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O43526 (KCNQ2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily KQT member 2
Alternative name(s):
KQT-like 2
Neuroblastoma-specific potassium channel subunit alpha KvLQT2
Voltage-gated potassium channel subunit Kv7.2
Gene names
Name:KCNQ2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length872 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. KCNQ2/KCNQ3 current is blocked by linopirdine and XE991, and activated by the anticonvulsant retigabine. Muscarinic agonist oxotremorine-M strongly suppress KCNQ2/KCNQ3 current in cells in which cloned KCNQ2/KCNQ3 channels were coexpressed with M1 muscarinic receptors.

Subunit structure

Heteromultimer with KCNQ3. May associate with KCNE2.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

In adult and fetal brain. Highly expressed in areas containing neuronal cell bodies, low in spinal chord and corpus callosum. Isoform 2 is preferentially expressed in differentiated neurons. Isoform 6 is prominent in fetal brain, undifferentiated neuroblastoma cells and brain tumors. Ref.19

Domain

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.

Post-translational modification

In Xenopus oocytes KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminus region.

Involvement in disease

Seizures, benign familial neonatal 1 (BFNS1) [MIM:121200]: A disorder characterized by clusters of seizures occurring in the first days of life. Most patients have spontaneous remission by 12 months of age and show normal psychomotor development. Some rare cases manifest an atypical severe phenotype associated with epileptic encephalopathy and psychomotor retardation. The disorder is distinguished from benign familial infantile seizures by an earlier age at onset. In some patients, neonatal convulsions are followed later in life by myokymia, a benign condition characterized by spontaneous involuntary contractions of skeletal muscles fiber groups that can be observed as vermiform movement of the overlying skin. Electromyography typically shows continuous motor unit activity with spontaneous oligo- and multiplet-discharges of high intraburst frequency (myokymic discharges). Some patients may have isolated myokymia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.23 Ref.24 Ref.25 Ref.27

Epileptic encephalopathy, early infantile, 7 (EIEE7) [MIM:613720]: An autosomal dominant seizure disorder characterized by infantile onset of refractory seizures with resultant delayed neurologic development and persistent neurologic abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.27

Miscellaneous

Inclusion of isoform 6 in heteromultimers results in attenuation of potassium current. Prominent expression of isoform 6 in the developing brain may alter firing repertoires of immature neurons excitability to provide cues for proliferation rather than differentiation.

Mutagenesis experiments were carried out in Xenopus oocytes by coexpression of either KCNQ2(mut) and KCNQ3 at the ratio of 1:1, or of KCNQ2(mut), KCNQ2(wt) and KCNQ3 at the ratio of 1:1:2, to mimic the situation in a heterozygous patient with BFNC1 disease.

Sequence similarities

Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.2/KCNQ2 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epilepsy
Mental retardation
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

nervous system development

Traceable author statement Ref.2. Source: ProtInc

potassium ion transport

Traceable author statement Ref.6. Source: ProtInc

synaptic transmission

Traceable author statement. Source: Reactome

transmission of nerve impulse

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon initial segment

Inferred from sequence or structural similarity PubMed 16525039. Source: BHF-UCL

node of Ranvier

Inferred from sequence or structural similarity PubMed 16525039. Source: BHF-UCL

plasma membrane

Inferred from sequence or structural similarity PubMed 16525039. Source: BHF-UCL

voltage-gated potassium channel complex

Traceable author statement Ref.6. Source: ProtInc

   Molecular_functionankyrin binding

Inferred from physical interaction PubMed 16525039. Source: BHF-UCL

delayed rectifier potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium channel activity

Traceable author statement Ref.3. Source: ProtInc

voltage-gated potassium channel activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O43526-1)

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.
Isoform 2 (identifier: O43526-2)

The sequence of this isoform differs from the canonical sequence as follows:
     417-434: Missing.
Isoform 3 (identifier: O43526-3)

The sequence of this isoform differs from the canonical sequence as follows:
     373-382: Missing.
     417-434: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 4 (identifier: O43526-4)

The sequence of this isoform differs from the canonical sequence as follows:
     417-446: Missing.
     509-509: Missing.
Isoform 5 (identifier: O43526-5)

The sequence of this isoform differs from the canonical sequence as follows:
     310-320: Missing.
     417-434: Missing.
Isoform 6 (identifier: O43526-6)

Also known as: HNSPC;

The sequence of this isoform differs from the canonical sequence as follows:
     373-393: SSQTQTYGASRLIPPLNQLEL → RYRRRAPATKQLFHFLFSICS
     394-872: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 872872Potassium voltage-gated channel subfamily KQT member 2
PRO_0000054030

Regions

Transmembrane92 – 11221Helical; Name=Segment S1; Potential
Topological domain113 – 12210Extracellular Potential
Transmembrane123 – 14321Helical; Name=Segment S2; Potential
Topological domain144 – 16623Cytoplasmic Potential
Transmembrane167 – 18721Helical; Name=Segment S3; Potential
Topological domain188 – 1958Extracellular Potential
Transmembrane196 – 21823Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain219 – 23113Cytoplasmic Potential
Transmembrane232 – 25221Helical; Name=Segment S5; Potential
Topological domain253 – 26412Extracellular Potential
Intramembrane265 – 28521Pore-forming; Name=Segment H5; Potential
Topological domain286 – 2916Extracellular Potential
Transmembrane292 – 31221Helical; Name=Segment S6; Potential
Topological domain313 – 872560Cytoplasmic Potential
Motif277 – 2826Selectivity filter By similarity

Amino acid modifications

Modified residue521Phosphoserine; by PKA Ref.10
Modified residue2171Phosphothreonine Ref.21

Natural variations

Alternative sequence310 – 32011Missing in isoform 5.
VSP_000984
Alternative sequence373 – 39321SSQTQ…NQLEL → RYRRRAPATKQLFHFLFSIC S in isoform 6.
VSP_000986
Alternative sequence373 – 38210Missing in isoform 3.
VSP_000985
Alternative sequence394 – 872479Missing in isoform 6.
VSP_000987
Alternative sequence417 – 44630Missing in isoform 4.
VSP_000989
Alternative sequence417 – 43418Missing in isoform 2, isoform 3 and isoform 5.
VSP_000988
Alternative sequence5091Missing in isoform 4.
VSP_000990
Natural variant2071R → Q in a patient with isolated myokymia and no history of neonatal seizures; leads to a shift of voltage-dependent activation. Ref.28
VAR_043819
Natural variant2071R → W in BFNS1; phenotype manifestations include myokymia in some patients; leads to a shift of voltage-dependent activation of the channel and a dramatic slowing of activation upon depolarization. Ref.24
VAR_026987
Natural variant2081M → V in BFNS1; minor effect on maximal current but clearly exhibits a faster rate of deactivation. Ref.25
VAR_026988
Natural variant2141R → W in BFNS1. Ref.23
Corresponds to variant rs28939684 [ dbSNP | Ensembl ].
VAR_010929
Natural variant2281H → Q in BFNS1. Ref.25
VAR_026989
Natural variant2431L → F in BFNS1. Ref.25
VAR_026990
Natural variant2471S → W in EIEE7; reduces channel currents by more than 50% in homomeric channels. Ref.26
VAR_026991
Natural variant2841Y → C in BFNS1; 30%-60% reduction of wt heteromeric current. Ratio 1:1 or 20%-30%; ratio of 1:1:2. Ref.2 Ref.10 Ref.25
Corresponds to variant rs28939683 [ dbSNP | Ensembl ].
VAR_010930
Natural variant3061A → T in BFNS1; 20%-40% reduction of wt heteromeric current. Ratio of 1:1:2. Ref.2 Ref.10 Ref.25
VAR_010931
Natural variant3331R → Q in BFNS1; moderate effect; less than 50% reduction in current compared with wt heteromeric channels. Ref.25
VAR_026992
Natural variant5541K → N in BFNS1 and EIEE7; decreases the voltage-dependence of the channel. Ref.27
VAR_026993
Natural variant7801N → T. Ref.22
Corresponds to variant rs1801475 [ dbSNP | Ensembl ].
VAR_010932

