Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P19024 (KCNA5_RAT)

Entry version 170 (02 Dec 2020)
Sequence version 1 (01 Nov 1990)
Previous versions | rss
Add a publicationFeedback
Protein

Potassium voltage-gated channel subfamily A member 5

Gene

Kcna5

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. 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 (PubMed:2361015, PubMed:15618540). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:15618540). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (PubMed:15618540). Homotetrameric channels display rapid activation and slow inactivation. May play a role in regulating the secretion of insulin in normal pancreatic islets (By similarity).By similarity3 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-1296072, Voltage gated Potassium channels

<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 A member 5
Alternative name(s):
RCK7
RK4
Voltage-gated potassium channel subunit Kv1.5
<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:Kcna5
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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: Chromosome 4

Organism-specific databases

Rat genome database

More...RGDi		2953, Kcna5

<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 – 238CytoplasmicBy similarityAdd BLAST238
<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>Transmembranei239 – 260Helical; Name=Segment S1By similarityAdd BLAST22
Topological domaini261 – 314ExtracellularBy similarityAdd BLAST54
Transmembranei315 – 336Helical; Name=Segment S2By similarityAdd BLAST22
Topological domaini337 – 347CytoplasmicBy similarityAdd BLAST11
Transmembranei348 – 368Helical; Name=Segment S3By similarityAdd BLAST21
Topological domaini369 – 384ExtracellularBy similarityAdd BLAST16
Transmembranei385 – 405Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST21
Topological domaini406 – 420CytoplasmicBy similarityAdd BLAST15
Transmembranei421 – 442Helical; Name=Segment S5By similarityAdd BLAST22
Topological domaini443 – 456ExtracellularBy similarityAdd BLAST14
<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>Intramembranei457 – 468Helical; Name=Pore helixBy similarityAdd BLAST12
Intramembranei469 – 476By similarity8
Topological domaini477 – 483ExtracellularBy similarity7
Transmembranei484 – 512Helical; Name=Segment S6By similarityAdd BLAST29
Topological domaini513 – 602CytoplasmicBy similarityAdd BLAST90

Keywords - Cellular componenti

Cell membrane, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi600 – 602TDL → AAA: Loss of interaction with DLG1. 1 Publication3

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4295724

<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_00000539891 – 602Potassium voltage-gated channel subfamily A member 5Add BLAST602

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 residuei81Phosphoserine; by CK2 and PKASequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi337S-palmitoyl cysteineSequence analysis1
Cross-linki525Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei535Phosphoserine; by PKASequence analysis1
Modified residuei546Phosphoserine; by PKASequence analysis1
Modified residuei569Phosphoserine; by PKASequence analysis1

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P19024

PRoteomics IDEntifications database

More...PRIDEi		P19024

<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 equally in atrium, ventricle, aorta and skeletal muscle. Weaker expression in brain.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression regulated by cAMP in a tissue-specific manner. In primary cardiac cells, levels increase by 6-fold, and in GH3 cells, levels decrease 5-6-fold.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000019719, Expressed in Ammon's horn and 17 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P19024, RN

<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 and heterotetramer of potassium channel proteins.

Interacts with DLG1, which enhances channel currents (PubMed:11709425).

Forms a ternary complex with DLG1 and CAV3 (PubMed:15277200).

Interacts with KCNAB1 (By similarity).

Interacts with UBE2I (By similarity).

By similarity2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		247503, 6 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P19024

Protein interaction database and analysis system

More...IntActi		P19024, 4 interactors

Molecular INTeraction database

More...MINTi		P19024

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000026691

<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

3D structure databases

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

More...SMRi		P19024

Database of comparative protein structure models

More...ModBasei		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

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>Regioni407 – 420S4-S5 linkerBy similarityAdd BLAST14

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>Motifi469 – 474Selectivity filterBy similarity6
Motifi600 – 602PDZ-binding3

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi373 – 376Poly-Gly4

<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 N-terminus may be important in determining the rate of inactivation of the channel while the C-terminal PDZ-binding motif may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
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

Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. [View classification]Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1545, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161860

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_011722_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P19024

Identification of Orthologs from Complete Genome Data

More...OMAi		ADHSPHL

Database of Orthologous Groups

More...OrthoDBi		695337at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P19024

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

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
IPR003972, K_chnl_volt-dep_Kv1
IPR004052, K_chnl_volt-dep_Kv1.5
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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01512, KV15CHANNEL
PR01491, KVCHANNEL
PR01496, SHAKERCHANEL

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.

