Kcnq2
entrez
16536
canonical
uniprot
Q9Z351
canonical
ensembl
ENSMUSG00000016346
resolver
ensp
ENSMUSP00000016491
resolver
ensp
ENSMUSP00000052453
resolver
ensp
ENSMUSP00000080243
resolver
ensp
ENSMUSP00000099336
resolver
ensp
ENSMUSP00000099337
resolver
ensp
ENSMUSP00000099338
resolver
ensp
ENSMUSP00000099339
resolver
ensp
ENSMUSP00000099340
resolver
ensp
ENSMUSP00000122915
resolver
ensp
ENSMUSP00000123488
resolver
ensp
ENSMUSP00000143263
resolver
ensp
ENSMUSP00000184672
resolver
ensp
ENSMUSP00000343024
resolver
enst
ENSMUST00000016491
resolver
enst
ENSMUST00000049792
resolver
enst
ENSMUST00000081528
resolver
enst
ENSMUST00000103047
resolver
enst
ENSMUST00000103048
resolver
enst
ENSMUST00000103050
resolver
enst
ENSMUST00000103051
resolver
enst
ENSMUST00000149964
resolver
enst
ENSMUST00000197015
resolver
genesymbol
Kcnq2
resolver
genesymbol_syn
Kqt2
resolver
uniprot
A0A0G2JFQ2
resolver
uniprot
B7ZBV4
resolver
uniprot
B7ZBV5
resolver
uniprot
B7ZBV6
resolver
uniprot
B7ZBV7
resolver
uniprot
B7ZBV8
resolver
uniprot
B7ZBV9
resolver
uniprot
B7ZBW1
resolver
uniprot
B7ZBW2
resolver
uniprot
B7ZNV7
resolver
uniprot
Q3UTI0
resolver
uniprot
Q3UY10
resolver
uniprot
Q8R498
resolver
uniprot
Q9QWN9
resolver
uniprot
Q9Z342
resolver
uniprot
Q9Z343
resolver
uniprot
Q9Z344
resolver
uniprot
Q9Z345
resolver
uniprot
Q9Z346
resolver
uniprot
Q9Z347
resolver
uniprot
Q9Z348
resolver
uniprot
Q9Z349
resolver
uniprot
Q9Z350
resolver
uniprot_entry
A0A0G2JFQ2_MOUSE
resolver
uniprot_entry
B7ZBV4_MOUSE
resolver
uniprot_entry
B7ZBV5_MOUSE
resolver
uniprot_entry
B7ZBV6_MOUSE
resolver
uniprot_entry
B7ZBV7_MOUSE
resolver
uniprot_entry
B7ZBV8_MOUSE
resolver
uniprot_entry
B7ZBV9_MOUSE
resolver
uniprot_entry
B7ZBW1_MOUSE
resolver
uniprot_entry
B7ZBW2_MOUSE
resolver
uniprot_entry
B7ZNV7_MOUSE
resolver
uniprot_entry
KCNQ2_MOUSE
resolver
uniprot_entry
Q3UY10_MOUSE
resolver
uniprot_sec
Q3UTI0
resolver
uniprot_sec
Q8R498
resolver
uniprot_sec
Q9QWN9
resolver
uniprot_sec
Q9Z342
resolver
uniprot_sec
Q9Z343
resolver
uniprot_sec
Q9Z344
resolver
uniprot_sec
Q9Z345
resolver
uniprot_sec
Q9Z346
resolver
uniprot_sec
Q9Z347
resolver
uniprot_sec
Q9Z348
resolver
uniprot_sec
Q9Z349
resolver
uniprot_sec
Q9Z350
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatidylinositol-4,5-bisphosphate (PIP2) potentiates the activation of KCNQ channels by enhancing the electro-mechanical coupling of the voltage-sensing domain (VSD) and the pore-forming domain (PD). In the closed state of the channel, PIP2 is anchored at the S2-S3 loop; upon channel activation, PIP2 interacts with the S4-S5 linker and is involved in channel gating. Calcium suppresses KCNQ2 and KCNQ2-KCNQ3 channel currents, with calcium-bound calmodulin inducing a change in channel configuration which leads to the reduction of channel affinity for PIP2 and subsequent current suppression. {ECO:0000250|UniProtKB:O43526}.
uniprot
proteins
amino_acid_sequence
MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRPKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMYRLIPPLNQLELLRNLKSKSGLTFRKEPQPEPSPSQKVSLKDRVFSSPRGMAAKGKGSPQAQTVRRSPSADQSLDDSPSKVPKSWSFGDRSRTRQAFRIKGAASRQNSEEASLPGEDIVEDNKSCNCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRIDMIVGPPPPSTPRDKKYPTKGPTAPSRESPQYSPRVDHIVGRGPTITDKDRTKGPAETELPEDPSMMGRLGKVEKQVLSMEKKLDFLVSIYTQRMGIPPAETEAYFGAKEPEPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRNYAAPPAIPPAQCPPSTSWQQSHQRHGTSPVGDHGSLVLRLERSAGMMSCH
uniprot
proteins
function
FUNCTION: Pore-forming subunit of the voltage-gated potassium (Kv) M-channel which is responsible for the M-current, a key controller of neuronal excitability (PubMed:12223552). M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers. The native M-current has 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 (PubMed:12223552). M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+). Suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (By similarity). {ECO:0000250|UniProtKB:O43526, ECO:0000269|PubMed:12223552}.
uniprot
proteins
mass_dalton
84450
uniprot
proteins
mutagenesis
MUTAGEN 345; /note="R->E: Loss of interaction with calmodulin."; /evidence="ECO:0000269|PubMed:12223552"; MUTAGEN 525; /note="K->E: Loss of interaction with calmodulin; when associated with E-526."; /evidence="ECO:0000269|PubMed:12223552"; MUTAGEN 526; /note="R->E: Loss of interaction with calmodulin; when associated with E-525."; /evidence="ECO:0000269|PubMed:12223552
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:O43526}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43526}.
uniprot
proteins
protein_family
KQT (TC 1.A.1.15) subfamily
uniprot
proteins
protein_family
Kv7.2/KCNQ2 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
10854243
uniprot
proteins
pubmed
12223552
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27979964
uniprot
proteins
pubmed
38440182
uniprot
proteins
pubmed
9666519
uniprot
proteins
sequence_length
759
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12223552}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 91..113; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 124..145; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 164..183; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 197..215; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 228..253; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 288..314; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:O43526
uniprot
proteins