Experimental info

Mutagenesis521S → E: 40% increase in potassium current amplitude. Ratio of 1:1. Ref.10
Mutagenesis521S → Q: Decrease of PKA stimulation. Ratio of 1:1. Ref.10
Mutagenesis2171T → A: No effect on current or expression. Ref.21
Mutagenesis2171T → D: Abolishes currents without reducing channel protein expression. Ref.21
Mutagenesis2791G → S: More than 50% reduction of wt heteromeric current. Ratio of 1:1 and 1:1:2. Ref.10
Sequence conflict6991K → E in AAD16988. Ref.4
Sequence conflict8541R → C in AAD16988. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 22E8A0880A27B58C

FASTA87295,848
        10         20         30         40         50         60 
MVQKSRNGGV YPGPSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR GSILSKPRAG 

        70         80         90        100        110        120 
GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK 

       130        140        150        160        170        180 
SSEGALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASI 

       190        200        210        220        230        240 
AVLAAGSQGN VFATSALRSL RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF 

       250        260        270        280        290        300 
LCLILASFLV YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI 

       310        320        330        340        350        360 
GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QSAWRFYATN LSRTDLHSTW 

       370        380        390        400        410        420 
QYYERTVTVP MYSSQTQTYG ASRLIPPLNQ LELLRNLKSK SGLAFRKDPP PEPSPSKGSP 

       430        440        450        460        470        480 
CRGPLCGCCP GRSSQKVSLK DRVFSSPRGV AAKGKGSPQA QTVRRSPSAD QSLEDSPSKV 

       490        500        510        520        530        540 
PKSWSFGDRS RARQAFRIKG AASRQNSEEA SLPGEDIVDD KSCPCEFVTE DLTPGLKVSI 

       550        560        570        580        590        600 
RAVCVMRFLV SKRKFKESLR PYDVMDVIEQ YSAGHLDMLS RIKSLQSRVD QIVGRGPAIT 

       610        620        630        640        650        660 
DKDRTKGPAE AELPEDPSMM GRLGKVEKQV LSMEKKLDFL VNIYMQRMGI PPTETEAYFG 

       670        680        690        700        710        720 
AKEPEPAPPY HSPEDSREHV DRHGCIVKIV RSSSSTGQKN FSAPPAAPPV QCPPSTSWQP 

       730        740        750        760        770        780 
QSHPRQGHGT SPVGDHGSLV RIPPPPAHER SLSAYGGGNR ASMEFLRQED TPGCRPPEGN 

       790        800        810        820        830        840 
LRDSDTSISI PSVDHEELER SFSGFSISQS KENLDALNSC YAAVAPCAKV RPYIAEGESD 

       850        860        870 
TDSDLCTPCG PPPRSATGEG PFGDVGWAGP RK 

« Hide

Isoform 2 [UniParc].

Checksum: CF3F5EC2E23E21FC
Show »

FASTA85494,100
Isoform 3 [UniParc].

Checksum: 5228E1B8C3D8C17F
Show »

FASTA84493,089
Isoform 4 [UniParc].

Checksum: 065E37AF63726B10
Show »

FASTA84192,596
Isoform 5 [UniParc].

Checksum: AF6F5146789F4167
Show »

FASTA84393,057
Isoform 6 (HNSPC) [UniParc].

