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Entry version 181 (29 Sep 2021)
Sequence version 2 (27 Jul 2011)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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.2 Publications1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Potassium channel, Voltage-gated channel
Biological processExocytosis, Ion transport, Potassium transport, Transport
LigandPotassium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1296072, Voltage gated Potassium channels
R-MMU-381676, Glucagon-like Peptide-1 (GLP1) regulates insulin secretion

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Kcnb1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:96666, Kcnb1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSMUSG00000050556

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 186CytoplasmicBy similarityAdd BLAST186
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei187 – 208Helical; Name=Segment S1By similarityAdd BLAST22
Topological domaini209 – 228ExtracellularBy similarityAdd BLAST20
Transmembranei229 – 250Helical; Name=Segment S2By similarityAdd BLAST22
Topological domaini251 – 259CytoplasmicBy similarity9
Transmembranei260 – 280Helical; Name=Segment S3By similarityAdd BLAST21
Topological domaini281 – 294ExtracellularBy similarityAdd BLAST14
Transmembranei295 – 316Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST22
Topological domaini317 – 330CytoplasmicBy similarityAdd BLAST14
Transmembranei331 – 351Helical; Name=Segment S5By similarityAdd BLAST21
Topological domaini352 – 364ExtracellularBy similarityAdd BLAST13
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei365 – 376Helical; Name=Pore helixBy similarityAdd BLAST12
Intramembranei377 – 384By similarity8
Topological domaini385 – 391ExtracellularBy similarity7
Transmembranei392 – 420Helical; Name=Segment S6By similarityAdd BLAST29
Topological domaini421 – 857CytoplasmicBy similarityAdd BLAST437

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

Chemistry databases

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
546

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000540431 – 857Potassium voltage-gated channel subfamily B member 1Add BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei15PhosphoserineBy similarity1
Modified residuei128Phosphotyrosine; by SrcBy similarity1
Modified residuei444PhosphoserineCombined sources1
Modified residuei457PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei484PhosphoserineBy similarity1
Modified residuei496PhosphoserineBy similarity1
Modified residuei503PhosphoserineBy similarity1
Modified residuei519PhosphoserineBy similarity1
Modified residuei520Phosphoserine; by CDK5; in vitroBy similarity1
Modified residuei541PhosphoserineBy similarity1
Modified residuei567PhosphoserineBy similarity1
Modified residuei590PhosphoserineBy similarity1
Modified residuei607Phosphoserine; by CDK5By similarity1
Modified residuei655PhosphoserineCombined sources1
Modified residuei719PhosphoserineBy similarity1
Modified residuei771PhosphoserineBy similarity1
Modified residuei799PhosphoserineBy similarity1
Modified residuei804PhosphoserineCombined sources1
Modified residuei836PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q03717

MaxQB - The MaxQuant DataBase

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MaxQBi
Q03717

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q03717

PeptideAtlas

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PeptideAtlasi
Q03717

PRoteomics IDEntifications database

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PRIDEi
Q03717

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
269451

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q03717

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q03717

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q03717

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000050556, Expressed in retina and 205 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q03717, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
200886, 15 interactors

Protein interaction database and analysis system

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IntActi
Q03717, 3 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000057981

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q03717, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 21DisorderedSequence analysisAdd BLAST21
Regioni59 – 75Self-associationBy similarityAdd BLAST17
Regioni448 – 481Self-associationBy similarityAdd BLAST34
Regioni475 – 569DisorderedSequence analysisAdd BLAST95
Regioni608 – 627DisorderedSequence analysisAdd BLAST20
Regioni768 – 802DisorderedSequence analysisAdd BLAST35
Regioni816 – 857DisorderedSequence analysisAdd BLAST42

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi377 – 382Selectivity filterBy similarity6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi491 – 506Polar residuesSequence analysisAdd BLAST16
Compositional biasi513 – 561Polar residuesSequence analysisAdd BLAST49

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 subunits 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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3713, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000154899

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_011722_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q03717

Identification of Orthologs from Complete Genome Data

More...
OMAi
AFNFHDA

Database of Orthologous Groups

More...
OrthoDBi
203440at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q03717

