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O43526

- KCNQ2_HUMAN

UniProt

O43526 - KCNQ2_HUMAN

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Protein

Potassium voltage-gated channel subfamily KQT member 2

Gene

KCNQ2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (6)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

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.

GO - Molecular functioni

  1. ankyrin binding Source: BHF-UCL
  2. delayed rectifier potassium channel activity Source: RefGenome
  3. potassium channel activity Source: ProtInc
  4. voltage-gated potassium channel activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. nervous system development Source: ProtInc
  3. potassium ion transport Source: ProtInc
  4. synaptic transmission Source: Reactome
  5. transmission of nerve impulse Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_22266. Interaction between L1 and Ankyrins.
REACT_75770. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.A.1.15.2. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
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
Gene namesi
Name:KCNQ2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:6296. KCNQ2.

Subcellular locationi

Membrane; Multi-pass membrane protein

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei92 – 11221Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Topological domaini113 – 12210ExtracellularSequence Analysis
Transmembranei123 – 14321Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Topological domaini144 – 16623CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei167 – 18721Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Topological domaini188 – 1958ExtracellularSequence Analysis
Transmembranei196 – 21823Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Topological domaini219 – 23113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei232 – 25221Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Topological domaini253 – 26412ExtracellularSequence AnalysisAdd
BLAST
Intramembranei265 – 28521Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Topological domaini286 – 2916ExtracellularSequence Analysis
Transmembranei292 – 31221Helical; Name=Segment S6Sequence AnalysisAdd
BLAST
Topological domaini313 – 872560CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon initial segment Source: BHF-UCL
  2. node of Ranvier Source: BHF-UCL
  3. plasma membrane Source: BHF-UCL
  4. voltage-gated potassium channel complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071R → 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. 1 Publication
VAR_026987
Natural varianti208 – 2081M → V in BFNS1; minor effect on maximal current but clearly exhibits a faster rate of deactivation. 1 Publication
VAR_026988
Natural varianti214 – 2141R → W in BFNS1. 1 Publication
Corresponds to variant rs28939684 [ dbSNP | Ensembl ].		VAR_010929
Natural varianti228 – 2281H → Q in BFNS1. 1 Publication
VAR_026989
Natural varianti243 – 2431L → F in BFNS1. 1 Publication
VAR_026990
Natural varianti284 – 2841Y → C in BFNS1; 30%-60% reduction of wt heteromeric current. Ratio 1:1 or 20%-30%; ratio of 1:1:2. 2 Publications
Corresponds to variant rs28939683 [ dbSNP | Ensembl ].		VAR_010930
Natural varianti306 – 3061A → T in BFNS1; 20%-40% reduction of wt heteromeric current. Ratio of 1:1:2. 2 Publications
VAR_010931
Natural varianti333 – 3331R → Q in BFNS1; moderate effect; less than 50% reduction in current compared with wt heteromeric channels. 1 Publication
VAR_026992
Natural varianti554 – 5541K → N in BFNS1 and EIEE7; decreases the voltage-dependence of the channel. 1 Publication
VAR_026993
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471S → W in EIEE7; reduces channel currents by more than 50% in homomeric channels. 1 Publication
VAR_026991
Natural varianti554 – 5541K → N in BFNS1 and EIEE7; decreases the voltage-dependence of the channel. 1 Publication
VAR_026993

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521S → E: 40% increase in potassium current amplitude. Ratio of 1:1. 1 Publication
Mutagenesisi52 – 521S → Q: Decrease of PKA stimulation. Ratio of 1:1. 1 Publication
Mutagenesisi217 – 2171T → A: No effect on current or expression. 1 Publication
Mutagenesisi217 – 2171T → D: Abolishes currents without reducing channel protein expression. 1 Publication
Mutagenesisi279 – 2791G → S: More than 50% reduction of wt heteromeric current. Ratio of 1:1 and 1:1:2. 1 Publication

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

MIMi121200. phenotype.
613720. phenotype.
Orphaneti306. Benign familial infantile epilepsy.
1949. Benign familial neonatal seizures.
140927. Benign familial neonatal-infantile seizures.
1934. Early infantile epileptic encephalopathy.
PharmGKBiPA30074.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 872872Potassium voltage-gated channel subfamily KQT member 2PRO_0000054030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine; by PKA1 Publication
Modified residuei217 – 2171Phosphothreonine1 Publication

Post-translational modificationi

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-terminal region.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO43526.
PRIDEiO43526.