Checksum: 9415BC4FC2F84675
Show »

FASTA39344,261

References

« Hide 'large scale' references
[1]"Identification and cloning of neuroblastoma-specific and nerve tissue-specific genes through compiled expression profiles."
Yokoyama M., Nishi Y., Yoshii J., Okubo K., Matsubara K.
DNA Res. 3:311-320(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
Tissue: Neuroblastoma.
[2]"A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns."
Singh N.A., Charlier C., Stauffer D., DuPont B.R., Leach R.J., Melis R., Ronen G.M., Bjerre I., Quattlebaum T., Murphy J.V., McHarg M.L., Gagnon D., Rosales T.O., Peiffer A., Anderson V.E., Leppert M.
Nat. Genet. 18:25-29(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS BFNS1 CYS-284 AND THR-306.
Tissue: Brain, Fetal brain and Temporal cortex.
[3]"A potassium channel mutation in neonatal human epilepsy."
Biervert C., Schroeder B.C., Kubisch C., Berkovic S.F., Propping P., Jentsch T.J., Steinlein O.K.
Science 279:403-406(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Fetal brain.
[4]"KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel."
Wang H.-S., Pan Z., Shi W., Brown B.S., Wymore R.S., Cohen I.S., Dixon J.E., McKinnon D.
Science 282:1890-1893(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[5]"The KCNQ2 potassium channel: splice variants, functional and developmental expression. Brain localization and comparison with KCNQ3."
Tinel N., Lauritzen I., Chouabe C., Lazdunski M., Borsotto M.
FEBS Lett. 438:171-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5).
[6]"Functional expression of two KvLQT1-related potassium channels responsible for an inherited idiopathic epilepsy."
Yang W.-P., Levesque P.C., Little W.A., Conder M.L., Ramakrishnan P., Neubauer M.G., Blanar M.A.
J. Biol. Chem. 273:19419-19423(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Brain and Fetal brain.
[7]"Differential expression of KCNQ2 splice variants: implications to M current function during neuronal development."
Smith J.S., Iannotti C.A., Dargis P.G., Christian E.P., Aiyar J.
J. Neurosci. 21:1096-1103(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[8]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 6).
Tissue: Eye.
[10]"Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy."
Schroeder B.C., Kubisch C., Stein V., Jentsch T.J.
Nature 396:687-690(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-52 AND GLY-279, PHOSPHORYLATION AT SER-52, CHARACTERIZATION OF VARIANTS CYS-284 AND THR-306.
[11]"Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute to the M-like current in a mammalian neuronal cell."
Selyanko A.A., Hadley J.K., Wood I.C., Abogadie F.C., Delmas P., Buckley N.J., London B., Brown D.A.
J. Neurosci. 19:7742-7756(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN M-LIKE CURRENT.
[12]"M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2 subunit."
Tinel N., Diochot S., Lauritzen I., Barhanin J., Lazdunski M., Borsotto M.
FEBS Lett. 480:137-141(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH KCNE2.
[13]"Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy."
Schwake M., Pusch M., Kharkovets T., Jentsch T.J.
J. Biol. Chem. 275:13343-13348(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SURFACE EXPRESSION OF HETEROMERS.
[14]"Reconstitution of muscarinic modulation of the KCNQ2/KCNQ3 K(+) channels that underlie the neuronal M current."
Shapiro M.S., Roche J.P., Kaftan E.J., Cruzblanca H., Mackie K., Hille B.
J. Neurosci. 20:1710-1721(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY M1 MUSCARINIC RECEPTORS.
[15]"Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors."
Selyanko A.A., Hadley J.K., Wood I.C., Abogadie F.C., Jentsch T.J., Brown D.A.
J. Physiol. (Lond.) 522:349-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY M1 MUSCARINIC RECEPTORS.
[16]"Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine."
Main M.J., Cryan J.E., Dupere J.R., Cox B., Clare J.J., Burbidge S.A.
Mol. Pharmacol. 58:253-262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY RETICABINE.
[17]"Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3 potassium channels."
Wickenden A.D., Yu W., Zou A., Jegla T., Wagoner P.K.
