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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
KCNQ2_HUMAN, Homo sapiens (human) KCNQ2 Voltage-gated potassium channel subunit Kv7.2 Functions
wild_type
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Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended 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
Protein IDs
(Accession numbers)
UniProtKB
 O43526
NCBI RefSeq

NP_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.
Organism
Latin Name/
(Common Name)
Homo sapiens (Human).
Taxonomic Identifier (NCBI)
 9606
Gene Names
 KCNQ2 [GenPool]
GeneID

3785
Genome
Annotation (Ensembl)

ENST00000359125, ENSP00000352035; ENSG00000075043
Protein Sequence
 
SEQUENCE   872 AA;  95848 MW;  22E8A0880A27B58C CRC64;
MVQKSRNGGV YPGPSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR GSILSKPRAG
GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK
SSEGALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASI
AVLAAGSQGN VFATSALRSL RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF
LCLILASFLV YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI
GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QSAWRFYATN LSRTDLHSTW
QYYERTVTVP MYSSQTQTYG ASRLIPPLNQ LELLRNLKSK SGLAFRKDPP PEPSPSKGSP
CRGPLCGCCP GRSSQKVSLK DRVFSSPRGV AAKGKGSPQA QTVRRSPSAD QSLEDSPSKV
PKSWSFGDRS RARQAFRIKG AASRQNSEEA SLPGEDIVDD KSCPCEFVTE DLTPGLKVSI
RAVCVMRFLV SKRKFKESLR PYDVMDVIEQ YSAGHLDMLS RIKSLQSRVD QIVGRGPAIT
DKDRTKGPAE AELPEDPSMM GRLGKVEKQV LSMEKKLDFL VNIYMQRMGI PPTETEAYFG
AKEPEPAPPY HSPEDSREHV DRHGCIVKIV RSSSSTGQKN FSAPPAAPPV QCPPSTSWQP
QSHPRQGHGT SPVGDHGSLV RIPPPPAHER SLSAYGGGNR ASMEFLRQED TPGCRPPEGN
LRDSDTSISI PSVDHEELER SFSGFSISQS KENLDALNSC YAAVAPCAKV RPYIAEGESD
TDSDLCTPCG PPPRSATGEG PFGDVGWAGP RK
General annotation
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.
Cofactor
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.
Induction
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 beincreased by intracellular cyclic AMP, an effect that depends onphosphorylation of Ser-52 in the N-terminus region.
Involvement in disease

Defects in KCNQ2 are the cause of benign neonatal epilepsy type 1 (EBN1) [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.

Defects in KCNQ2 are the cause of epileptic encephalopathy early infantile type 7 (EIEE7) [MIM:613720]. EIEE7 is an autosomal dominant seizure disorder characterized by infantile onset of refractory seizures with resultant delayed neurologic development and persistent neurologic abnormalities.
References

  • "Identification and cloning of neuroblastoma-specific and nervetissue-specific genes through compiled expression profiles.";,Yokoyama M., Nishi Y., Yoshii J., Okubo K., Matsubara K.;,DNA Res. 3:311-320(1996)., PubMeb:9039501 DOI:10.1093/dnares/3.5.311

  • "A novel potassium channel gene, KCNQ2, is mutated in an inheritedepilepsy 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)., PubMeb:9425895 DOI:10.1038/ng0198-25

  • "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)., PubMeb:9430594 DOI:10.1126/science.279.5349.403

  • "KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates ofthe 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)., PubMeb:9836639 DOI:10.1126/science.282.5395.1890

  • "The KCNQ2 potassium channel: splice variants, functional anddevelopmental expression. Brain localization and comparison withKCNQ3.";,Tinel N., Lauritzen I., Chouabe C., Lazdunski M., Borsotto M.;,FEBS Lett. 438:171-176(1998)., PubMeb:9827540 DOI:10.1016/S0014-5793(98)01296-4

  • "Functional expression of two KvLQT1-related potassium channelsresponsible 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)., PubMeb:9677360 DOI:10.1074/jbc.273.31.19419

  • "Differential expression of KCNQ2 splice variants: implications to Mcurrent function during neuronal development.";,Smith J.S., Iannotti C.A., Dargis P.G., Christian E.P., Aiyar J.;,J. Neurosci. 21:1096-1103(2001)., PubMeb:11160379

  • "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., 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)., PubMeb:11780052 DOI:10.1038/414865a

