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Entry version 102 (02 Jun 2021)
Sequence version 2 (07 Oct 2020)
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Protein

Potassium voltage-gated channel subfamily KQT member 1

Gene

KCNQ1

Organism
Sus scrofa (Pig)
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 transcript 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

Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity).

Associates with KCNE beta subunits that modulates current kinetics (By similarity).

Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity).

Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity).

During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity).

Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity).

When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity).

This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity).

During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity).

Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity).

When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity).

When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity).

When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity).

Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity).

Binds with phosphatidylinositol 4,5-bisphosphate (By similarity).

By similarity

<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 functionCalmodulin-binding, Ion 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 KQT member 1By similarity
Alternative name(s):
IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1By similarity
KQT-like 1By similarity
Voltage-gated potassium channel subunit Kv7.1By similarity
<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:KCNQ1By similarity
Synonyms:KVLQT1By similarity
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<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
  • UP000314985 <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: Unassembled WGS sequence
  • UP000008227 Componenti: Chromosome 2

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:99782, KCNQ1

<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%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 – 119CytoplasmicCuratedAdd BLAST119
<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>Transmembranei120 – 140Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini141 – 145ExtracellularCurated5
Transmembranei146 – 166Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini167 – 194CytoplasmicCuratedAdd BLAST28
Transmembranei195 – 215Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini216 – 223ExtracellularCurated8
Transmembranei224 – 246Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST23
Topological domaini247 – 259CytoplasmicCuratedAdd BLAST13
Transmembranei260 – 280Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini281 – 297ExtracellularCuratedAdd BLAST17
<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>Intramembranei298 – 318Pore-forming; Name=Segment H5Sequence analysisAdd BLAST21
Topological domaini319 – 325ExtracellularCurated7
Transmembranei326 – 346Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini347 – 673CytoplasmicCuratedAdd BLAST327

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Membrane

<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_00000540251 – 673Potassium voltage-gated channel subfamily KQT member 1Add BLAST673

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 residuei27PhosphoserineBy similarity1
<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
Modified residuei405PhosphoserineBy similarity1
Modified residuei407PhosphoserineBy similarity1

<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

Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated form is internalized through a clathrin-mediated endocytosis by interacting with AP2M1 and is recycled back to the cell membrane via RAB4A and RAB11A.By similarity
Deubiquitinated by USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores the membrane localization.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9TTJ7

<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

Tetramer. Heterotetramer with KCNE1; targets to the membrane raft.

Interacts (via C-terminus) with CALM; forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner.

Interacts with AKAP9; targets protein kinase A (PKA) catalytic and regulatory subunits and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex, allowing PKA-mediated phosphorylation and increase of delayed rectifier potassium channel activity.

Interacts with KCNE2; form a heterooligomer complex that targets to the membrane raft and leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current.

Interacts with AP2M1; mediates estrogen-induced internalization via clathrin-coated vesicles.

Interacts with NEDD4L; promotes internalization and decreases I(Ks) currents.

Interacts with USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restore plasma membrane localization. Heterotetramer with KCNQ5; has a voltage-gated potassium channel activity.

Interacts with KCNE3; alters membrane raft localization.

Interacts with KCNE4; impairs KCNQ1 localization in lipid rafts and inhibits voltage-gated potassium channel activity.

Interacts with KCNE5; impairs KCNQ1 localization in lipid rafts and only conducts current upon strong and continued depolarization.

By similarity

GO - Molecular functioni

<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
Q9TTJ7

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>Regioni1 – 28DisorderedSequence analysisAdd BLAST28
Regioni61 – 80DisorderedSequence analysisAdd BLAST20
Regioni368 – 380Interaction with CALMBy similarityAdd BLAST13
Regioni514 – 528Interaction with CALM; calcium-dependentBy similarityAdd BLAST15
Regioni534 – 571Interaction with KCNE1 C-terminusBy similarityAdd BLAST38
Regioni587 – 615Interaction with AKAP9By similarityAdd BLAST29
Regioni588 – 619C-terminal assembly domainBy similarityAdd BLAST32
Regioni619 – 673DisorderedSequence analysisAdd BLAST55

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>Motifi310 – 315Selectivity 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 segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.By similarity
The C-terminal coiled-coil domain interacts with a single CALM molecule via the first two membrane-proximal helical regions, with CALM forming a clamp-like structure. Binding of CALM C-terminus to the first helical region is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to the second helical region is calcium-dependent and regulates electrophysiological activity of the channel.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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000161001

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9TTJ7

Database of Orthologous Groups

More...
OrthoDBi
1168835at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005821, Ion_trans_dom
IPR003937, K_chnl_volt-dep_KCNQ
IPR013821, K_chnl_volt-dep_KCNQ_C
IPR005827, K_chnl_volt-dep_KCQN1
IPR028325, VG_K_chnl

The PANTHER Classification System

More...
PANTHERi
PTHR11537, PTHR11537, 1 hit
PTHR11537:SF266, PTHR11537:SF266, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00520, Ion_trans, 1 hit
PF03520, KCNQ_channel, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01460, KCNQ1CHANNEL
PR01459, KCNQCHANNEL