Mol. Pharmacol. 58:591-600(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY RETICABINE.
[18]"The novel anticonvulsant retigabine activates M-currents in Chinese hamster ovary-cells transfected with human KCNQ2/3 subunits."
Rundfeldt C., Netzer R.
Neurosci. Lett. 282:73-76(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY RETICABINE.
[19]"Colocalization and coassembly of two human brain M-type potassium channel subunits that are mutated in epilepsy."
Cooper E.C., Aldape K.D., Abosch A., Barbaro N.M., Berger M.S., Peacock W.S., Jan Y.N., Jan L.Y.
Proc. Natl. Acad. Sci. U.S.A. 97:4914-4919(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, BIOCHEMICAL CHARACTERIZATION.
[20]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[21]"Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels."
Surti T.S., Huang L., Jan Y.N., Jan L.Y., Cooper E.C.
Proc. Natl. Acad. Sci. U.S.A. 102:17828-17833(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-217, MUTAGENESIS OF THR-217.
[22]"Structural and mutational analysis of KCNQ2, the major gene locus for benign familial neonatal convulsions."
Biervert C., Steinlein O.K.
Hum. Genet. 104:234-240(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-780.
[23]"Benign familial neonatal convulsions (BFNC) resulting from mutation of the KCNQ2 voltage sensor."
Miraglia del Giudice E., Coppola G., Scuccimarra G., Cirillo G., Bellini G., Pascotto A.
Eur. J. Hum. Genet. 8:994-997(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BFNS1 TRP-214.
[24]"Myokymia and neonatal epilepsy caused by a mutation in the voltage sensor of the KCNQ2 K+ channel."
Dedek K., Kunath B., Kananura C., Reuner U., Jentsch T.J., Steinlein O.K.
Proc. Natl. Acad. Sci. U.S.A. 98:12272-12277(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BFNS1 TRP-207, CHARACTERIZATION OF VARIANT BFNS1 TRP-207.
[25]"KCNQ2 and KCNQ3 potassium channel genes in benign familial neonatal convulsions: expansion of the functional and mutation spectrum."
The BFNC physician consortium
Singh N.A., Westenskow P., Charlier C., Pappas C., Leslie J., Dillon J., Anderson V.E., Sanguinetti M.C., Leppert M.F.
Brain 126:2726-2737(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BFNS1 VAL-208; GLN-228; PHE-243; CYS-284; THR-306 AND GLN-333, CHARACTERIZATION OF VARIANTS BFNS1 VAL-208 AND GLN-333.
[26]"Neonatal convulsions and epileptic encephalopathy in an Italian family with a missense mutation in the fifth transmembrane region of KCNQ2."
Dedek K., Fusco L., Teloy N., Steinlein O.K.
Epilepsy Res. 54:21-27(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EIEE7 TRP-247, CHARACTERIZATION OF VARIANT EIEE7 TRP-247.
[27]"A novel mutation in KCNQ2 associated with BFNC, drug resistant epilepsy, and mental retardation."
Borgatti R., Zucca C., Cavallini A., Ferrario M., Panzeri C., Castaldo P., Soldovieri M.V., Baschirotto C., Bresolin N., Dalla Bernardina B., Taglialatela M., Bassi M.T.
Neurology 63:57-65(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BFNS1 ASN-554, VARIANT EIEE7 ASN-554, CHARACTERIZATION OF VARIANT BFNS1 ASN-554.
[28]"Peripheral nerve hyperexcitability due to dominant-negative KCNQ2 mutations."
Wuttke T.V., Jurkat-Rott K., Paulus W., Garncarek M., Lehmann-Horn F., Lerche H.
Neurology 69:2045-2053(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-207, CHARACTERIZATION OF VARIANT GLN-207.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D82346 mRNA. Translation: BAA11557.1.
AF033348 mRNA. Translation: AAB97315.1.
Y15065 mRNA. Translation: CAA75348.1.
AF110020 mRNA. Translation: AAD16988.1.
AF074247 mRNA. Translation: AAC25921.1.
AL353658, AL121827, AL121829 Genomic DNA. Translation: CAH72958.1.
AL353658, AL121827, AL121829 Genomic DNA. Translation: CAH72959.1.
AL121827, AL121829, AL353658 Genomic DNA. Translation: CAI95054.1.
AL121829, AL121827, AL353658 Genomic DNA. Translation: CAI95740.1.
AL121829, AL121827, AL353658 Genomic DNA. Translation: CAI95744.1.
BC000699 mRNA. Translation: AAH00699.1.
PIRJC5275.
RefSeqNP_004509.2. NM_004518.4.
NP_742104.1. NM_172106.1.
NP_742105.1. NM_172107.2.
NP_742106.1. NM_172108.3.
NP_742107.1. NM_172109.1.
UniGeneHs.161851.
Hs.652468.