PTM databases

PhosphoSiteiO43526.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO43526.
CleanExiHS_KCNQ2.
ExpressionAtlasiO43526. baseline and differential.
GenevestigatoriO43526.

Organism-specific databases

HPAiHPA016642.

Interactioni

Subunit structurei

Heteromultimer with KCNQ3. May associate with KCNE2.

Protein-protein interaction databases

BioGridi109986. 6 interactions.
IntActiO43526. 1 interaction.
MINTiMINT-8402812.
STRINGi9606.ENSP00000352035.

Structurei

3D structure databases

ProteinModelPortaliO43526.
SMRiO43526. Positions 65-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi277 – 2826Selectivity 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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00550000074513.
HOVERGENiHBG059014.
InParanoidiO43526.
KOiK04927.
OrthoDBiEOG73804Z.
PhylomeDBiO43526.
TreeFamiTF315186.

Family and domain databases

InterProiIPR020969. 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]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
PF11956. KCNQC3-Ank-G_bd. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01461. KCNQ2CHANNEL.
PR01459. KCNQCHANNEL.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O43526-1) [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
MVQKSRNGGV YPGPSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR 
        60         70         80         90        100
GSILSKPRAG GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF 
       110        120        130        140        150
LLVFSCLVLS VFSTIKEYEK SSEGALYILE IVTIVVFGVE YFVRIWAAGC 
       160        170        180        190        200
CCRYRGWRGR LKFARKPFCV IDIMVLIASI AVLAAGSQGN VFATSALRSL 
       210        220        230        240        250
RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF LCLILASFLV 
       260        270        280        290        300
YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI 
       310        320        330        340        350
GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QSAWRFYATN 
       360        370        380        390        400
LSRTDLHSTW QYYERTVTVP MYSSQTQTYG ASRLIPPLNQ LELLRNLKSK 
       410        420        430        440        450
SGLAFRKDPP PEPSPSKGSP CRGPLCGCCP GRSSQKVSLK DRVFSSPRGV 
       460        470        480        490        500
AAKGKGSPQA QTVRRSPSAD QSLEDSPSKV PKSWSFGDRS RARQAFRIKG 
       510        520        530        540        550
AASRQNSEEA SLPGEDIVDD KSCPCEFVTE DLTPGLKVSI RAVCVMRFLV 
       560        570        580        590        600
SKRKFKESLR PYDVMDVIEQ YSAGHLDMLS RIKSLQSRVD QIVGRGPAIT 
       610        620        630        640        650
DKDRTKGPAE AELPEDPSMM GRLGKVEKQV LSMEKKLDFL VNIYMQRMGI 
       660        670        680        690        700
PPTETEAYFG AKEPEPAPPY HSPEDSREHV DRHGCIVKIV RSSSSTGQKN 
       710        720        730        740        750
FSAPPAAPPV QCPPSTSWQP QSHPRQGHGT SPVGDHGSLV RIPPPPAHER 
       760        770        780        790        800
SLSAYGGGNR ASMEFLRQED TPGCRPPEGN LRDSDTSISI PSVDHEELER 
       810        820        830        840        850
SFSGFSISQS KENLDALNSC YAAVAPCAKV RPYIAEGESD TDSDLCTPCG 
       860        870 
PPPRSATGEG PFGDVGWAGP RK
Length:872
Mass (Da):95,848
Last modified:June 1, 2001 - v2
Checksum:i22E8A0880A27B58C
GO
Isoform 2 (identifier: O43526-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-434: Missing.

Show »
Length:854
Mass (Da):94,100
Checksum:iCF3F5EC2E23E21FC
GO
Isoform 3 (identifier: O43526-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:844
Mass (Da):93,089
Checksum:i5228E1B8C3D8C17F
GO
Isoform 4 (identifier: O43526-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-446: Missing.
     509-509: Missing.

Show »
Length:841
Mass (Da):92,596
Checksum:i065E37AF63726B10
GO
Isoform 5 (identifier: O43526-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     310-320: Missing.
     417-434: Missing.

Show »
Length:843
Mass (Da):93,057
Checksum:iAF6F5146789F4167
GO
Isoform 6 (identifier: O43526-6) [UniParc]FASTAAdd to Basket

Also known as: HNSPC

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

Show »
Length:393
Mass (Da):44,261
Checksum:i9415BC4FC2F84675
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti699 – 6991K → E in AAD16988. (PubMed:9836639)Curated
Sequence conflicti854 – 8541R → C in AAD16988. (PubMed:9836639)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071R → Q in a patient with isolated myokymia and no history of neonatal seizures; leads to a shift of voltage-dependent activation. 1 Publication
VAR_043819
Natural varianti207 – 2071R → 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. 1 Publication
VAR_026987
Natural varianti208 – 2081M → V in BFNS1; minor effect on maximal current but clearly exhibits a faster rate of deactivation. 1 Publication
VAR_026988
Natural varianti214 – 2141R → W in BFNS1. 1 Publication
Corresponds to variant rs28939684 [ dbSNP | Ensembl ].		VAR_010929
Natural varianti228 – 2281H → Q in BFNS1. 1 Publication
VAR_026989
Natural varianti243 – 2431L → F in BFNS1. 1 Publication
VAR_026990
Natural varianti247 – 2471S → W in EIEE7; reduces channel currents by more than 50% in homomeric channels. 1 Publication
VAR_026991
Natural varianti284 – 2841Y → C in BFNS1; 30%-60% reduction of wt heteromeric current. Ratio 1:1 or 20%-30%; ratio of 1:1:2. 2 Publications
Corresponds to variant rs28939683 [ dbSNP | Ensembl ].		VAR_010930
Natural varianti306 – 3061A → T in BFNS1; 20%-40% reduction of wt heteromeric current. Ratio of 1:1:2. 2 Publications
VAR_010931
Natural varianti333 – 3331R → Q in BFNS1; moderate effect; less than 50% reduction in current compared with wt heteromeric channels. 1 Publication
VAR_026992
Natural varianti554 – 5541K → N in BFNS1 and EIEE7; decreases the voltage-dependence of the channel. 1 Publication
VAR_026993
Natural varianti780 – 7801N → T.1 Publication
Corresponds to variant rs1801475 [ dbSNP | Ensembl ].		VAR_010932

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei310 – 32011Missing in isoform 5. 1 PublicationVSP_000984Add
BLAST
Alternative sequencei373 – 39321SSQTQ…NQLEL → RYRRRAPATKQLFHFLFSIC S in isoform 6. 2 PublicationsVSP_000986Add
BLAST
Alternative sequencei373 – 38210Missing in isoform 3. 1 PublicationVSP_000985
Alternative sequencei394 – 872479Missing in isoform 6. 2 PublicationsVSP_000987Add
BLAST
Alternative sequencei417 – 44630Missing in isoform 4. 1 PublicationVSP_000989Add
BLAST
Alternative sequencei417 – 43418Missing in isoform 2, isoform 3 and isoform 5. 3 PublicationsVSP_000988Add
BLAST
Alternative sequencei509 – 5091Missing in isoform 4. 1 PublicationVSP_000990

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13518.1. [O43526-3]
CCDS13519.1. [O43526-2]
CCDS13520.1. [O43526-1]
CCDS13521.1. [O43526-6]
CCDS46629.1. [O43526-4]
PIRiJC5275.
RefSeqiNP_004509.2. NM_004518.4. [O43526-3]
NP_742104.1. NM_172106.1. [O43526-2]
NP_742105.1. NM_172107.2. [O43526-1]
NP_742106.1. NM_172108.3. [O43526-4]
NP_742107.1. NM_172109.1. [O43526-6]
UniGeneiHs.161851.
Hs.652468.

