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Protein

Potassium voltage-gated channel subfamily H member 1

Gene

KCNH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).9 Publications

Enzyme regulationi

Channel activity is inhibited by interaction with Ca2+-bound calmodulin (PubMed:10880439, PubMed:27325704, PubMed:27005320, 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).By similarity4 Publications

GO - Molecular functioni

  • delayed rectifier potassium channel activity Source: UniProtKB
  • phosphatidylinositol bisphosphate binding Source: UniProtKB
  • phosphorelay sensor kinase activity Source: InterPro

GO - Biological processi

  • cellular response to calcium ion Source: UniProtKB
  • myoblast fusion Source: ProtInc
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • potassium ion transmembrane transport Source: UniProtKB
  • potassium ion transport Source: ProtInc
  • regulation of cell proliferation Source: UniProtKB
  • regulation of membrane potential Source: GO_Central
  • startle response Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calmodulin-binding, Lipid-binding, Potassium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143473-MONOMER.
ReactomeiR-HSA-1296072. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily H member 1
Alternative name(s):
Ether-a-go-go potassium channel 11 Publication
Short name:
EAG channel 12 Publications
Short name:
h-eag
Short name:
hEAG12 Publications
Voltage-gated potassium channel subunit Kv10.1
Gene namesi
Name:KCNH1
Synonyms:EAG1 Publication, EAG12 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6250. KCNH1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 220CytoplasmicBy similarityAdd BLAST220
Transmembranei221 – 241Helical; Name=Segment S1By similarityAdd BLAST21
Topological domaini242 – 248ExtracellularBy similarity7
Transmembranei249 – 269Helical; Name=Segment S2By similarityAdd BLAST21
Topological domaini270 – 290CytoplasmicBy similarityAdd BLAST21
Transmembranei291 – 309Helical; Name=Segment S3By similarityAdd BLAST19
Topological domaini310 – 345ExtracellularBy similarityAdd BLAST36
Transmembranei346 – 368Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST23
Topological domaini369 – 377CytoplasmicBy similarity9
Transmembranei378 – 399Helical; Name=Segment S5By similarityAdd BLAST22
Topological domaini400 – 448ExtracellularBy similarityAdd BLAST49
Intramembranei449 – 470Pore-forming; Name=Segment H5By similarityAdd BLAST22
Topological domaini471 – 477ExtracellularBy similarity7
Transmembranei478 – 498Helical; Name=Segment S6By similarityAdd BLAST21
Topological domaini499 – 989CytoplasmicBy similarityAdd BLAST491

GO - Cellular componenti

  • axolemma Source: Ensembl
  • cell surface Source: Ensembl
  • dendrite Source: Ensembl
  • early endosome membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nuclear inner membrane Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: Reactome
  • presynaptic membrane Source: Ensembl
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endosome, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

Temple-Baraitser syndrome (TMBTS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:611816
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072612217K → N in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 PublicationCorresponds to variant rs727502822dbSNPEnsembl.1
Natural variantiVAR_072613489L → F in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication1
Natural variantiVAR_072614494I → V in TMBTS and ZLS1; gain-of-function effect; resulting in a decreased threshold of channel activation and slower deactivation. 2 PublicationsCorresponds to variant rs727502819dbSNPEnsembl.1
Natural variantiVAR_072615503Q → R in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 PublicationCorresponds to variant rs727502821dbSNPEnsembl.1
Zimmermann-Laband syndrome 1 (ZLS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by gingival fibromatosis, dysplastic or absent nails, finger abnormalities, hepatosplenomegaly, and abnormalities of the cartilage of the nose and/or ears.
See also OMIM:135500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073957352S → Y in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with L-383. 1 PublicationCorresponds to variant rs730882172dbSNPEnsembl.1
Natural variantiVAR_073958375G → R in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation. 1 PublicationCorresponds to variant rs730882174dbSNPEnsembl.1
Natural variantiVAR_073959379L → V in ZLS1. 1 PublicationCorresponds to variant rs730882176dbSNPEnsembl.1
Natural variantiVAR_073960383V → L in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with Y-352. 1 PublicationCorresponds to variant rs730882173dbSNPEnsembl.1
Natural variantiVAR_072614494I → V in TMBTS and ZLS1; gain-of-function effect; resulting in a decreased threshold of channel activation and slower deactivation. 2 PublicationsCorresponds to variant rs727502819dbSNPEnsembl.1
Natural variantiVAR_073961496G → R in ZLS1; gain-of-function effect; increased conductance at negative potentials. 1 PublicationCorresponds to variant rs730882175dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi699 – 701YNL → ANA: Shifts the voltage-dependence of channel gating and decreases the rate of channel opening. 1 Publication3
Mutagenesisi737V → S: Abolishes inhibition of channel activity by elevated cytoplasmic Ca(2+). 1 Publication1
Mutagenesisi740L → S: Abolishes inhibition of channel activity by elevated cytoplasmic Ca(2+). 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNETi3756.
MalaCardsiKCNH1.
MIMi135500. phenotype.
611816. phenotype.
OpenTargetsiENSG00000143473.
PharmGKBiPA30037.

Chemistry databases

ChEMBLiCHEMBL2362996.
GuidetoPHARMACOLOGYi570.

Polymorphism and mutation databases

BioMutaiKCNH1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539941 – 989Potassium voltage-gated channel subfamily H member 1Add BLAST989

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi415N-linked (GlcNAc...)Sequence analysis1
Glycosylationi433N-linked (GlcNAc...)Sequence analysis1
Modified residuei974PhosphoserineBy similarity1
Modified residuei978PhosphoserineBy similarity1
Modified residuei981PhosphoserineBy similarity1

Post-translational modificationi

Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6 (PubMed:24587194).1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO95259.
PaxDbiO95259.
PeptideAtlasiO95259.
PRIDEiO95259.