3D structure databases

ProteinModelPortalO43526.
SMRO43526. Positions 65-316, 530-555, 615-644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109986. 5 interactions.
IntActO43526. 1 interaction.
MINTMINT-8402812.
STRING9606.ENSP00000352035.

Chemistry

BindingDBO43526.
ChEMBLCHEMBL2363063.
DrugBankDB00321. Amitriptyline.
GuidetoPHARMACOLOGY561.

Protein family/group databases

TCDB1.A.1.15.2. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteO43526.

Proteomic databases

PaxDbO43526.
PRIDEO43526.

Protocols and materials databases

DNASU3785.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344425; ENSP00000345523; ENSG00000075043. [O43526-6]
ENST00000344462; ENSP00000339611; ENSG00000075043. [O43526-4]
ENST00000357249; ENSP00000349789; ENSG00000075043. [O43526-2]
ENST00000359125; ENSP00000352035; ENSG00000075043. [O43526-1]
ENST00000360480; ENSP00000353668; ENSG00000075043. [O43526-3]
GeneID3785.
KEGGhsa:3785.
UCSCuc002yey.1. human. [O43526-1]
uc002yez.1. human. [O43526-4]
uc002yfa.1. human. [O43526-2]
uc002yfb.1. human. [O43526-3]

Organism-specific databases

CTD3785.
GeneCardsGC20M062038.
HGNCHGNC:6296. KCNQ2.
HPAHPA016642.
MIM121200. phenotype.
602235. gene.
613720. phenotype.
neXtProtNX_O43526.
Orphanet306. Benign familial infantile seizures.
1949. Benign familial neonatal seizures.
140927. Benign familial neonatal-infantile seizures.
1934. Early infantile epileptic encephalopathy.
PharmGKBPA30074.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOVERGENHBG059014.
KOK04927.
OrthoDBEOG73804Z.
PhylomeDBO43526.
TreeFamTF315186.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressO43526.
BgeeO43526.
CleanExHS_KCNQ2.
GenevestigatorO43526.

Family and domain databases

InterProIPR020969. Ankyrin-G_BS.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR003947. K_chnl_volt-dep_KCNQ2.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
PF11956. KCNQC3-Ank-G_bd. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01461. KCNQ2CHANNEL.
PR01459. KCNQCHANNEL.
ProtoNetSearch...

Other

ChiTaRSKCNQ2. human.
GeneWikiKvLQT2.
GenomeRNAi3785.
NextBio14859.
PROO43526.
SOURCESearch...

Entry information

Entry nameKCNQ2_HUMAN
AccessionPrimary (citable) accession number: O43526
Secondary accession number(s): O43796 expand/collapse secondary AC list , O75580, O95845, Q4VXP4, Q4VXR6, Q5VYT8, Q96J59, Q99454
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM