By similarity). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity). Channel properties are also modulated by cytoplasmic ancillary beta subunits, such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels (PubMed:22056818). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle (PubMed:10506487, PubMed:12270920, PubMed:17767909, PubMed:23161216, PubMed:24494598). Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation (By similarity). Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (PubMed:24494598). Contributes to the regulation of the glucose-induced amplitude and duration of action potentials in pancreatic beta-cells, hence limiting calcium influx and insulin secretion (PubMed:12270920, PubMed:17767909, PubMed:19383458, PubMed:23161216). Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells (By similarity). May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval (PubMed:10506487, PubMed:14684365). Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury (By similarity). May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (By similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits (By similarity). Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner (By similarity).By similarity8 Publications

Enzyme regulationi

Inhibited by 42 nM hanatoxin 1 (HaTx1), a spider venom toxin of the tarantula G.spatulata. Inhibited by 100 nM stromatoxin 1 (ScTx1), a spider venom toxin of the tarantula S.calceata (By similarity). Modestly sensitive to millimolar levels of tetraethylammonium (TEA) and 4-aminopyridine (4-AP) (PubMed:2002364, PubMed:10414301, PubMed:15858231). Completely insensitive to toxins such as dendrotoxin (DTX) and charybdotoxin (CTX) (By similarity).By similarity2 Publications1 Publication

Kineticsi

Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of more than 20 msec (PubMed:2002364). After that, inactivate very slowly, i.e within more than 5 sec (PubMed:2002364). Their activation requires low threshold potentials at about -20 to -30 mV with a midpoint activation at about 10 mV. For inactivation, the voltage at half-maximal amplitude is about -20 mV. The time constant for recovery after inactivation is about 1.6 sec. Channels have an unitary conductance of about 8 pS. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, the presence or absence of ancillary subunits and post-translational modifications.By similarity

2 Publications1 Publication

      GO - Molecular functioni

      GO - Biological processi

      Complete GO annotation...

      Keywords - Molecular functioni

      Ion channel, Potassium channel, Voltage-gated channel

      Keywords - Biological processi

      Exocytosis, Ion transport, Potassium transport, Transport

      Keywords - Ligandi

      Potassium

      Enzyme and pathway databases

      ReactomeiREACT_287159. Voltage gated Potassium channels.
      REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Potassium voltage-gated channel subfamily B member 1By similarity
      Alternative name(s):
      Voltage-gated potassium channel subunit Kv2.1
      mShab1 Publication
      Gene namesi
      Name:Kcnb1Imported
      OrganismiMus musculus (Mouse)
      Taxonomic identifieri10090 [NCBI]
      Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
      ProteomesiUP000000589 Componenti: Chromosome 2

      Organism-specific databases

      MGIiMGI:96666. Kcnb1.

      Subcellular locationi

      Topology

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Topological domaini1 – 186186CytoplasmicBy similarityAdd
      BLAST
      Transmembranei187 – 20822Helical; Name=Segment S1By similarityAdd
      BLAST
      Topological domaini209 – 22820ExtracellularBy similarityAdd
      BLAST
      Transmembranei229 – 25022Helical; Name=Segment S2By similarityAdd
      BLAST
      Topological domaini251 – 2599CytoplasmicBy similarity
      Transmembranei260 – 28021Helical; Name=Segment S3By similarityAdd
      BLAST
      Topological domaini281 – 29414ExtracellularBy similarityAdd
      BLAST
      Transmembranei295 – 31622Helical; Voltage-sensor; Name=Segment S4By similarityAdd
      BLAST
      Topological domaini317 – 33014CytoplasmicBy similarityAdd
      BLAST
      Transmembranei331 – 35121Helical; Name=Segment S5By similarityAdd
      BLAST
      Topological domaini352 – 36413ExtracellularBy similarityAdd
      BLAST
      Intramembranei365 – 37612Helical; Name=Pore helixBy similarityAdd
      BLAST
      Intramembranei377 – 3848By similarity
      Topological domaini385 – 3917ExtracellularBy similarity
      Transmembranei392 – 42029Helical; Name=Segment S6By similarityAdd
      BLAST
      Topological domaini421 – 857437CytoplasmicBy similarityAdd
      BLAST

      GO - Cellular componenti

      • axon Source: UniProtKB
      • dendrite Source: UniProtKB
      • dendrite membrane Source: Ensembl
      • integral component of membrane Source: GO_Central
      • neuronal cell body membrane Source: UniProtKB
      • perikaryon Source: UniProtKB
      • plasma membrane Source: UniProtKB
      • postsynaptic membrane Source: Ensembl
      • voltage-gated potassium channel complex Source: UniProtKB
      Complete GO annotation...

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

      Pathology & Biotechi

      Disruption phenotypei

      Mice show normal motor coordination and visual acuity, but are hyperactive, exhibit defects in spatial learning ability and show reduced anxiety-like behavior (PubMed:24494598). Show a higher incidence and a shorter latency to seizure progression compared to wild-type mice (PubMed:24494598). Display reduced fasting blood glucose levels and elevated serum insulin levels (PubMed:17767909, PubMed:19383458). Glucose tolerance and insulin secretion is enhanced compared to control animals (PubMed:17767909, PubMed:19383458). Show impaired long-term potentiation in hippocampal neurons (PubMed:24494598). Display a reduction in the slowly deactivating delayed rectifier potassium current in hippocampal pyramidal neurons (PubMed:24494598). Glucose-induced action potential (AP) duration and amplitude is increased while the firing frequency is reduced in pancreatic beta cells (PubMed:17767909, PubMed:19383458).3 Publications

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 857857Potassium voltage-gated channel subfamily B member 1PRO_0000054043Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Modified residuei15 – 151PhosphoserineBy similarity
      Modified residuei128 – 1281Phosphotyrosine; by SrcBy similarity
      Modified residuei457 – 4571PhosphoserineBy similarity
      Cross-linki475 – 475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
      Modified residuei484 – 4841PhosphoserineBy similarity
      Modified residuei496 – 4961PhosphoserineBy similarity
      Modified residuei503 – 5031PhosphoserineBy similarity
      Modified residuei520 – 5201Phosphoserine; by CDK5; in vitroBy similarity
      Modified residuei541 – 5411PhosphoserineBy similarity
      Modified residuei567 – 5671PhosphoserineBy similarity
      Modified residuei590 – 5901PhosphoserineBy similarity
      Modified residuei607 – 6071Phosphoserine; by CDK5By similarity
      Modified residuei655 – 6551Phosphoserine; by CDK5; in vitroBy similarity1 Publication
      Modified residuei719 – 7191PhosphoserineBy similarity
      Modified residuei771 – 7711PhosphoserineBy similarity
      Modified residuei799 – 7991PhosphoserineBy similarity
      Modified residuei804 – 8041Phosphoserine; by CDK5, MAPK14; in vitroBy similarity
      Modified residuei836 – 8361PhosphothreonineBy similarity

      Post-translational modificationi

      Phosphorylated. Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons. Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities. Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity. Phosphorylated on Tyr-128 by Src and on Ser-804 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program. Phosphorylated on Ser-520, Ser-655, Ser-607 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation. The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS). Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons. Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival. 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 on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties. Dephosphorylation by phosphatase PTPRE confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn2+-dependent manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA. Hypoxia-, seizure- or glutamate-induced neuronal activities promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity. In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated. In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced (By similarity). Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue (PubMed:10921884).By similarity1 Publication
      Acetylated. Acetylation occurs in pancreatic beta cells in response to stimulation by incretin hormones in a histone acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent signaling pathway, promoting beta cell survival.By similarity
      Sumoylated on Lys-474, preferentially with SUMO1; sumoylation induces a positive shift in the voltage-dependence of activation and inhibits channel activity. Sumoylation increases the frequency of repetitive action potential firing at the cell surface of hippocampal neurons and decreases its frequency in pancreatic beta cells. Desumoylated by SENP1.By similarity

      Keywords - PTMi

      Isopeptide bond, Phosphoprotein, Ubl conjugation

      Proteomic databases

      MaxQBiQ03717.
      PaxDbiQ03717.
      PRIDEiQ03717.

      PTM databases

      PhosphoSiteiQ03717.

      Expressioni

      Tissue specificityi

      Expressed in the brain (PubMed:17767909, PubMed:22056818). Expressed in the heart (PubMed:14684365). Expressed in pyramidal neurons and interneurons of the hippocampus (PubMed:22056818, PubMed:24494598). Expressed in neocortical pyramidal neurons (PubMed:22056818, PubMed:24477962). Expressed in dorsal root ganglia (DRG) neurons (PubMed:19357235). Expressed in pancreatic beta cells (PubMed:12270920, PubMed:17767909). Expressed in Schwann cells (PubMed:10921884). Expressed in ventricular myocytes (at protein level) (PubMed:14684365, PubMed:10506487).9 Publications

      Gene expression databases

      BgeeiQ03717.
      ExpressionAtlasiQ03717. baseline and differential.
      GenevisibleiQ03717. MM.

      Interactioni

      Subunit structurei

      Homotetramer or heterotetramer with KCNB2. Heterotetramer with non-conducting channel-forming alpha subunits such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1 (By similarity). Channel activity is regulated by association with ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3 (PubMed:22056818). Self-associates (via N-terminus and C-terminus); self-association is required to regulate trafficking, gating and C-terminal phosphorylation-dependent modulation of the channel. Interacts (via C-terminus) with STX1A (via C-terminus); this decreases the rate of channel activation and increases the rate of channel inactivation in pancreatic beta cells, induces also neuronal apoptosis in response to oxidative injury as well as pore-independent enhancement of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta cells and from the soma of dorsal root ganglia (DRG) neurons. Interacts (via N-terminus) with SNAP25; this decreases the rate of channel inactivation in pancreatic beta cells and also increases interaction during neuronal apoptosis in a N-methyl-D-aspartate receptor (NMDAR)-dependent manner. Interacts (via N-terminus and C-terminus) with VAMP2 (via N-terminus); stimulates channel inactivation rate. Interacts with CREB1; this promotes channel acetylation in response to stimulation by incretin hormones. Interacts (via N-terminus and C-terminus) with MYL12B. Interacts (via N-terminus) with PIAS3; this increases the number of functional channels at the cell surface. Interacts with SUMO1 (By similarity). Interacts (via phosphorylated form) with PTPRE isoform 2; this reduces phosphorylation and channel activity in heterologous cells (PubMed:10921884).By similarity2 Publications

      Binary interactionsi

      WithEntry#Exp.IntActNotes
      Amigo1Q80ZD84EBI-7511364,EBI-7511393

      Protein-protein interaction databases

      BioGridi200886. 3 interactions.
      IntActiQ03717. 1 interaction.
      MINTiMINT-8298631.
      STRINGi10090.ENSMUSP00000057981.

      Structurei

      3D structure databases

      ProteinModelPortaliQ03717.
      SMRiQ03717. Positions 30-462.
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Region

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Regioni59 – 7517Self-associationBy similarityAdd
      BLAST
      Regioni448 – 48134Self-associationBy similarityAdd
      BLAST

      Motif

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Motifi377 – 3826Selectivity filterBy similarity

      Compositional bias

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Compositional biasi517 – 5204Poly-Ser

      Domaini

      The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity
      The N-terminal and C-terminal cytoplasmic regions mediate homooligomerization; self-association is required to regulate trafficking, gating and C-terminal phosphorylation-dependent modulation of the channel (By similarity). The N-terminal cytoplasmic region is important for interaction with other channel-forming alpha subnunits and with ancillary beta subunits (PubMed:22056818). The C-terminus is necessary and sufficient for the restricted localization to, and clustering within, both in soma and proximal portions of dendrite of neurons and in lateral membrane of non-neuronal polarized cells. The C-terminus is both necessary and sufficient as a mediator of cholinergic and calcium-stimulated modulation of channel cell membrane clustering localization and activity in hippocampal neurons (By similarity).By similarity1 Publication

      Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      eggNOGiCOG1226.
      GeneTreeiENSGT00760000118981.
      HOGENOMiHOG000113206.
      HOVERGENiHBG052225.
      InParanoidiQ03717.
      KOiK04885.
      OMAiTEGVIDM.
      OrthoDBiEOG7CRTPP.
      TreeFamiTF313103.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. 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]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      PF03521. Kv2channel. 1 hit.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01514. KV21CHANNEL.
      PR01491. KVCHANNEL.
      PR01495. SHABCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 1 hit.

      Sequencei

      Sequence statusi: Complete.

      Q03717-1 [UniParc]FASTAAdd to basket

      « Hide

              10         20         30         40         50
      MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD
      60 70 80 90 100
      RLPRTRLGKL RDCNTHDSLL QVCDDYSLED NEYFFDRHPG AFTSILNFYR
      110 120 130 140 150
      TGRLHMMEEM CALSFSQELD YWGIDEIYLE SCCQARYHQK KEQMNEELKR
      160 170 180 190 200
      EAETLREREG EEFDNTCCAE KRKKLWDLLE KPNSSVAAKI LAIISIMFIV
      210 220 230 240 250
      LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF TMEYLLRFLS
      260 270 280 290 300
      SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
      310 320 330 340 350
      IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF
      360 370 380 390 400
      FAEKDEDDTK FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA
      410 420 430 440 450
      GVLVIALPIP IIVNNFSEFY KEQKRQEKAI KRREALERAK RNGSIVSMNM
      460 470 480 490 500
      KDAFARSIEM MDIVVEKNGE GVAKKDKVQD NHLSPNKWKW TKRALSETSS
      510 520 530 540 550
      SKSFETKEQG SPEKARSSSS PQHLNVQQLQ DMYSKMAKTQ SQPILNTKEM
      560 570 580 590 600
      APQSQPQEEL EMGSMPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
      610 620 630 640 650
      ATRFSHSPLA SLSGKSGGST APEVGWRGAL GASGGRLMET NPIPEASRSG
      660 670 680 690 700
      FFVESPRSSM KTHNPMKLRA LKVNFLEGDP TPLLPALGLY HDPLRNRGGA
      710 720 730 740 750
      AAAVAGLECA SLLDKPVLSP ESSIYTTASA RTPPRSPEKH TAIAFNFEAG
      760 770 780 790 800
      VHQYIDTDTD DEGQLLYSVD SSPPKSLHGS TSPKFSLGAR TEKNHFESSP
      810 820 830 840 850
      LPTSPKFLRP NCVYASEGLP GKGPGAQEKC KLENHTSPDV HMLPGGGAHG

      STRDQSI
      Length:857
      Mass (Da):95,591
      Last modified:July 27, 2011 - v2
      Checksum:i5FE2D80E58E60710
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti701 – 7011A → R in AAA40112 (PubMed:2002364).Curated
      Sequence conflicti773 – 7731P → L in AAA40112 (PubMed:2002364).Curated

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      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.
      CCDSiCCDS17096.1.
      PIRiI56529.
      RefSeqiNP_032446.2. NM_008420.4.
      UniGeneiMm.205341.
      Mm.490804.

      Genome annotation databases

      EnsembliENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
      GeneIDi16500.
      KEGGimmu:16500.
      UCSCiuc008nzh.2. mouse.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      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.
      CCDSiCCDS17096.1.
      PIRiI56529.
      RefSeqiNP_032446.2. NM_008420.4.
      UniGeneiMm.205341.
      Mm.490804.

      3D structure databases

      ProteinModelPortaliQ03717.
      SMRiQ03717. Positions 30-462.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi200886. 3 interactions.
      IntActiQ03717. 1 interaction.
      MINTiMINT-8298631.
      STRINGi10090.ENSMUSP00000057981.

      Chemistry

      GuidetoPHARMACOLOGYi546.

      PTM databases

      PhosphoSiteiQ03717.

      Proteomic databases

      MaxQBiQ03717.
      PaxDbiQ03717.
      PRIDEiQ03717.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
      GeneIDi16500.
      KEGGimmu:16500.
      UCSCiuc008nzh.2. mouse.

      Organism-specific databases

      CTDi3745.
      MGIiMGI:96666. Kcnb1.

      Phylogenomic databases

      eggNOGiCOG1226.
      GeneTreeiENSGT00760000118981.
      HOGENOMiHOG000113206.
      HOVERGENiHBG052225.
      InParanoidiQ03717.
      KOiK04885.
      OMAiTEGVIDM.
      OrthoDBiEOG7CRTPP.
      TreeFamiTF313103.

      Enzyme and pathway databases

      ReactomeiREACT_287159. Voltage gated Potassium channels.
      REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

      Miscellaneous databases

      ChiTaRSiKcnb1. mouse.
      NextBioi289823.
      PROiQ03717.
      SOURCEiSearch...

      Gene expression databases

      BgeeiQ03717.
      ExpressionAtlasiQ03717. baseline and differential.
      GenevisibleiQ03717. MM.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. 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]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      PF03521. Kv2channel. 1 hit.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01514. KV21CHANNEL.
      PR01491. KVCHANNEL.
      PR01495. SHABCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 1 hit.
      ProtoNetiSearch...

      Publicationsi

      « Hide 'large scale' publications
      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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
        Tissue: Brain.
      2. 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. Cited for: REVIEW.
      6. "Attenuation of the slow component of delayed rectification, action potential prolongation, and triggered activity in mice expressing a dominant-negative Kv2 alpha subunit."
        Xu H., Barry D.M., Li H., Brunet S., Guo W., Nerbonne J.M.
        Circ. Res. 85:623-633(1999) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      7. "Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon."
        Peretz A., Gil-Henn H., Sobko A., Shinder V., Attali B., Elson A.
        EMBO J. 19:4036-4045(2000) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION, INTERACTION WITH PTPRE, TISSUE SPECIFICITY.
      8. "Inhibition of Kv2.1 voltage-dependent K+ channels in pancreatic beta-cells enhances glucose-dependent insulin secretion."
        MacDonald P.E., Sewing S., Wang J., Joseph J.W., Smukler S.R., Sakellaropoulos G., Wang J., Saleh M.C., Chan C.B., Tsushima R.G., Salapatek A.M., Wheeler M.B.
        J. Biol. Chem. 277:44938-44945(2002) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      9. "Attenuation of I(K,slow1) and I(K,slow2) in Kv1/Kv2DN mice prolongs APD and QT intervals but does not suppress spontaneous or inducible arrhythmias."
        Kodirov S.A., Brunner M., Nerbonne J.M., Buckett P., Mitchell G.F., Koren G.
        Am. J. Physiol. 286:H368-H374(2004) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      10. "Molecular determinants of voltage-gated potassium currents in vascular smooth muscle."
        Cox R.H.
        Cell Biochem. Biophys. 42:167-195(2005) [PubMed] [Europe PMC] [Abstract]
        Cited for: REVIEW.
      11. "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.
      12. "Kv2.1 ablation alters glucose-induced islet electrical activity, enhancing insulin secretion."
        Jacobson D.A., Kuznetsov A., Lopez J.P., Kash S., Ammala C.E., Philipson L.H.
        Cell Metab. 6:229-235(2007) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      13. "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.
      14. "A model of action potentials and fast Ca2+ dynamics in pancreatic beta-cells."
        Fridlyand L.E., Jacobson D.A., Kuznetsov A., Philipson L.H.
        Biophys. J. 96:3126-3139(2009) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, DISRUPTION PHENOTYPE.
      15. "AMIGO is an auxiliary subunit of the Kv2.1 potassium channel."
        Peltola M.A., Kuja-Panula J., Lauri S.E., Taira T., Rauvala H.
        EMBO Rep. 12:1293-1299(2011) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBUNIT, INTERACTION WITH AMIGO1, DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      16. "The role of voltage-gated potassium channels Kv2.1 and Kv2.2 in the regulation of insulin and somatostatin release from pancreatic islets."
        Li X.N., Herrington J., Petrov A., Ge L., Eiermann G., Xiong Y., Jensen M.V., Hohmeier H.E., Newgard C.B., Garcia M.L., Wagner M., Zhang B.B., Thornberry N.A., Howard A.D., Kaczorowski G.J., Zhou Y.P.
        J. Pharmacol. Exp. Ther. 344:407-416(2013) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION.
      17. Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
      18. "A unique ion channel clustering domain on the axon initial segment of mammalian neurons."
        King A.N., Manning C.F., Trimmer J.S.
        J. Comp. Neurol. 522:2594-2608(2014) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      19. "Kv2.1 and silent Kv subunits underlie the delayed rectifier K+ current in cultured small mouse DRG neurons."
        Bocksteins E., Raes A.L., Van de Vijver G., Bruyns T., Van Bogaert P.P., Snyders D.J.
        Am. J. Physiol. 296:C1271-C1278(2009) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

      Entry informationi

      Entry nameiKCNB1_MOUSE
      AccessioniPrimary (citable) accession number: Q03717
      Secondary accession number(s): Q8K0D1
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: October 25, 2002
      Last sequence update: July 27, 2011
      Last modified: June 24, 2015
      This is version 136 of the entry and version 2 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program

      Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. MGD cross-references
        Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
      2. SIMILARITY comments
        Index of protein domains and families

      External Data

      Dasty 3

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.