KCNT2
entrez
343450
canonical
uniprot
Q6UVM3
canonical
ensembl
ENSG00000162687
resolver
ensembl
ENSG00000291999
resolver
ensp
ENSP00000294725
resolver
ensp
ENSP00000356403
resolver
ensp
ENSP00000476657
resolver
ensp
ENSP00000496885
resolver
ensp
ENSP00000517745
resolver
ensp
ENSP00000552085
resolver
enst
ENST00000647658
resolver
enst
ENST00000709530
resolver
genesymbol
KCNT2
resolver
genesymbol_syn
SLICK
resolver
genesymbol_syn
Slo2.1
resolver
hgnc
HGNC:18866
resolver
uniprot
A0A3B3IRL4
resolver
uniprot
A9LNM6
resolver
uniprot
Q3SY59
resolver
uniprot
Q5VTN1
resolver
uniprot
Q6ZMT3
resolver
uniprot_entry
A0A3B3IRL4_HUMAN
resolver
uniprot_entry
A9LNM6_HUMAN
resolver
uniprot_entry
KCNT2_HUMAN
resolver
uniprot_sec
Q3SY59
resolver
uniprot_sec
Q5VTN1
resolver
uniprot_sec
Q6ZMT3
resolver
activity_regulation
ACTIVITY REGULATION: Are normally in a closed state unless activated by an increase in intracellular Na(+) and Cl(-) (PubMed:14684870, PubMed:16687497, PubMed:29069600). Inhibited upon stimulation of G protein-coupled receptors, such as CHRM1 and GRM1 (PubMed:16687497). There is conflicting data about the effect of ATP on KNCT2 channels activity. Intracellular ATP was initially report to inhibit the channel activity (PubMed:14684870). However, others studies conclude that KNCT2 channels are not inhibited by intracellular ATP (PubMed:25214519). {ECO:0000269|PubMed:14684870, ECO:0000269|PubMed:16687497, ECO:0000269|PubMed:25214519, ECO:0000269|PubMed:29069600}.
uniprot
proteins
amino_acid_sequence
MVDLESEVPPLPPRYRFRDLLLGDQGWQNDDRVQVEFYMNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLSCLLYIIRVLLENPSQGNEWSHIFWVNRSLPLWGLQVSVALISLFETILLGYLSYKGNIWEQILRIPFILEIINAVPFIISIFWPSLRNLFVPVFLNCWLAKHALENMINDLHRAIQRTQSAMFNQVLILISTLLCLIFTCICGIQHLERIGKKLNLFDSLYFCIVTFSTVGFGDVTPETWSSKLFVVAMICVALVVLPIQFEQLAYLWMERQKSGGNYSRHRAQTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPTEMDVQVRRVLQIPMWSQRVIYLQGSALKDQDLLRAKMDDAEACFILSSRCEVDRTSSDHQTILRAWAVKDFAPNCPLYVQILKPENKFHIKFADHVVCEEEFKYAMLALNCICPATSTLITLLVHTSRGQEGQQSPEQWQKMYGRCSGNEVYHIVLEESTFFAEYEGKSFTYASFHAHKKFGVCLIGVRREDNKNILLNPGPRYIMNSTDICFYINITKEENSAFKNQDQQRKSNVSRSFYHGPSRLPVHSIIASMGTVAIDLQDTSCRSASGPTLSLPTEGSKEIRRPSIAPVLEVADTSSIQTCDLLSDQSEDETTPDEEMSSNLEYAKGYPPYSPYIGSSPTFCHLLHEKVPFCCLRLDKSCQHNYYEDAKAYGFKNKLIIVAAETAGNGLYNFIVPLRAYYRPKKELNPIVLLLDNPPDMHFLDAICWFPMVYYMVGSIDNLDDLLRCGVTFAANMVVVDKESTMSAEEDYMADAKTIVNVQTLFRLFSSLSIITELTHPANMRFMQFRAKDCYSLALSKLEKKERERGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMISITRLLLGLDTTPGSGFLCSMKITADDLWIRTYARLYQKLCSSTGDVPIGIYRTESQKLTTSESQISISVEEWEDTKDSKEQGHHRSNHRNSTSSDQSDHPLLRRKSMQWARRLSRKGPKHSGKTAEKITQQRLNLYRRSERQELAELVKNRMKHLGLSTVGYDEMNDHQSTLSYILINPSPDTRIELNDVVYLIRPDPLAYLPNSEPSRRNSICNVTGQDSREETQL
uniprot
proteins
disease_involvement
DISEASE: Developmental and epileptic encephalopathy 57 (DEE57) [MIM:617771]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE57 is an autosomal dominant condition. {ECO:0000269|PubMed:29069600, ECO:0000269|PubMed:29740868}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Sodium-activated and chloride-activated potassium channel (PubMed:14684870, PubMed:16687497, PubMed:25214519, PubMed:27682982, PubMed:29069600, PubMed:29740868). Produces rapidly activating outward rectifier K(+) currents (PubMed:14684870). Contributes to regulate neuronal excitability (PubMed:29069600). {ECO:0000269|PubMed:14684870, ECO:0000269|PubMed:16687497, ECO:0000269|PubMed:25214519, ECO:0000269|PubMed:27682982, ECO:0000269|PubMed:29069600, ECO:0000269|PubMed:29740868}.
uniprot
proteins
mass_dalton
130501
uniprot
proteins
mutagenesis
MUTAGEN 267; /note="L->H,N,T,E,Q,S: Constitutively open channel."; /evidence="ECO:0000269|PubMed:27682982"; MUTAGEN 267; /note="L->N: Constitutively open channel; when associated with N-270."; /evidence="ECO:0000269|PubMed:27682982"; MUTAGEN 270; /note="L->N: Does not affect channel activity. Constitutively open channel; when associated with N-267."; /evidence="ECO:0000269|PubMed:27682982"; MUTAGEN 270; /note="L->W,H,Q: Constitutively open channel."; /evidence="ECO:0000269|PubMed:27682982"; MUTAGEN 282; /note="M->A: Does not induce constitutive opening."; /evidence="ECO:0000269|PubMed:27682982"; MUTAGEN 1031; /note="K->A: Does not affect KCNT2 channel activity."; /evidence="ECO:0000269|PubMed:25214519
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by protein kinase C. Phosphorylation of the C-terminal domain inhibits channel activity. {ECO:0000269|PubMed:16687497}.
uniprot
proteins
protein_family
Calcium-activated (TC 1.A.1.3) subfamily
uniprot
proteins
protein_family
KCa4.2/KCNT2 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
14684870
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16687497
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
25214519
uniprot
proteins
pubmed
27682982
uniprot
proteins
pubmed
29069600
uniprot
proteins
pubmed
29740868
uniprot
proteins
sequence_length
1135
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29069600}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 64..84; /note="Helical; Name=Segment S1"; /evidence="ECO:0000255"; TRANSMEM 102..122; /note="Helical; Name=Segment S2"; /evidence="ECO:0000255"; TRANSMEM 138..158; /note="Helical; Name=Segment S3"; /evidence="ECO:0000255"; TRANSMEM 165..185; /note="Helical; Name=Segment S4"; /evidence="ECO:0000255"; TRANSMEM 199..219; /note="Helical; Name=Segment S5"; /evidence="ECO:0000255"; TRANSMEM 257..277; /note="Helical; Name=Segment S6"; /evidence="ECO:0000255
uniprot
proteins