  • "The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).";,Genome Res. 14:2121-2127(2004).,PubMeb:15489334 DOI:10.1101/gr.2596504

  • "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)., PubMeb:9872318 DOI:10.1038/25367

  • "Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute tothe 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)., PubMeb:10479678

  • "M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2subunit.";,Tinel N., Diochot S., Lauritzen I., Barhanin J., Lazdunski M.,Borsotto M.;,FEBS Lett. 480:137-141(2000)., PubMeb:11034315 DOI:10.1016/S0014-5793(00)01918-9

  • "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)., PubMeb:10788442 DOI:10.1074/jbc.275.18.13343

  • "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)., PubMeb:10684873

  • "Inhibition of KCNQ1-4 potassium channels expressed in mammalian cellsvia 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)., PubMeb:10713961DOI:10.1111/j.1469-7793.2000.t01-2-00349.x

  • "Modulation of KCNQ2/3 potassium channels by the novel anticonvulsantretigabine.";,Main M.J., Cryan J.E., Dupere J.R., Cox B., Clare J.J., Burbidge S.A.;,Mol. Pharmacol. 58:253-262(2000)., PubMeb:10908292

  • "Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3potassium channels.";,Wickenden A.D., Yu W., Zou A., Jegla T., Wagoner P.K.;,Mol. Pharmacol. 58:591-600(2000)., PubMeb:10953053

  • "The novel anticonvulsant retigabine activates M-currents in Chinesehamster ovary-cells tranfected with human KCNQ2/3 subunits.";,Rundfeldt C., Netzer R.;,Neurosci. Lett. 282:73-76(2000)., PubMeb:10713399 DOI:10.1016/S0304-3940(00)00866-1

  • "Colocalization and coassembly of two human brain M-type potassiumchannel 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)., PubMeb:10781098 DOI:10.1073/pnas.090092797

  • "An unappreciated role for RNA surveillance.";,Hillman R.T., Green R.E., Brenner S.E.;,Genome Biol. 5:R8.1-R8.16(2004).,PubMeb:14759258 DOI:10.1186/gb-2004-5-2-r8

  • "Structural and mutational analysis of KCNQ2, the major gene locus forbenign familial neonatal convulsions.";,Biervert C., Steinlein O.K.;,Hum. Genet. 104:234-240(1999)., PubMeb:10323247 DOI:10.1007/s004390050941

  • "Benign familial neonatal convulsions (BFNC) resulting from mutationof 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)., PubMeb:11175290 DOI:10.1038/sj.ejhg.5200570

  • "Myokymia and neonatal epilepsy caused by a mutation in the voltagesensor 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).,PubMeb:11572947 DOI:10.1073/pnas.211431298

  • "KCNQ2 and KCNQ3 potassium channel genes in benign familial neonatalconvulsions: expansion of the functional and mutation spectrum.";,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).,PubMeb:14534157 DOI:10.1093/brain/awg286

  • "Neonatal convulsions and epileptic encephalopathy in an Italianfamily with a missense mutation in the fifth transmembrane region ofKCNQ2.";,Dedek K., Fusco L., Teloy N., Steinlein O.K.;,Epilepsy Res. 54:21-27(2003).,PubMeb:12742592 DOI:10.1016/S0920-1211(03)00037-8

  • "A novel mutation in KCNQ2 associated with BFNC, drug resistantepilepsy, 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).,PubMeb:15249611

  • "Peripheral nerve hyperexcitability due to dominant-negative KCNQ2mutations.";,Wuttke T.V., Jurkat-Rott K., Paulus W., Garncarek M., Lehmann-Horn F.,Lerche H.;,Neurology 69:2045-2053(2007).,PubMeb:17872363 DOI:10.1212/01.wnl.0000275523.95103.36

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Protein Domain Databases
InterPro

IPR020969, Ankyrin-G_BS.

IPR005821, Ion_trans.

IPR003091, K_chnl.

IPR003937, K_chnl_volt-dep_KCNQ.

IPR003947, K_chnl_volt-dep_KCNQ2.

IPR013821, K_chnl_volt-dep_KCNQ_C.
Gene3D
PANTHER
Pfam

PF00520, Ion_trans; 1.

PF03520, KCNQ_channel; 1.

PF11956, KCNQC3-Ank-G_bd; 1.
PRINTS

PR00169, KCHANNEL.