Genome annotation databases

EnsembliENST00000344425; ENSP00000345523; ENSG00000075043. [O43526-6]
ENST00000344462; ENSP00000339611; ENSG00000075043. [O43526-4]
ENST00000357249; ENSP00000349789; ENSG00000075043. [O43526-2]
ENST00000359125; ENSP00000352035; ENSG00000075043. [O43526-1]
ENST00000360480; ENSP00000353668; ENSG00000075043. [O43526-3]
GeneIDi3785.
KEGGihsa:3785.
UCSCiuc002yey.1. human. [O43526-1]
uc002yez.1. human. [O43526-4]
uc002yfa.1. human. [O43526-2]
uc002yfb.1. human. [O43526-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 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 .
CCDSi CCDS13518.1. [O43526-3 ]
CCDS13519.1. [O43526-2 ]
CCDS13520.1. [O43526-1 ]
CCDS13521.1. [O43526-6 ]
CCDS46629.1. [O43526-4 ]
PIRi JC5275.
RefSeqi NP_004509.2. NM_004518.4. [O43526-3 ]
NP_742104.1. NM_172106.1. [O43526-2 ]
NP_742105.1. NM_172107.2. [O43526-1 ]
NP_742106.1. NM_172108.3. [O43526-4 ]
NP_742107.1. NM_172109.1. [O43526-6 ]
UniGenei Hs.161851.
Hs.652468.

3D structure databases

ProteinModelPortali O43526.
SMRi O43526. Positions 65-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109986. 6 interactions.
IntActi O43526. 1 interaction.
MINTi MINT-8402812.
STRINGi 9606.ENSP00000352035.

Chemistry

BindingDBi O43526.
ChEMBLi CHEMBL2476.
DrugBanki DB00321. Amitriptyline.
DB00586. Diclofenac.
DB04953. Ezogabine.
DB00939. Meclofenamic acid.
GuidetoPHARMACOLOGYi 561.

Protein family/group databases

TCDBi 1.A.1.15.2. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei O43526.

Proteomic databases

PaxDbi O43526.
PRIDEi O43526.

Protocols and materials databases

DNASUi 3785.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344425 ; ENSP00000345523 ; ENSG00000075043 . [O43526-6 ]
ENST00000344462 ; ENSP00000339611 ; ENSG00000075043 . [O43526-4 ]
ENST00000357249 ; ENSP00000349789 ; ENSG00000075043 . [O43526-2 ]
ENST00000359125 ; ENSP00000352035 ; ENSG00000075043 . [O43526-1 ]
ENST00000360480 ; ENSP00000353668 ; ENSG00000075043 . [O43526-3 ]
GeneIDi 3785.
KEGGi hsa:3785.
UCSCi uc002yey.1. human. [O43526-1 ]
uc002yez.1. human. [O43526-4 ]
uc002yfa.1. human. [O43526-2 ]
uc002yfb.1. human. [O43526-3 ]

Organism-specific databases

CTDi 3785.
GeneCardsi GC20M062038.
GeneReviewsi KCNQ2.
HGNCi HGNC:6296. KCNQ2.
HPAi HPA016642.
MIMi 121200. phenotype.
602235. gene.
613720. phenotype.
neXtProti NX_O43526.
Orphaneti 306. Benign familial infantile epilepsy.
1949. Benign familial neonatal seizures.
140927. Benign familial neonatal-infantile seizures.
1934. Early infantile epileptic encephalopathy.
PharmGKBi PA30074.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00550000074513.
HOVERGENi HBG059014.
InParanoidi O43526.
KOi K04927.
OrthoDBi EOG73804Z.
PhylomeDBi O43526.
TreeFami TF315186.

Enzyme and pathway databases

Reactomei REACT_22266. Interaction between L1 and Ankyrins.
REACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSi KCNQ2. human.
GeneWikii KvLQT2.
GenomeRNAii 3785.
NextBioi 14859.
PROi O43526.
SOURCEi Search...

Gene expression databases

Bgeei O43526.
CleanExi HS_KCNQ2.
ExpressionAtlasi O43526. baseline and differential.
Genevestigatori O43526.

Family and domain databases

InterProi IPR020969. 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 ]
PANTHERi PTHR11537. PTHR11537. 1 hit.
Pfami PF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
PF11956. KCNQC3-Ank-G_bd. 1 hit.
[Graphical view ]
PRINTSi PR00169. KCHANNEL.
PR01461. KCNQ2CHANNEL.
PR01459. KCNQCHANNEL.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS BFNS1 CYS-284 AND THR-306.
    Tissue: Brain, Fetal brain and Temporal cortex.
  3. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiKCNQ2_HUMAN
AccessioniPrimary (citable) accession number: O43526
Secondary accession number(s): O43796
, O75580, O95845, Q4VXP4, Q4VXR6, Q5VYT8, Q96J59, Q99454
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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