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Protein

Potassium voltage-gated channel subfamily KQT member 1

Gene

Kcnq1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) (PubMed:16314573, PubMed:11120752, PubMed:15004216). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PubMed:17597584, PubMed:15004216). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PubMed:8900282). 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) (PubMed:15004216, PubMed:17597584). 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 (PubMed:16314573). 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 (PubMed:19491250). When associated with KCNE2, forms an 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; has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity).By similarity6 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calmodulin-binding, Potassium

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.
R-MMU-5576890. Phase 3 - rapid repolarisation.
R-MMU-5576893. Phase 2 - plateau phase.

Protein family/group databases

TCDBi1.A.1.15.1. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily KQT member 1
Alternative name(s):
IKs producing slow voltage-gated potassium channel subunit alpha KvLQT11 Publication
KQT-like 1By similarity
Voltage-gated potassium channel subunit Kv7.1By similarity
Gene namesi
Name:Kcnq1Imported
Synonyms:Kcna9Imported, Kvlqt11 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:108083. Kcnq1.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasmic vesicle membrane By similarity
  • Early endosome By similarity
  • Membrane raft By similarity
  • Endoplasmic reticulum By similarity
  • Basolateral cell membrane By similarity

  • Note: Colocalized with KCNE3 at the plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained at the endoplasmic reticulum and is localized outside of lipid raft microdomains. During the early stages of epithelial cell polarization induced by the calcium switch it removed from plasma membrane to the endoplasmic reticulum where it retained and it is redistributed to the basolateral cell surface in a PI3K-dependent manner at a later stage.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei121 – 14121Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini142 – 1465ExtracellularSequence analysis
Transmembranei147 – 16721Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini168 – 19528CytoplasmicSequence analysisAdd
BLAST
Transmembranei196 – 21621Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini217 – 2248ExtracellularSequence analysis
Transmembranei225 – 24723Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini248 – 26013CytoplasmicSequence analysisAdd
BLAST
Transmembranei261 – 28121Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini282 – 29817ExtracellularSequence analysisAdd
BLAST
Intramembranei299 – 31921Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Topological domaini320 – 33011ExtracellularSequence analysisAdd
BLAST
Transmembranei331 – 35121Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini352 – 668317CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mice lacking Kcnq1 show an intestinal absorption impairment which is associated with reduced serum vitamin B12 concentrations, mild macrocytic anemia, and fecal loss of sodium and potassium ions (PubMed:16314573). Mice lacking Kcnq1 show microvillar secretory membranes intact, but basal acid secretion is absent and forskolin-stimulated acid output is reduced by approximately 90% in gastric mucosa (PubMed:19491250). Homozygous Kcnq1 mice develop normally and are viable, demonstrate hyperactivity, circling, and nodding behaviors; exhibit no electrocardiographic abnormalities but present a complete deafness, as well as circular movement and repetitive falling; show severe anatomic disruption of the cochlear and vestibular end organs; also display threefold enlargement by weight of the stomach resulting from mucous neck cell hyperplasia (PubMed:11120752). Mice neonates lacking Kcnq1 display significantly prolonged QT intervals during baseline ECG assessments which significantly increased following isoproterenol challenge; furthermore, the slow delayed rectifier potassium current (IKs) is absent (PubMed:15004216).4 Publications

Chemistry

GuidetoPHARMACOLOGYi560.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668Potassium voltage-gated channel subfamily KQT member 1PRO_0000054024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine; by PKABy similarity
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence analysis
Modified residuei406 – 4061PhosphoserineCombined sources
Modified residuei408 – 4081PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9.By similarity
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

PaxDbiP97414.
PRIDEiP97414.

PTM databases

iPTMnetiP97414.
PhosphoSiteiP97414.

Expressioni

Tissue specificityi

Expressed in heart, kidney and salivary glands. Detected in the cochlea. Almost undetectable in brain, skeletal muscle and liver. Widely expressed in embryonic and neonatal tissues.1 Publication

Gene expression databases

BgeeiP97414.
ExpressionAtlasiP97414. baseline and differential.
GenevisibleiP97414. MM.

Interactioni

Subunit structurei

Tetramer (By similarity). Heterotetramer with KCNE1; form the native cardiac channel I(Ks) which increases the amplitude and slows down the activation kinetics of outward potassium current and targets to the membrane raft (By similarity) (PubMed:8900282). Interacts (via C-terminus) with CALM; forms a heterotetramer 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 an 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).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP97414. 1 interaction.
STRINGi10090.ENSMUSP00000009689.

Structurei

3D structure databases

ProteinModelPortaliP97414.
SMRiP97414. Positions 146-423, 503-534, 584-610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni534 – 57138Interaction with KCNE1 C-terminusBy similarityAdd
BLAST
Regioni587 – 61529Interaction with AKAP9By similarityAdd
BLAST
Regioni588 – 61932C-terminal assembly domainBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili584 – 62037By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi311 – 3166Selectivity filterBy similarity

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 coiled-coil domain mediates tetramerization.By similarity
The segment S6 is involved in the inhibition of voltage-gated potassium channel activity by KCNE4.By similarity
The C-terminal assembly domain promotes self-interactiona; allows functional channel.By similarity

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1419. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00550000074513.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiP97414.
KOiK04926.
OMAiGWGRLPG.
OrthoDBiEOG73804Z.
TreeFamiTF315186.

Family and domain databases

InterProiIPR005821. 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.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 2 hits.
PTHR11537:SF151. PTHR11537:SF151. 2 hits.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01460. KCNQ1CHANNEL.
PR01459. KCNQCHANNEL.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform I (identifier: P97414-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDTASSPPSA ERKRAGWSRL LGARRGSAVV KKCPFSLELA EGGPEGSTVY
60 70 80 90 100
APIAPTGAPG LAPPMSTPVS PAPAPADLGP RPRVSLDPRV SIYSARRPLL
110 120 130 140 150
ARTHIQGRVY NFLERPTGWK CFVYHFTVFL IVLVCLIFSV LSTIEQYAAL
160 170 180 190 200
ATGTLFWMEI VLVVFFGTEY VVRLWSAGCR SKYVGIWGRL RFARKPISII
210 220 230 240 250
DLIVVVASMV VLCVGSKGQV FATSAIRGIR FLQILRMLHV DRQGGTWRLL
260 270 280 290 300
GSVVFIHRQE LITTLYIGFL GLIFSSYFVY LAEKDAVNES GRIEFGSYAD
310 320 330 340 350
ALWWGVVTVT TIGYGDKVPQ TWVGKTIASC FSVFAISFFA LPAGILGSGF
360 370 380 390 400
ALKVQQKQRQ KHFNRQIPAA ASLIQTAWRC YAAENPDSAT WKIYVRKPAR
410 420 430 440 450
SHTLLSPSPK PKKSVMVKKK KFKLDKDNGM SPGEKMFNVP HITYDPPEDR
460 470 480 490 500
RPDHFSIDGY DSSVRKSPTL LEVSTPHFLR TNSFAEDLDL EGETLLTPIT
510 520 530 540 550
HVSQLRDHHR ATIKVIRRMQ YFVAKKKFQQ ARKPYDVRDV IEQYSQGHLN
560 570 580 590 600
LMVRIKELQR RLDQSIGKPS LFIPISEKSK DRGSNTIGAR LNRVEDKVTQ
610 620 630 640 650
LDQRLVIITD MLHQLLSMQQ GGPTCNSRSQ VVASNEGGSI NPELFLPSNS
660
LPTYEQLTVP QTGPDEGS
Length:668
Mass (Da):74,514
Last modified:July 27, 2011 - v3
Checksum:i8CE35CBA3102B85B
GO
Isoform II (identifier: P97414-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: Missing.
     112-128: FLERPTGWKCFVYHFTV → MHQLPTSILIPKNMPGG

Show »
Length:557
Mass (Da):62,640
Checksum:i56D3B3EF5F8D0FA0
GO

Sequence cautioni

The sequence AAB36518.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti473 – 4731V → L in AAP93874 (PubMed:15004216).Curated
Sequence conflicti473 – 4731V → L in AAB36518 (PubMed:8900282).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111Missing in isoform II. CuratedVSP_011748Add
BLAST
Alternative sequencei112 – 12817FLERP…YHFTV → MHQLPTSILIPKNMPGG in isoform II. CuratedVSP_000983Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY331142 mRNA. Translation: AAP93874.1.
AK154244 mRNA. Translation: BAE32460.1.
BC045142 mRNA. Translation: AAH45142.2.
BC055304 mRNA. Translation: AAH55304.1.
U70068 mRNA. Translation: AAB36518.1. Different initiation.
AJ002201 mRNA. Translation: CAA05246.1.
CCDSiCCDS22039.1. [P97414-1]
RefSeqiNP_032460.2. NM_008434.2. [P97414-1]
XP_011240285.1. XM_011241983.1. [P97414-2]
UniGeneiMm.439769.
Mm.453036.
Mm.453037.