PR01461, KCNQ2CHANNEL.

PR01459, KCNQCHANNEL.
SUPFAM
PROSITE
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Polypeptide chain 1 - 872 872 Potassium voltage-gated channel subfamily /FTId=PRO_0000054030.
Transmembrane region 92 - 112 21 Helical; Name=Segment S1; (Potential).
Transmembrane region 123 - 143 21 Helical; Name=Segment S2; (Potential).
Transmembrane region 167 - 187 21 Helical; Name=Segment S3; (Potential).
Transmembrane region 196 - 218 23 Helical; Voltage-sensor; Name=Segment S4;
Transmembrane region 232 - 252 21 Helical; Name=Segment S5; (Potential).
Transmembrane region 292 - 312 21 Helical; Name=Segment S6; (Potential).
Topological domain 113 - 122 10 Extracellular (Potential).
Topological domain 144 - 166 23 Cytoplasmic (Potential).
Topological domain 188 - 195 8 Extracellular (Potential).
Topological domain 219 - 231 13 Cytoplasmic (Potential).
Topological domain 253 - 264 12 Extracellular (Potential).
Topological domain 286 - 291 6 Extracellular (Potential).
Topological domain 313 - 872 560 Cytoplasmic (Potential).
Located in a membrane without crossing it 265 - 285 21 Pore-forming; Name=Segment H5;
Sequence motif 277 - 282 6 Selectivity filter (By similarity).
Posttranslational modification of a residue 52 1 Phosphoserine; by PKA.
Posttranslational modification of a residue 466 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 468 1 Phosphoserine (By similarity).
Natural variance 310 - 320 11 Missing (in isoform 5). /FTId=VSP_000984.
Natural variance 373 - 393 21 SSQTQTYGASRLIPPLNQLEL -> RYRRRAPATKQLFHFL /FTId=VSP_000986.
Natural variance 373 - 382 10 Missing (in isoform 3). /FTId=VSP_000985.
Natural variance 394 - 872 479 Missing (in isoform 6). /FTId=VSP_000987.
Natural variance 417 - 446 30 Missing (in isoform 4). /FTId=VSP_000989.
Natural variance 417 - 434 18 Missing (in isoform 2, isoform 3 and /FTId=VSP_000988.
Natural variance 509 1 Missing (in isoform 4). /FTId=VSP_000990.
Natural variance 207 1 R -> Q (in a patient with isolated /FTId=VAR_043819.
Natural variance 207 1 R -> W (in EBN1; phenotype manifestations /FTId=VAR_026987.
Natural variance 208 1 M -> V (in EBN1; minor effect on maximal /FTId=VAR_026988.
Natural variance 214 1 R -> W (in EBN1; dbSNP:rs28939684). /FTId=VAR_010929.
Natural variance 228 1 H -> Q (in EBN1). /FTId=VAR_026989.
Natural variance 243 1 L -> F (in EBN1). /FTId=VAR_026990.
Natural variance 247 1 S -> W (in EIEE7; reduces channel /FTId=VAR_026991.
Natural variance 284 1 Y -> C (in EBN1; 30%-60% reduction of wt /FTId=VAR_010930.
Natural variance 306 1 A -> T (in EBN1; 20%-40% reduction of wt /FTId=VAR_010931.
Natural variance 333 1 R -> Q (in EBN1; moderate effect; less /FTId=VAR_026992.
Natural variance 554 1 K -> N (in EBN1 and EIEE7; decreases the /FTId=VAR_026993.
Natural variance 780 1 N -> T (in dbSNP:rs1801475). /FTId=VAR_010932.
Mutagenesis 52 1 S->E: 40% increase in potassium current
Mutagenesis 52 1 S->Q: Decrease of PKA stimulation. Ratio
Mutagenesis 279 1 G->S: More than 50% reduction of wt
Different sources report differing sequences 699 1 K -> E (in Ref. 4; AAD16988).
Different sources report differing sequences 854 1 R -> C (in Ref. 4; AAD16988).
Protein-protein
Interaction
Databases
DIP
IntAct

O43526
MINT
STRING

O43526
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome

REACT_18266, Axon guidance.
Phylogenomic Database
HOVERGEN

HBG059014
InParanoid
OMA
OrthoDB
Proteomics
Database (PRIDE)

O43526
Comparative
Toxicogenomics
Database (CTD)

3785
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