KCNK12
entrez
56660
canonical
uniprot
Q9HB15
canonical
ensembl
ENSG00000184261
resolver
ensp
ENSP00000327611
resolver
enst
ENST00000327876
resolver
genesymbol
KCNK12
resolver
hgnc
HGNC:6274
resolver
uniprot_entry
KCNKC_HUMAN
resolver
amino_acid_sequence
MSSRSPRPPPRRSRRRLPRPSCCCCCCRRSHLNEDTGRFVLLAALIGLYLVAGATVFSALESPGEAEARARWGATLRNFSAAHGVAEPELRAFLRHYEAALAAGVRADALRPRWDFPGAFYFVGTVVSTIGFGMTTPATVGGKAFLIAYGLFGCAGTILFFNLFLERIISLLAFIMRACRERQLRRSGLLPATFRRGSALSEADSLAGWKPSVYHVLLILGLFAVLLSCCASAMYTSVEGWDYVDSLYFCFVTFSTIGFGDLVSSQHAAYRNQGLYRLGNFLFILLGVCCIYSLFNVISILIKQVLNWMLRKLSCRCCARCCPAPGAPLARRNAITPGSRLRRRLAALGADPAARDSDAEGRRLSGELISMRDLTASNKVSLALLQKQLSETANGYPRSVCVNTRQNGFSGGVGALGIMNNRLAETSASR
uniprot
proteins
function
FUNCTION: K(+) channel subunit that may homo- and heterodimerize to form functional channels with distinct regulatory and gating properties. Can heterodimerize with KCNK13 subunit to conduct K(+) outward rectifying currents at the plasma membrane. The homodimers are mainly retained in the endoplasmic reticulum compartment and may be targeted to the cell surface upon phosphorylation or other activation signals yet to be elucidated. {ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687}.
uniprot
proteins
mass_dalton
46889
uniprot
proteins
mutagenesis
MUTAGEN 11; /note="R->A: Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-12; A-14; A-15 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-12; A-14; A-15 and A-16."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 12; /note="R->A: Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-14; A-15 and A-16. Results in 174 -fold increase in current amplitude; when associated with P-155; D-158; A-11; A-14; A-15 and A-16."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 13; /note="S->A: Mimics the dephosphorylated state which decreases trafficking from the ER to the plasma membrane."; /evidence="ECO:0000269|PubMed:24163367"; MUTAGEN 13; /note="S->D: Mimics the phosphorylated state which increases trafficking from the ER to the plasma membrane and leads to increased K(+) currents."; /evidence="ECO:0000269|PubMed:24163367"; MUTAGEN 14; /note="R->A: Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-15 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-15 and A-16."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 15; /note="R->A: Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-14 and A-16. Results in 174-fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-14 and A-16."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 16; /note="R->A: Disrupts ER retention/retrieval signal resulting in localization at the plasma membrane and K(+) channel conductance; when associated with A-11; A-12; A-14 and A-15. Results in 174 -fold increase in current amplitude; when associated with P-155; D-158; A-11; A-12; A-14 and A-15."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 131; /note="G->E: Acts as a dominant negative when it assembles with wild-type subunit, abolishing K(+) flux."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 155; /note="A->P: Increases channel basal activity. Results in 7-fold increase in current amplitude. Displays additive gating effects and results in a 19-fold increase in current amplitude; when associated with D-158. Results in 174-fold increase in current amplitude; when associated with D-158; A-11; A-12; A-14; A-15 and A-16. Does not affect channel ion selectivity, pH sensitivity nor inhibition by halothane."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 158; /note="I->D: Increases channel basal activity. Results in 6-fold increase in current amplitude. Confers nonlinear I-V relationship, with currents that saturate upon strong membrane depolarization around 0 mV. Displays additive gating effects and results in a 19-fold increase in current amplitude; when associated with P-155. Results in 174-fold increase in current amplitude; when associated with P-155; A-11; A-12; A-14; A-15 and A-16."; /evidence="ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687"; MUTAGEN 158; /note="I->G: Does not affect channel basal activity."; /evidence="ECO:0000269|PubMed:24163367"; MUTAGEN 163; /note="L->G: Does not affect channel basal activity."; /evidence="ECO:0000269|PubMed:24163367"; MUTAGEN 165; /note="L->G: Does not affect channel basal activity."; /evidence="ECO:0000269|PubMed:24163367
uniprot
proteins
protein_family
Two pore domain potassium channel (TC 1.A.1.8) family
uniprot
proteins
pubmed
11060316
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
24163367
uniprot
proteins
pubmed
25148687
uniprot
proteins
sequence_length
430
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25148687}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24163367, ECO:0000269|PubMed:25148687}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 39..59; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 145..165; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 213..233; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 282..302; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins