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Entry version 138 (02 Dec 2020)
Sequence version 2 (25 Oct 2002)
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Protein

Potassium voltage-gated channel subfamily B member 2

Gene

Kcnb2

Organism
Rattus norvegicus (Rat)
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 and smooth muscle cells (PubMed:1550672). Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:1550672). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; 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 KCNS1 and KCNS2, creating a functionally diverse range of channel complexes (PubMed:9305895). 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. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells (PubMed:1550672, PubMed:20202934).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 quinine at micromolar levels (By similarity). Modestly sensitive to millimolar levels of tetraethylammonium (TEA) (PubMed:1550672). Modestly sensitive to millimolar levels of 4-aminopyridine (4-AP).By similarity1 Publication1 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 about 20 msec (PubMed:1550672). After that, inactivate very slowly (PubMed:1550672). Their activation requires low threshold potentials of about -20 to -30 mV, with a midpoint activation at about 10 mV. For inactivation, the voltage at half-maximal amplitude is about -30 mV. Channels have an unitary conductance of about 14 pS. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system and post-translational modifications.1 Publication1 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 processIon transport, Potassium transport, Transport
      LigandPotassium

      <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%5Fand%5Ftaxonomy%5Fsection">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 2Imported
      Alternative name(s):
      CDRK1 Publication
      Voltage-gated potassium channel subunit Kv2.2
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Kcnb2Imported
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
      • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

      Organism-specific databases

      Rat genome database

      More...
      RGDi
      621349, Kcnb2

      <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

      Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

      Topology

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 190CytoplasmicBy similarityAdd BLAST190
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei191 – 212Helical; Name=Segment S1By similarityAdd BLAST22
      Topological domaini213 – 232ExtracellularBy similarityAdd BLAST20
      Transmembranei233 – 254Helical; Name=Segment S2By similarityAdd BLAST22
      Topological domaini255 – 265CytoplasmicBy similarityAdd BLAST11
      Transmembranei266 – 284Helical; Name=Segment S3By similarityAdd BLAST19
      Topological domaini285 – 296ExtracellularBy similarityAdd BLAST12
      Transmembranei297 – 317Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST21
      Topological domaini318 – 332CytoplasmicBy similarityAdd BLAST15
      Transmembranei333 – 355Helical; Name=Segment S5By similarityAdd BLAST23
      Topological domaini356 – 368ExtracellularBy similarityAdd BLAST13
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Intramembranei369 – 380Helical; Name=Pore helixBy similarityAdd BLAST12
      Intramembranei381 – 388By similarity8
      Topological domaini389 – 395ExtracellularBy similarity7
      Transmembranei396 – 424Helical; Name=Segment S6By similarityAdd BLAST29
      Topological domaini425 – 907CytoplasmicBy similarityAdd BLAST483

      Keywords - Cellular componenti

      Cell membrane, Cell projection, Membrane

      <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

      Chemistry databases

      IUPHAR/BPS Guide to PHARMACOLOGY

      More...
      GuidetoPHARMACOLOGYi
      547

      <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_00000540501 – 907Potassium voltage-gated channel subfamily B member 2Add BLAST907

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi287N-linked (GlcNAc...) asparagineSequence analysis1
      <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 residuei448PhosphoserineCombined sources1

      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 (PubMed:20202934).1 Publication

      Keywords - PTMi

      Glycoprotein, Phosphoprotein

      Proteomic databases

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

      More...
      PaxDbi
      Q63099

      PRoteomics IDEntifications database

      More...
      PRIDEi
      Q63099

      PTM databases

      GlyGen: Computational and Informatics Resources for Glycoscience

      More...
      GlyGeni
      Q63099, 1 site

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      Q63099

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

      More...
      PhosphoSitePlusi
      Q63099

      <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 pyramidal neurons of the cerebral cortex (at protein level) (PubMed:20202934). In the brain, the greatest density occurs in the olfactory bulb, followed by the cerebral cortex, hippocampus, and cerebellum. In peripheral tissues it is most prominent in whole tongue epithelium and circumvallate papillae (PubMed:1550672).2 Publications

      <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Homotetramer or heterotetramer with KCNB1 (PubMed:20202934). Heterotetramer with KCNS1 and KCNS2 (PubMed:9305895).

      By similarity2 Publications

      GO - Molecular functioni

      Protein-protein interaction databases

      STRING: functional protein association networks

      More...
      STRINGi
      10116.ENSRNOP00000050431

      <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

      Secondary structure

      1907
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...
      SMRi
      Q63099

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      Protein Data Bank in Europe - Knowledge Base

      More...
      PDBe-KBi
      Search...