P19024-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEISLVPLEN GSAMTLRGGG EAGASCVQTP RGECGCPPTS GLNNQSKETL 
        60         70         80         90        100
LRGRTTLEDA NQGGRPLPPM AQELPQPRRL SAEDEEGEGD PGLGTVEEDQ 
       110        120        130        140        150
APQDAGSLHH QRVLINISGL RFETQLGTLA QFPNTLLGDP AKRLHYFDPL 
       160        170        180        190        200
RNEYFFDRNR PSFDGILYYY QSGGRLRRPV NVSLDVFADE IRFYQLGDEA 
       210        220        230        240        250
MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA RAIAIVSVLV 
       260        270        280        290        300
ILISIITFCL ETLPEFRDER ELLRHPPVPP QPPAPAPGIN GSVSGALSSG 
       310        320        330        340        350
PTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI 
       360        370        380        390        400
IDVVAIFPYF ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF 
       410        420        430        440        450
KLSRHSKGLQ ILGKTLQASM RELGLLIFFL FIGVILFSSA VYFAEADNHG 
       460        470        480        490        500
SHFSSIPDAF WWAVVTMTTV GYGDMRPITV GGKIVGSLCA IAGVLTIALP 
       510        520        530        540        550
VPVIVSNFNY FYHRETDHEE QAALKEEQGN QRRESGLDTG GQRKVSCSKA 
       560        570        580        590        600
SFCKTGGSLE SSDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET 

DL
Length:602
Mass (Da):66,553
Last modified:November 1, 1990 - v1
<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:i6A784535FF226ED7
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 conflicti553C → S no nucleotide entry (PubMed:1705709).Curated1

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
M27158 Genomic DNA Translation: AAA41498.1
L23434 Genomic DNA Translation: AAA42337.1

Protein sequence database of the Protein Information Resource

More...PIRi		JH0166

NCBI Reference Sequences

More...RefSeqi		NP_037104.1, NM_012972.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000026691; ENSRNOP00000026691; ENSRNOG00000019719

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25470

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25470

UCSC genome browser

More...UCSCi		RGD:2953, 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
M27158 Genomic DNA Translation: AAA41498.1
L23434 Genomic DNA Translation: AAA42337.1
PIRiJH0166
RefSeqiNP_037104.1, NM_012972.1

3D structure databases

SMRiP19024
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi247503, 6 interactors
CORUMiP19024
IntActiP19024, 4 interactors
MINTiP19024
STRINGi10116.ENSRNOP00000026691

Chemistry databases

ChEMBLiCHEMBL4295724

Proteomic databases

PaxDbiP19024
PRIDEiP19024

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P19024, 1 sequenced antibody

Genome annotation databases

EnsembliENSRNOT00000026691; ENSRNOP00000026691; ENSRNOG00000019719
GeneIDi25470
KEGGirno:25470
UCSCiRGD:2953, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3741
RGDi2953, Kcna5

Phylogenomic databases

eggNOGiKOG1545, Eukaryota
GeneTreeiENSGT00940000161860
HOGENOMiCLU_011722_4_0_1
InParanoidiP19024
OMAiADHSPHL
OrthoDBi695337at2759
PhylomeDBiP19024
TreeFamiTF313103

Enzyme and pathway databases

ReactomeiR-RNO-1296072, Voltage gated Potassium channels

Miscellaneous databases

Protein Ontology

More...PROi		PR:P19024

Gene expression databases

BgeeiENSRNOG00000019719, Expressed in Ammon's horn and 17 other tissues
GenevisibleiP19024, RN

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
IPR003972, K_chnl_volt-dep_Kv1
IPR004052, K_chnl_volt-dep_Kv1.5
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
PRINTSiPR01512, KV15CHANNEL
PR01491, KVCHANNEL
PR01496, SHAKERCHANEL
SMARTiView protein in SMART
SM00225, BTB, 1 hit
SUPFAMiSSF54695, SSF54695, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiKCNA5_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: P19024
Secondary accession number(s): Q6LEB7
<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: November 1, 1990
Last sequence update: November 1, 1990
Last modified: December 2, 2020
This is version 170 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again