Kcnb1
entrez
25736
canonical
uniprot
P15387
canonical
ensembl
ENSRNOG00000046949
resolver
ensembl
ENSRNOG00055004620
resolver
ensembl
ENSRNOG00060001059
resolver
ensembl
ENSRNOG00065013004
resolver
ensp
ENSRNOP00000065961
resolver
ensp
ENSRNOP00055005484
resolver
ensp
ENSRNOP00060000671
resolver
ensp
ENSRNOP00065016456
resolver
enst
ENSRNOT00000074023
resolver
enst
ENSRNOT00055007323
resolver
enst
ENSRNOT00060001439
resolver
enst
ENSRNOT00065021296
resolver
genesymbol
Kcnb1
resolver
uniprot
A0A0H2UI34
resolver
uniprot_entry
A0A0H2UI34_RAT
resolver
uniprot_entry
KCNB1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 42 nM hanatoxin 1 (HaTx1), a spider venom toxin of the tarantula G.spatulata (PubMed:7576642). Inhibited by 100 nM stromatoxin 1 (ScTx1), a spider venom toxin of the tarantula S.calceata (PubMed:12065754). Modestly sensitive to millimolar levels of tetraethylammonium (TEA) and 4-aminopyridine (4-AP) (PubMed:1875913, PubMed:2770868, PubMed:8083226, PubMed:9362476). Completely insensitive to toxins such as dendrotoxin (DTX) and charybdotoxin (CTX) (PubMed:9362476). {ECO:0000269|PubMed:12065754, ECO:0000269|PubMed:1875913, ECO:0000269|PubMed:2770868, ECO:0000269|PubMed:7576642, ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:9362476, ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231}.
uniprot
proteins
amino_acid_sequence
MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLQVCDDYSLEDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGESIAKKDKVQDNHLSPNKWKWTKRALSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYSKMAKTQSQPILNTKEMAPQSKPPEELEMSSMPSPVAPLPARTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLASLSSKAGSSTAPEVGWRGALGASGGRLTETNPIPETSRSGFFVESPRSSMKTNNPLKLRALKVNFVEGDPTPLLPSLGLYHDPLRNRGGAAAAVAGLECASLLDKPVLSPESSIYTTASARTPPRSPEKHTAIAFNFEAGVHHYIDTDTDDEGQLLYSVDSSPPKSLHGSTSPKFSTGARTEKNHFESSPLPTSPKFLRPNCVYSSEGLTGKGPGAQEKCKLENHTPPDVHMLPGGGAHGSTRDQSI
uniprot
proteins
function
FUNCTION: 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:10024359, PubMed:10618149, PubMed:12451110, PubMed:17379638, PubMed:19276663, PubMed:23878373). Also plays a role in the regulation of exocytosis independently of its electrical function (PubMed:20484665). 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:12560340, PubMed:1875913, PubMed:2206531, PubMed:2770868, PubMed:8083226, PubMed:8978827, PubMed:9351973, PubMed:9565597). 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 (PubMed:20202934). 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 (PubMed:8670833, PubMed:8980147, PubMed:9079713, PubMed:9305895, PubMed:9362476, PubMed:9696692). 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 (PubMed:9362476). 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:12954870, PubMed:19219384). 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 slowly inactivating 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 cells (PubMed:10024359, PubMed:10414968, PubMed:10618149, PubMed:11463864, PubMed:12127166, PubMed:12403834, PubMed:12451110, PubMed:12621036, PubMed:12807875, PubMed:12832499, PubMed:12954870, PubMed:15195093, PubMed:15322114, PubMed:16407566, PubMed:17301173, PubMed:17379638, PubMed:18167541, PubMed:18463252, PubMed:19276663, PubMed:20484665, PubMed:21518833, PubMed:22411134, PubMed:23878373, PubMed:9362476, PubMed:9616203). 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 (PubMed:10618149, PubMed:12451110, PubMed:16319318, PubMed:16917065, PubMed:17379638, PubMed:19276663, PubMed:23878373). Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (By similarity). Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion (PubMed:11463864). Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells (PubMed:9616203). May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval (By similarity). Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury (PubMed:12832499, PubMed:16273079, PubMed:17360683, PubMed:19077057, PubMed:19622611, PubMed:24928958). May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (PubMed:16319318). 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 (PubMed:11463864, PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134). {ECO:0000250|UniProtKB:Q03717, ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:11463864, ECO:0000269|PubMed:12127166, ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:12621036, ECO:0000269|PubMed:12807875, ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:15322114, ECO:0000269|PubMed:16273079, ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:18167541, ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:1875913, ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:19276663, ECO:0000269|PubMed:19622611, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:2206531, ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24928958, ECO:0000269|PubMed:2770868, ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:8980147, ECO:0000269|PubMed:9079713, ECO:0000269|PubMed:9305895, ECO:0000269|PubMed:9351973, ECO:0000269|PubMed:9362476, ECO:0000269|PubMed:9565597, ECO:0000269|PubMed:9616203, ECO:0000269|PubMed:9696692}.
