ID  O95259;
PN  Potassium voltage-gated channel subfamily H member 1;
GN  KCNH1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: 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.
DR  UNIPROT: O95259;
DR  UNIPROT: B1AQ26;
DR  UNIPROT: O76035;
DR  UNIPROT: Q14CL3;
DR  PDB: 5J7E;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  Pfam: PF13426;
DR  PROSITE: PS50042;
DR  PROSITE: PS50113;
DR  PROSITE: PS50112;
DR  OMIM: 135500;
DR  OMIM: 603305;
DR  OMIM: 611816;
DR  DisGeNET: 3756;
DE  Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:9738473, PubMed:11943152, PubMed:10880439, PubMed:22732247, PubMed:25556795, PubMed:27325704, PubMed:27005320, PubMed:27618660). 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:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}.
DE  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. 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.
DE  Reference Proteome: Yes;
DE  Interaction: P02638; IntAct: EBI-8161978; Score: 0.54
DE  Interaction: P62158; IntAct: EBI-8162095; Score: 0.72
DE  Interaction: O35550; IntAct: EBI-7991537; Score: 0.37
DE  Interaction: Q63472; IntAct: EBI-7991588; Score: 0.37
DE  Interaction: Q15276; IntAct: EBI-7991852; Score: 0.27
DE  Interaction: P18067; IntAct: EBI-7991934; Score: 0.27
DE  Interaction: P62490; IntAct: EBI-7991888; Score: 0.27
DE  Interaction: O00560; IntAct: EBI-10179865; Score: 0.56
DE  Interaction: Q7L8L6; IntAct: EBI-10256563; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-10287297; Score: 0.56
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
GO  GO:0070161;
GO  GO:0030673;
GO  GO:0009986;
GO  GO:0030425;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0099056;
GO  GO:0043231;
GO  GO:0005637;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0008076;
GO  GO:0071889;
GO  GO:0005516;
GO  GO:0005251;
GO  GO:0042802;
GO  GO:1902936;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0071277;
GO  GO:0007520;
GO  GO:0048015;
GO  GO:0071805;
GO  GO:0006813;
GO  GO:0042127;
GO  GO:0034765;
GO  GO:0042391;
GO  GO:0001964;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q63472};
SQ  MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTI
SQ  EKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTS
SQ  SRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVS
SQ  FKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA
SQ  FMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSI
SQ  GDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFA
SQ  VAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICP
SQ  KDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGK
SQ  GDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEER
SQ  MKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSF
SQ  QAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSC
SQ  DSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTS
SQ  RRSSQSPQELFEISRPQSPESERDIFGAS
//