Genome annotation databases

EnsembliENSMUST00000009689; ENSMUSP00000009689; ENSMUSG00000009545. [P97414-1]
GeneIDi16535.
KEGGimmu:16535.
UCSCiuc009kpb.1. mouse. [P97414-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY331142 mRNA. Translation: AAP93874.1.
AK154244 mRNA. Translation: BAE32460.1.
BC045142 mRNA. Translation: AAH45142.2.
BC055304 mRNA. Translation: AAH55304.1.
U70068 mRNA. Translation: AAB36518.1. Different initiation.
AJ002201 mRNA. Translation: CAA05246.1.
CCDSiCCDS22039.1. [P97414-1]
RefSeqiNP_032460.2. NM_008434.2. [P97414-1]
XP_011240285.1. XM_011241983.1. [P97414-2]
UniGeneiMm.439769.
Mm.453036.
Mm.453037.

3D structure databases

ProteinModelPortaliP97414.
SMRiP97414. Positions 146-423, 503-534, 584-610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97414. 1 interaction.
STRINGi10090.ENSMUSP00000009689.

Chemistry

GuidetoPHARMACOLOGYi560.

Protein family/group databases

TCDBi1.A.1.15.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiP97414.
PhosphoSiteiP97414.

Proteomic databases

PaxDbiP97414.
PRIDEiP97414.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009689; ENSMUSP00000009689; ENSMUSG00000009545. [P97414-1]
GeneIDi16535.
KEGGimmu:16535.
UCSCiuc009kpb.1. mouse. [P97414-1]

Organism-specific databases

CTDi3784.
MGIiMGI:108083. Kcnq1.

Phylogenomic databases

eggNOGiKOG1419. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00550000074513.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiP97414.
KOiK04926.
OMAiGWGRLPG.
OrthoDBiEOG73804Z.
TreeFamiTF315186.

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.
R-MMU-5576890. Phase 3 - rapid repolarisation.
R-MMU-5576893. Phase 2 - plateau phase.

Miscellaneous databases

ChiTaRSiKcnq1. mouse.
PROiP97414.
SOURCEiSearch...

Gene expression databases

BgeeiP97414.
ExpressionAtlasiP97414. baseline and differential.
GenevisibleiP97414. MM.

Family and domain databases

InterProiIPR005821. 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.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 2 hits.
PTHR11537:SF151. PTHR11537:SF151. 2 hits.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01460. KCNQ1CHANNEL.
PR01459. KCNQCHANNEL.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isoproterenol exacerbates a long QT phenotype in Kcnq1-deficient neonatal mice: possible roles for human-like Kcnq1 isoform 1 and slow delayed rectifier K+ current."
    Knollmann B.C., Casimiro M.C., Katchman A.N., Sirenko S.G., Schober T., Rong Q., Pfeifer K., Ebert S.N.
    J. Pharmacol. Exp. Ther. 310:311-318(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), FUNCTION, DISRUPTION PHENOTYPE.
    Strain: 129/SvJ.
    Tissue: Heart.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
    Strain: NOD.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
    Strain: FVB/N.
    Tissue: Colon and Olfactory epithelium.
  4. "K(V)LQT1 and IsK (minK) proteins associate to form the I(Ks) cardiac potassium current."
    Barhanin J., Lesage F., Guillemare E., Fink M., Lazdunski M., Romey G.
    Nature 384:78-80(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-668 (ISOFORM I), FUNCTION, INTERACTION WITH KCNE1.
    Tissue: Heart.
  5. "Syntenic organization of the mouse distal chromosome 7 imprinting cluster and the Beckwith-Wiedemann syndrome region in chromosome 11p15.5."
    Paulsen M., Davies K.R., Bowden L.M., Villar A.J., Franck O., Fuermann M., Dean W.L., Moore T.F., Rodrigues N., Davies K.E., Hu R.-J., Feinberg A.P., Maher E.R., Reik W., Walter J.
    Hum. Mol. Genet. 7:1149-1159(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM II), TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  6. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  8. "Kcnq1 contributes to an adrenergic-sensitive steady-state K+ current in mouse heart."
    Knollmann B.C., Sirenko S., Rong Q., Katchman A.N., Casimiro M., Pfeifer K., Ebert S.N.
    Biochem. Biophys. Res. Commun. 360:212-218(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "KCNQ1 is the luminal K+ recycling channel during stimulation of gastric acid secretion."
    Song P., Groos S., Riederer B., Feng Z., Krabbenhoeft A., Smolka A., Seidler U.
    J. Physiol. (Lond.) 587:3955-3965(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney and Pancreas.

Entry informationi

Entry nameiKCNQ1_MOUSE
AccessioniPrimary (citable) accession number: P97414
Secondary accession number(s): O88702
, Q3U4H1, Q7TNZ1, Q7TPL7, Q80VR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.