<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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9TTJ7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAATSPPRA ERKRWGGGRL PGARRGSAGL AKKCPFSLEL AEGGPTGGAL
60 70 80 90 100
YAPIGPPGVP GPSSPAAPAA SPAAADLGPR PRVSLDPRVS IYSARRPLLA
110 120 130 140 150
RTHIQGRVYN FLERPTGWKC FVYHFAVFLI VLVCLIFSVL STIEQYVALA
160 170 180 190 200
TGTLFWMEIV LVVFFGTEYA VRLWSAGCRS KYVGIWGRLR FARKPISIID
210 220 230 240 250
LIVVVASMVV LCVGSKGQVF ATSAIRGIRF LQILRMLHVD RQGGTWRLLG
260 270 280 290 300
SVVFIHRQEL ITTLYIGFLG LIFSSYFVYL AEKDAVNESG QVEFGSYADA
310 320 330 340 350
LWWGVVTVTT IGYGDKVPQT WVGKTIASCF SVFAISFFAL PAGILGSGFA
360 370 380 390 400
LKVQQKQRQK HFNRQIPAAA SLIQTAWRCY AAENPDSSTW KIYVRKPSRS
410 420 430 440 450
QALLSPSPKP KKSVMVKKKK FKLDKDNGLS PGEKMLAVPQ ITCDLASEEQ
460 470 480 490 500
RPDHFSVDGC DNSVKKSPTL LEVSTAQFTR TNSFAEDLDL EGETLLTPIT
510 520 530 540 550
HVSQLREHHR ATIKVIRRMQ YFVAKKKFQQ ARKPYDVRDV IEQYSQGHLN
560 570 580 590 600
LMVRIKELQR RLDQSIGRPA LFISSSEKVK DRGSNTIGAR LNRVEDKVTQ
610 620 630 640 650
LDQRLELITD MLQQLLSLHR GGTPGSRAPG GGGAQVAQPC SGGSINPELF
660 670
LPSNALPTYE QLTVPGRGPE EGS
Length:673
Mass (Da):74,032
Last modified:October 7, 2020 - 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:i23F4B913CD83540F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A287AVP7A0A287AVP7_PIG
IKs producing slow voltage-gated po...
KCNQ1
771Annotation 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>
A0A5G2QST9A0A5G2QST9_PIG
IKs producing slow voltage-gated po...
KCNQ1
548Annotation score:

Annotation score:3 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>

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
AEMK02000006 Genomic DNA No translation available.
AB033207 mRNA Translation: BAA88580.1
DQIR01113270 Transcribed RNA Translation: HDA68746.1
DQIR01186501 Transcribed RNA Translation: HDB41978.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00000053475; ENSSSCP00000038521; ENSSSCG00000039556
ENSSSCT00025034227; ENSSSCP00025014257; ENSSSCG00025025273
ENSSSCT00030103028; ENSSSCP00030047532; ENSSSCG00030073514
ENSSSCT00045008924; ENSSSCP00045006061; ENSSSCG00045005372
ENSSSCT00050012936; ENSSSCP00050005361; ENSSSCG00050009557
ENSSSCT00055005087; ENSSSCP00055003934; ENSSSCG00055002634
ENSSSCT00060050141; ENSSSCP00060021453; ENSSSCG00060036994
ENSSSCT00065089963; ENSSSCP00065039344; ENSSSCG00065065522
ENSSSCT00070029507; ENSSSCP00070024595; ENSSSCG00070015013

<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
AEMK02000006 Genomic DNA No translation available.
AB033207 mRNA Translation: BAA88580.1
DQIR01113270 Transcribed RNA Translation: HDA68746.1
DQIR01186501 Transcribed RNA Translation: HDB41978.1

3D structure databases

SMRiQ9TTJ7
ModBaseiSearch...

Proteomic databases

PRIDEiQ9TTJ7

Genome annotation databases

EnsembliENSSSCT00000053475; ENSSSCP00000038521; ENSSSCG00000039556
ENSSSCT00025034227; ENSSSCP00025014257; ENSSSCG00025025273
ENSSSCT00030103028; ENSSSCP00030047532; ENSSSCG00030073514
ENSSSCT00045008924; ENSSSCP00045006061; ENSSSCG00045005372
ENSSSCT00050012936; ENSSSCP00050005361; ENSSSCG00050009557
ENSSSCT00055005087; ENSSSCP00055003934; ENSSSCG00055002634
ENSSSCT00060050141; ENSSSCP00060021453; ENSSSCG00060036994
ENSSSCT00065089963; ENSSSCP00065039344; ENSSSCG00065065522
ENSSSCT00070029507; ENSSSCP00070024595; ENSSSCG00070015013

Organism-specific databases

VGNCiVGNC:99782, KCNQ1

Phylogenomic databases

GeneTreeiENSGT00940000161001
InParanoidiQ9TTJ7
OrthoDBi1168835at2759

Family and domain databases

InterProiView protein in InterPro
IPR005821, Ion_trans_dom
IPR003937, K_chnl_volt-dep_KCNQ
IPR013821, K_chnl_volt-dep_KCNQ_C
IPR005827, K_chnl_volt-dep_KCQN1
IPR028325, VG_K_chnl
PANTHERiPTHR11537, PTHR11537, 1 hit
PTHR11537:SF266, PTHR11537:SF266, 1 hit
PfamiView protein in Pfam
PF00520, Ion_trans, 1 hit
PF03520, KCNQ_channel, 1 hit
PRINTSiPR01460, KCNQ1CHANNEL
PR01459, KCNQCHANNEL

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 nameiKCNQ1_PIG
<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: Q9TTJ7
Secondary accession number(s): A0A287A438
<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: June 1, 2001
Last sequence update: October 7, 2020
Last modified: June 2, 2021
This is version 102 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. SIMILARITY comments
    Index of protein domains and families
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