KCNH1
entrez
3756
canonical
uniprot
O95259
canonical
ensembl
ENSG00000143473
resolver
ensp
ENSP00000271751
resolver
ensp
ENSP00000355974
resolver
ensp
ENSP00000492697
resolver
genesymbol
KCNH1
resolver
genesymbol_syn
EAG
resolver
genesymbol_syn
EAG1
resolver
hgnc
HGNC:6250
resolver
uniprot
B1AQ26
resolver
uniprot
O76035
resolver
uniprot
Q14CL3
resolver
uniprot_entry
KCNH1_HUMAN
resolver
uniprot_sec
B1AQ26
resolver
uniprot_sec
O76035
resolver
uniprot_sec
Q14CL3
resolver
activity_regulation
ACTIVITY REGULATION: Channel activity is inhibited by interaction with Ca(2+)-bound calmodulin (PubMed:10880439, PubMed:27005320, PubMed:27325704, PubMed:27618660). Interaction of a single pore-forming alpha subunit with a calmodulin chain is sufficient to promote channel closure (PubMed:10880439). Channel activity is not regulated by cyclic nucleotides (By similarity). Channel activity is inhibited by binding intracellular phosphatidylinositol-3,5-bisphosphate and phosphatidylinositol-4,5-bisphosphate (PIP2), but is not inhibited by phosphatidylinositol 4-phosphate (PubMed:27005320). Inhibited by the spider kappa-theraphotoxin-Aa1a and mu/kappa-theraphotoxin-Ap1a (PubMed:30149017). {ECO:0000250|UniProtKB:Q60603, ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660}.
uniprot
proteins
amino_acid_sequence
MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS
uniprot
proteins
disease_involvement
DISEASE: Temple-Baraitser syndrome (TMBTS) [MIM:611816]: A developmental disorder characterized by intellectual disability, epilepsy, hypoplasia or aplasia of the thumb and great toe nails, and broadening and/or elongation of the thumbs and halluces, which have a tubular aspect. Some patients show facial dysmorphism. {ECO:0000269|PubMed:25420144}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Zimmermann-Laband syndrome 1 (ZLS1) [MIM:135500]: A form of Zimmermann-Laband syndrome, a rare developmental disorder characterized by facial dysmorphism with bulbous nose and thick floppy ears, gingival enlargement, hypoplasia or aplasia of terminal phalanges and nails, hypertrichosis, joint hyperextensibility, and hepatosplenomegaly. Some patients manifest intellectual disability with or without epilepsy. ZLS1 inheritance is autosomal dominant. {ECO:0000269|PubMed:25915598}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel that mediates outward-rectifying potassium currents which, on depolarization, reaches a steady-state level and do not inactivate (PubMed:10880439, PubMed:11943152, PubMed:22732247, PubMed:25420144, PubMed:25556795, PubMed:25915598, PubMed:27005320, PubMed:27325704, PubMed:27618660, PubMed:30149017, PubMed:9738473). The activation kinetics depend on the prepulse potential and external divalent cation concentration (PubMed:11943152). With negative prepulses, the current activation is delayed and slowed down several fold, whereas more positive prepulses speed up activation (PubMed:11943152). The time course of activation is biphasic with a fast and a slowly activating current component (PubMed:11943152). Activates at more positive membrane potentials and exhibit a steeper activation curve (PubMed:11943152). Channel properties are modulated by subunit assembly (PubMed:11943152). Mediates IK(NI) current in myoblasts (PubMed:9738473). Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (PubMed:23881642). {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23881642, ECO:0000269|PubMed:25420144, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:25915598, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:30149017, ECO:0000269|PubMed:9738473}.
uniprot
proteins
mass_dalton
111423
uniprot
proteins
mutagenesis
MUTAGEN 699..701; /note="YNL->ANA: Shifts the voltage-dependence of channel gating and decreases the rate of channel opening."; /evidence="ECO:0000269|PubMed:22732247"; MUTAGEN 737; /note="V->S: Abolishes inhibition of channel activity by elevated cytoplasmic Ca(2+)."; /evidence="ECO:0000269|PubMed:27618660"; MUTAGEN 740; /note="L->S: Abolishes inhibition of channel activity by elevated cytoplasmic Ca(2+)."; /evidence="ECO:0000269|PubMed:27618660
uniprot
proteins
post_translational_modification
PTM: Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6 (PubMed:24587194). {ECO:0000269|PubMed:24587194}.
uniprot
proteins
protein_family
H (Eag) (TC 1.A.1.20) subfamily
uniprot
proteins
protein_family
Kv10.1/KCNH1 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
10523298
uniprot
proteins
pubmed
10880439
uniprot
proteins
pubmed
11943152
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
21559285
uniprot
proteins
pubmed
22732247
uniprot
proteins
pubmed
22841712
uniprot
proteins
pubmed
23144454
uniprot
proteins
pubmed
23881642
uniprot
proteins
pubmed
24587194
uniprot
proteins
pubmed
25420144
uniprot
proteins
pubmed
25556795
uniprot
proteins
pubmed
25915598
uniprot
proteins
pubmed
27005320
uniprot
proteins
pubmed
27325704
uniprot
proteins
pubmed
27487920
uniprot
proteins
pubmed
27618660
uniprot
proteins
pubmed
30149017
uniprot
proteins
pubmed
9738473
uniprot
proteins
sequence_length
989
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:21559285, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Nucleus inner membrane {ECO:0000269|PubMed:21559285}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q63472}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000269|PubMed:22841712}. Note=Perinuclear KCNH1 is located to NPC-free islands.
uniprot
proteins
transmembrane_region
TRANSMEM 221..241; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:Q63472"; TRANSMEM 249..269; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:Q63472"; TRANSMEM 291..309; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:Q63472"; TRANSMEM 346..368; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:Q63472"; TRANSMEM 378..399; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:Q63472"; TRANSMEM 478..498; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:Q63472
uniprot
proteins