uniprot
proteins
mass_dalton
95637
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation. Additive effect on activation and steady-state inactivation; when associated with A-457."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 15; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 71; /note="Q->E: Reduces channel activity."; /evidence="ECO:0000269|PubMed:12560340"; MUTAGEN 79; /note="E->D: No effect on channel activity."; /evidence="ECO:0000269|PubMed:12560340"; MUTAGEN 128; /note="Y->F: Reduces the increase of plasma membrane insertion and apoptotic enhancement of potassium current during cell death program. Significant loss of Src-mediated phosphorylation and channel activity. Reduces interaction with PTPRE. Increases cell viability against apoptotic insults. Abolishes the increase of plasma membrane insertion and apoptotic enhancement of potassium current during cell death program; when associated with D-804."; /evidence="ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:19622611"; MUTAGEN 149; /note="K->Q: No loss of SUMO-dependent channel activity modulation in hippocampal neurons."; /evidence="ECO:0000269|PubMed:21518833"; MUTAGEN 259; /note="K->Q: No loss of SUMO-dependent channel activity modulation in hippocampal neurons."; /evidence="ECO:0000269|PubMed:21518833"; MUTAGEN 369; /note="W->C: Reduces channel activity. Does not inhibit membrane plasma subcellular localization, interaction with STX1A, pore-independent exocytosis activity and apoptotic enhancement of potassium current during cell death program; when associated with T-384."; /evidence="ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:22411134"; MUTAGEN 384; /note="Y->T: Reduces channel activity. Does not inhibit membrane plasma subcellular localization, interaction with STX1A, pore-independent exocytosis activity and apoptotic enhancement of potassium current during cell death program; when associated with C-369."; /evidence="ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:22411134"; MUTAGEN 444; /note="S->A: No effect on Src-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:9351973"; MUTAGEN 457; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation. Additive effect on activation and steady-state inactivation; when associated with A-15."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 457; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 474; /note="K->Q: Loss of SUMO-dependent channel activity modulation in hippocampal neurons."; /evidence="ECO:0000269|PubMed:21518833"; MUTAGEN 484; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 484; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 496; /note="S->A: No effect on Src-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:9351973"; MUTAGEN 541; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 541; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 567; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation. Larger effect on activation and steady-state inactivation; when associated with A-607."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 567; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 587; /note="S->A: Abolishes clustered subcellular distribution in neurons."; /evidence="ECO:0000269|PubMed:10719893"; MUTAGEN 590; /note="S->A: Abolishes clustered subcellular distribution in neurons. Does not affect KCNB1-containing vesicles motility."; /evidence="ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:24569993"; MUTAGEN 591; /note="F->A: Abolishes clustered subcellular distribution in neurons."; /evidence="ECO:0000269|PubMed:10719893"; MUTAGEN 593; /note="S->A: Abolishes clustered subcellular distribution in neurons."; /evidence="ECO:0000269|PubMed:10719893"; MUTAGEN 607; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation. Larger effect on activation and steady-state inactivation; when associated with A-567."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 607; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 655; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 655; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 719; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 719; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 771; /note="S->A: Shift in voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 771; /note="S->D: Resists voltage-dependent gating on calcineurin-dependent activation and steady-state inactivation."; /evidence="ECO:0000269|PubMed:16917065"; MUTAGEN 804; /note="S->A: Reduces the increase of plasma membrane insertion and apoptotic enhancement of potassium current during cell death program. No change in calcineurin-dependent regulation of voltage-dependent gating. Abolishes the increase of plasma membrane insertion and apoptotic enhancement of potassium current during cell death program; when associated with F-128."; /evidence="ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:19622611"; MUTAGEN 804; /note="S->D: Does not reduce apoptotic enhancement of potassium current during the cell death program."; /evidence="ECO:0000269|PubMed:17360683
uniprot
proteins
post_translational_modification
PTM: Phosphorylated (PubMed:15195093, PubMed:16319318, PubMed:16407566, PubMed:18463252, PubMed:8083226). Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons (PubMed:16917065, PubMed:17192433, PubMed:9351973). Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities (PubMed:12615930, PubMed:17192433). Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE isoform 2 (PubMed:12615930). CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity (PubMed:21712386). 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 (PubMed:17360683, PubMed:19622611). Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation (PubMed:21712386). The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS) (PubMed:24477962). Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons (PubMed:16917065, PubMed:9351973). Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival (PubMed:21818121). 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 (PubMed:17192433). 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 (PubMed:16917065, PubMed:17192433). Dephosphorylation by phosphatase PTPRE isoform 2 confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn(2+)-dependent manner (PubMed:19622611). Dephosphorylated at Ser-607 by protein phosphatase PPP1CA (PubMed:21712386). Hypoxia-, seizure- or glutamate-induced neuronal activities promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity (PubMed:15195093, PubMed:16319318, PubMed:16407566, PubMed:16917065, PubMed:17192433). In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated (PubMed:17192433). In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced (PubMed:17192433). Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue (By similarity). Phosphorylation at Ser-593 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB (By similarity). {ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:18690023, ECO:0000269|PubMed:19622611, ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:21818121, ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:9351973}.; PTM: 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 (PubMed:21818121). {ECO:0000269|PubMed:21818121}.; PTM: Sumoylated on Lys-474, preferentially with SUMO1; sumoylation induces a positive shift in the voltage-dependence of activation and inhibits channel activity (PubMed:21518833). Sumoylation increases the frequency of repetitive action potential firing at the cell surface of hippocampal neurons and decreases its frequency in pancreatic beta cells (PubMed:21518833). Desumoylated by SENP1 (PubMed:21518833). {ECO:0000269|PubMed:21518833}.; PTM: Not glycosylated (PubMed:8083226). {ECO:0000269|PubMed:8083226}.
uniprot
proteins
protein_family
B (Shab) (TC 1.A.1.2) subfamily
uniprot
proteins
protein_family
Kv2.1/KCNB1 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
10024359
uniprot
proteins
pubmed
10414301
uniprot
proteins
pubmed
10414968
uniprot
proteins
pubmed
10618149
uniprot
proteins
pubmed
10719893
uniprot
proteins
pubmed
11463864
uniprot
proteins
pubmed
12065754
uniprot
proteins
pubmed
12127166
uniprot
proteins
pubmed
12403834
uniprot
proteins
pubmed
12451110
uniprot
proteins
pubmed
12560340
uniprot
proteins
pubmed
12615930
uniprot
proteins
pubmed
12621036
uniprot
proteins
pubmed
12807875
uniprot
proteins
pubmed
12832499
uniprot
proteins
pubmed
12954870
uniprot
proteins
pubmed
15195093
uniprot
proteins
pubmed
15322114
uniprot
proteins
pubmed
15855232
uniprot
proteins
pubmed
15858231
uniprot
proteins
pubmed
16273079
uniprot
proteins
pubmed
16319318
uniprot
proteins
pubmed
16407566
uniprot
proteins
pubmed
16917065
uniprot
proteins
pubmed
16988031
uniprot
proteins
pubmed
17192433
uniprot
proteins
pubmed
17301173
uniprot
proteins
pubmed
17360683
uniprot
proteins
pubmed
17379638
uniprot
proteins
pubmed
1740690
uniprot
proteins
pubmed
17606996
uniprot
proteins
pubmed
17965280
uniprot
proteins
pubmed
18004376
uniprot
proteins
pubmed
18167541
uniprot
proteins
pubmed
18463252
uniprot
proteins
pubmed
18542995
uniprot
proteins
pubmed
18690023
uniprot
proteins
pubmed
1875913
uniprot
proteins
pubmed
19014551
uniprot
proteins
pubmed
19074135
uniprot
proteins
pubmed
19077057
uniprot
proteins
pubmed
19219384
uniprot
proteins
pubmed
19276663
uniprot
proteins
pubmed
1961744
uniprot
proteins
pubmed
19622611
uniprot
proteins
pubmed
19690160
uniprot
proteins
pubmed
20202934
uniprot
proteins
pubmed
20360102
uniprot
proteins
pubmed
20484665
uniprot
proteins
pubmed
21518833
uniprot
proteins
pubmed
21712386
uniprot
proteins
pubmed
21818121
uniprot
proteins
pubmed
2206531
uniprot
proteins
pubmed
22411134
uniprot
proteins
pubmed
22648171
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23705070
uniprot
proteins
pubmed
23878373
uniprot
proteins
pubmed
24477962
uniprot
proteins
pubmed
24569993
uniprot
proteins
pubmed
24928958
uniprot
proteins
pubmed
2770868
uniprot
proteins
pubmed
7576642
uniprot
proteins
pubmed
7623158
uniprot
proteins
pubmed
8083226
uniprot
proteins
pubmed
8463836
uniprot
proteins
pubmed
8508921
uniprot
proteins
pubmed
8670833
uniprot
proteins
pubmed
8978827
uniprot
proteins
pubmed
8980147
uniprot
proteins
pubmed
9079713
uniprot
proteins
pubmed
9305895
uniprot
proteins
pubmed
9351973
uniprot
proteins
pubmed
9362476
uniprot
proteins
pubmed
9522360
uniprot
proteins
pubmed
9565597
uniprot
proteins
pubmed
9616203
uniprot
proteins
pubmed
9696692
uniprot
proteins
sequence_length
857
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12127166, ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:12621036, ECO:0000269|PubMed:12807875, ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:15322114, ECO:0000269|PubMed:15855232, ECO:0000269|PubMed:16273079, ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16988031, ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:17606996, ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:18167541, ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:18542995, ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:19276663, ECO:0000269|PubMed:19690160, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:24928958, ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:8508921, ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:8980147, ECO:0000269|PubMed:9079713, ECO:0000269|PubMed:9305895, ECO:0000269|PubMed:9362476, ECO:0000269|PubMed:9522360, ECO:0000269|PubMed:9565597, ECO:0000269|PubMed:9616203, ECO:0000269|PubMed:9696692}. Perikaryon {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16988031, ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:1961744, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:9522360}. Cell projection, dendrite {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:9522360}. Cell projection, axon {ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:24477962}. Postsynaptic cell membrane {ECO:0000269|PubMed:9522360}. Synapse {ECO:0000269|PubMed:9522360}. Synapse, synaptosome {ECO:0000269|PubMed:8508921}. Membrane {ECO:0000269|PubMed:8508921}; Multi-pass membrane protein. Lateral cell membrane {ECO:0000269|PubMed:8978827}. Cell membrane, sarcolemma {ECO:0000269|PubMed:17965280}. Note=Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner (PubMed:10024359, PubMed:10719893, PubMed:15195093, PubMed:16319318, PubMed:16407566, PubMed:16988031, PubMed:17379638, PubMed:17606996, PubMed:18463252, PubMed:19014551, PubMed:1961744, PubMed:22648171, PubMed:23878373, PubMed:24477962, PubMed:24569993, PubMed:8978827, PubMed:9522360). Also localizes to high-density clusters in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the surface of neocortical and hippocampal pyramidal neurons (PubMed:17379638, PubMed:19014551, PubMed:22648171, PubMed:24477962). KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively (PubMed:24477962). Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells (PubMed:17965280, PubMed:8978827). Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes (PubMed:17965280). Associated with lipid raft domains (PubMed:15855232). In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge (PubMed:16273079, PubMed:19077057). {ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:12807875, ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:15855232, ECO:0000269|PubMed:16273079, ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16988031, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:17606996, ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:1961744, ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:8508921, ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:9522360}.
uniprot
proteins
transmembrane_region
TRANSMEM 187..208; /note="Helical; Name=Segment S1"; /evidence="ECO:0000255"; TRANSMEM 229..250; /note="Helical; Name=Segment S2"; /evidence="ECO:0000255"; TRANSMEM 260..280; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 295..316; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 331..351; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 392..420; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:P63142
uniprot
proteins