      <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

      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>Motifi381 – 386Selectivity filterBy similarity6

      <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

      <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

      More...
      eggNOGi
      KOG3713, Eukaryota

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      Q63099

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      Q63099

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      1.20.120.350, 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
      IPR005826, K_chnl_volt-dep_Kv2.2
      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, 1 hit

      Protein Motif fingerprint database; a protein domain database

      More...
      PRINTSi
      PR01515, KV22CHANNEL
      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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

      Q63099-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MAEKAPPGLN RKTSRSTLSL PPEPVDIIRS KTCSRRVKIN VGGLNHEVLW
      60 70 80 90 100
      RTLDRLPRTR LGKLRDCNTH ESLLEVCDDY NLNENEYFFD RHPGAFTSIL
      110 120 130 140 150
      NFYRTGKLHM MEEMCALSFG QELDYWGIDE IYLESCCQAR YHQKKEQMNE
      160 170 180 190 200
      ELRREAETMR DGEGEEFDNT CCPEKRKKLW DLLEKPNSSV AAKILAIVSI
      210 220 230 240 250
      LFIVLSTIAL SLNTLPELQE NDEFGQPSDN RKLAHVEAVC IAWFTMEYLL
      260 270 280 290 300
      RFLSSPNKWK FFKGPLNVID LLAILPYYVT IFLTESNKSV LQFQNVRRVV
      310 320 330 340 350
      QIFRIMRILR ILKLARHSTG LQSLGFTLRR SYNELGLLIL FLAMGIMIFS
      360 370 380 390 400
      SLVFFAEKDE DATKFTSIPA SFWWATITMT TVGYGDIYPK TLLGKIVGGL
      410 420 430 440 450
      CCIAGVLVIA LPIPIIVNNF SEFYKEQKRQ EKAIKRREAL ERAKRNGSIV
      460 470 480 490 500
      SMNLKDAFAR SMELIDVAVE KAGESANIKD SVDDNHLSPS RWKWARKALS
      510 520 530 540 550
      ETSSNKSYEN KYQEVSQKDS HEQLNNTSSS SPQHLSAQKL EMLYNEITKT
      560 570 580 590 600
      QTHSHPNPDC QEQPERPSAY EEEIEMEEVV CPQEQLAVAQ TEVIVDMKST
      610 620 630 640 650
      SSIDSFTSCA TDFTETERSP LPPPSASHLQ MKFPTDLPGM DEHQRVRAPP
      660 670 680 690 700
      FLTLSRDKGP AAREAALDYA PIDITVNLDA GASHGPLQPD SASDSPKSSL
      710 720 730 740 750
      KGSNPLKSRS LKVNFQENRG SAPQTPPSTA RPLPVTTADF PLTTPQHMST
      760 770 780 790 800
      ILLEESPPPG TETLPGADVS AHCQGPSKGL SPRVPKQKLF PFSSRERRSF
      810 820 830 840 850
      TEIDTGEDED FLDLQRPRPD KQADPSPNCL ADKPGEARDP LREEGCVGSS
      860 870 880 890 900
      SPQNTDHNCR QDIYQAVGEV KKDSSQEGYK MENHLFAPEI HSNPGDTGYC

      PTRETSM
      Length:907
      Mass (Da):102,096
      Last modified:October 25, 2002 - 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:iB242D9A6753A1295
      GO

      <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

      The sequence AAA40905 differs from that shown. Reason: Frameshift.Curated

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      M77482 mRNA Translation: AAA40905.1 Frameshift.

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      JH0595

      Genome annotation databases

      UCSC genome browser

      More...
      UCSCi
      RGD:621349, rat

      <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
      M77482 mRNA Translation: AAA40905.1 Frameshift.
      PIRiJH0595

      3D structure databases

      Select the link destinations:

      Protein Data Bank Europe

      More...
      PDBei

      Protein Data Bank RCSB

      More...
      RCSB PDBi

      Protein Data Bank Japan

      More...
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      6EBKelectron microscopy3.30B/D/F/H278-311[»]
      6EBLelectron microscopy3.00B/D/F/H278-311[»]
      6EBMelectron microscopy4.00B/D/F/H278-311[»]
      SMRiQ63099
      ModBaseiSearch...
      PDBe-KBiSearch...

      Protein-protein interaction databases

      STRINGi10116.ENSRNOP00000050431

      Chemistry databases

      GuidetoPHARMACOLOGYi547

      PTM databases

      GlyGeniQ63099, 1 site
      iPTMnetiQ63099
      PhosphoSitePlusiQ63099

      Proteomic databases

      PaxDbiQ63099
      PRIDEiQ63099

      Protocols and materials databases

      ABCD curated depository of sequenced antibodies

      More...
      ABCDi
      Q63099, 3 sequenced antibodies

      Genome annotation databases

      UCSCiRGD:621349, rat

      Organism-specific databases

      RGDi621349, Kcnb2

      Phylogenomic databases

      eggNOGiKOG3713, Eukaryota
      InParanoidiQ63099
      PhylomeDBiQ63099

      Miscellaneous databases

      Protein Ontology

      More...
      PROi
      PR:Q63099

      Family and domain databases

      Gene3Di1.20.120.350, 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
      IPR005826, K_chnl_volt-dep_Kv2.2
      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, 1 hit
      PRINTSiPR01515, KV22CHANNEL
      PR01491, KVCHANNEL
      PR01495, SHABCHANNEL
      SMARTiView protein in SMART
      SM00225, BTB, 1 hit
      SUPFAMiSSF54695, SSF54695, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
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      MobiDB: a database of protein disorder and mobility annotations

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      MobiDBi
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      <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 nameiKCNB2_RAT
      <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: Q63099
      <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
      Last sequence update: October 25, 2002
      Last modified: December 2, 2020
      This is version 138 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

      3D-structure, Reference proteome

      Documents

      1. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      2. SIMILARITY comments
        Index of protein domains and families
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