TreeFam database of animal gene trees

More...
TreeFami
TF313103

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.350, 1 hit
3.30.710.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000210, BTB/POZ_dom
IPR005821, Ion_trans_dom
IPR003968, K_chnl_volt-dep_Kv
IPR003973, K_chnl_volt-dep_Kv2
IPR004350, K_chnl_volt-dep_Kv2.1
IPR011333, SKP1/BTB/POZ_sf
IPR003131, T1-type_BTB
IPR028325, VG_K_chnl
IPR027359, Volt_channel_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11537, PTHR11537, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02214, BTB_2, 1 hit
PF00520, Ion_trans, 1 hit
PF03521, Kv2channel, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01514, KV21CHANNEL
PR01491, KVCHANNEL
PR01495, SHABCHANNEL

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00225, BTB, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54695, SSF54695, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5FE2D80E58E60710
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti701A → R in AAA40112 (PubMed:2002364).Curated1
Sequence conflicti773P → L in AAA40112 (PubMed:2002364).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M64228 mRNA Translation: AAA40112.1
AL591711 Genomic DNA No translation available.
AL591854 Genomic DNA No translation available.
CH466551 Genomic DNA Translation: EDL06500.1
BC031776 mRNA Translation: AAH31776.1
BC061501 mRNA Translation: AAH61501.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS17096.1

Protein sequence database of the Protein Information Resource

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PIRi
I56529

NCBI Reference Sequences

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RefSeqi
NP_032446.2, NM_008420.4
XP_017171221.1, XM_017315732.1
XP_017171222.1, XM_017315733.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556
ENSMUST00000207917; ENSMUSP00000147093; ENSMUSG00000050556

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
16500

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:16500

UCSC genome browser

More...
UCSCi
uc008nzh.2, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64228 mRNA Translation: AAA40112.1
AL591711 Genomic DNA No translation available.
AL591854 Genomic DNA No translation available.
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
XP_017171221.1, XM_017315732.1
XP_017171222.1, XM_017315733.1

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi200886, 15 interactors
IntActiQ03717, 3 interactors
STRINGi10090.ENSMUSP00000057981

Chemistry databases

GuidetoPHARMACOLOGYi546

PTM databases

iPTMnetiQ03717
PhosphoSitePlusiQ03717
SwissPalmiQ03717

Proteomic databases

jPOSTiQ03717
MaxQBiQ03717
PaxDbiQ03717
PeptideAtlasiQ03717
PRIDEiQ03717
ProteomicsDBi269451

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
Q03717, 2 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
28477, 406 antibodies

The DNASU plasmid repository

More...
DNASUi
16500

Genome annotation databases

EnsembliENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556
ENSMUST00000207917; ENSMUSP00000147093; ENSMUSG00000050556
GeneIDi16500
KEGGimmu:16500
UCSCiuc008nzh.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3745
MGIiMGI:96666, Kcnb1
VEuPathDBiHostDB:ENSMUSG00000050556

Phylogenomic databases

eggNOGiKOG3713, Eukaryota
GeneTreeiENSGT00940000154899
HOGENOMiCLU_011722_2_1_1
InParanoidiQ03717
OMAiAFNFHDA
OrthoDBi203440at2759
PhylomeDBiQ03717
TreeFamiTF313103

Enzyme and pathway databases

ReactomeiR-MMU-1296072, Voltage gated Potassium channels
R-MMU-381676, Glucagon-like Peptide-1 (GLP1) regulates insulin secretion

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
16500, 0 hits in 61 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Kcnb1, mouse

Protein Ontology

More...
PROi
PR:Q03717
RNActiQ03717, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000050556, Expressed in retina and 205 other tissues
GenevisibleiQ03717, MM

Family and domain databases

Gene3Di1.20.120.350, 1 hit
3.30.710.10, 1 hit
InterProiView protein in InterPro
IPR000210, BTB/POZ_dom
IPR005821, Ion_trans_dom
IPR003968, K_chnl_volt-dep_Kv
IPR003973, K_chnl_volt-dep_Kv2
IPR004350, K_chnl_volt-dep_Kv2.1
IPR011333, SKP1/BTB/POZ_sf
IPR003131, T1-type_BTB
IPR028325, VG_K_chnl
IPR027359, Volt_channel_dom_sf
PANTHERiPTHR11537, PTHR11537, 1 hit
PfamiView protein in Pfam
PF02214, BTB_2, 1 hit
PF00520, Ion_trans, 1 hit
PF03521, Kv2channel, 2 hits
PRINTSiPR01514, KV21CHANNEL
PR01491, KVCHANNEL
PR01495, SHABCHANNEL
SMARTiView protein in SMART
SM00225, BTB, 1 hit
SUPFAMiSSF54695, SSF54695, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKCNB1_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q03717
Secondary accession number(s): Q8K0D1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: July 27, 2011
Last modified: September 29, 2021
This is version 181 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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
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