PTM databases

iPTMnetiO95259.
PhosphoSitePlusiO95259.

Expressioni

Tissue specificityi

Highly expressed in brain and in myoblasts at the onset of fusion, but not in other tissues. Detected in HeLa (cervical carcinoma), SH-SY5Y (neuroblastoma) and MCF-7 (epithelial tumor) cells, but not in normal epithelial cells.

Gene expression databases

BgeeiENSG00000143473.
CleanExiHS_KCNH1.
GenevisibleiO95259. HS.

Organism-specific databases

HPAiHPA019445.

Interactioni

Subunit structurei

The potassium channel is composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Heteromultimer with KCNH5/EAG2 (PubMed:11943152). Interacts with ALG10B (By similarity). Interacts with RABEP1 (By similarity). Interacts (via C-terminus) with CTTN (PubMed:23144454). Interacts (via C-terminal cytoplasmic region) with Ca2+-bound calmodulin (PubMed:10880439, PubMed:27325704, PubMed:27618660).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CALM3P621588EBI-9836801,EBI-397435
FASTKD5Q7L8L63EBI-2909270,EBI-747570
S100BP026383EBI-2909270,EBI-458452From a different organism.
SDCBPO005603EBI-2909270,EBI-727004
WDYHV1Q96HA83EBI-2909270,EBI-741158

Protein-protein interaction databases

BioGridi109958. 7 interactors.
IntActiO95259. 10 interactors.
MINTiMINT-138319.
STRINGi9606.ENSP00000271751.

Structurei

Secondary structure

1989
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 34Combined sources6
Beta strandi41 – 45Combined sources5
Helixi47 – 53Combined sources7
Helixi57 – 59Combined sources3
Turni60 – 62Combined sources3
Helixi68 – 70Combined sources3
Helixi77 – 88Combined sources12
Beta strandi93 – 100Combined sources8
Beta strandi106 – 117Combined sources12
Beta strandi123 – 132Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5J7EX-ray1.90A/B/C/D/E/F1-146[»]
ProteinModelPortaliO95259.
SMRiO95259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 94PASPROSITE-ProRule annotationAdd BLAST81
Domaini93 – 145PACPROSITE-ProRule annotationAdd BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni151 – 162Required for phosphatidylinositol bisphosphate binding1 PublicationAdd BLAST12
Regioni673 – 770Calmodulin-binding1 PublicationAdd BLAST98
Regioni699 – 701Interaction with cyclic nucleotide-binding pocketBy similarity3
Regioni924 – 964CAD (involved in subunit assembly)By similarityAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi463 – 468Selectivity filterBy similarity6

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.By similarity
The C-terminal region interacts with the cyclic nucleotide-binding domain and contributes to regulate channel gating.By similarity
The PAS and PAC domain interact with the cyclic nucleotide-binding domain and contribute to the regulation of channel gating (PubMed:27325704). Calmodulin binding clamps together the PAS and PAC domain with the cyclic nucleotide-binding domain from a neighboring subunit and causes a conformation change that leads to channel closure.By similarity1 Publication
The cyclic nucleotide-binding domain lacks residues that are essential for nucleotide-binding and cannot bind cyclic nucleotides. Instead, residues from the C-terminal domain (the so-called intrinsic ligand) bind in the cavity that would be expected to bind cyclic nucleotides. Interaction with the C-terminal region hinders interaction with CALM and reduces the affinity for CALM.By similarity

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000230794.
HOVERGENiHBG101348.
InParanoidiO95259.
KOiK04904.
OMAiIRTESWL.
OrthoDBiEOG091G0OXR.
PhylomeDBiO95259.
TreeFamiTF313130.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR003949. K_chnl_volt-dep_EAG.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF13426. PAS_9. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
PR01464. EAGCHANNEL.
SMARTiSM00100. cNMP. 1 hit.
SM00086. PAC. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
SSF55785. SSF55785. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: O95259-1) [UniParc]FASTAAdd to basket
Also known as: hEAGB

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTMAGGRRGL VAPQNTFLEN IVRRSNDTNF VLGNAQIVDW PIVYSNDGFC
60 70 80 90 100
KLSGYHRAEV MQKSSTCSFM YGELTDKDTI EKVRQTFENY EMNSFEILMY
110 120 130 140 150
KKNRTPVWFF VKIAPIRNEQ DKVVLFLCTF SDITAFKQPI EDDSCKGWGK
160 170 180 190 200
FARLTRALTS SRGVLQQLAP SVQKGENVHK HSRLAEVLQL GSDILPQYKQ
210 220 230 240 250
EAPKTPPHII LHYCVFKTTW DWIILILTFY TAILVPYNVS FKTRQNNVAW
260 270 280 290 300
LVVDSIVDVI FLVDIVLNFH TTFVGPAGEV ISDPKLIRMN YLKTWFVIDL
310 320 330 340 350
LSCLPYDVIN AFENVDEVSA FMGDPGKIGF ADQIPPPLEG RESQGISSLF
360 370 380 390 400
SSLKVVRLLR LGRVARKLDH YIEYGAAVLV LLVCVFGLAA HWMACIWYSI
410 420 430 440 450
GDYEIFDEDT KTIRNNSWLY QLAMDIGTPY QFNGSGSGKW EGGPSKNSVY
460 470 480 490 500
ISSLYFTMTS LTSVGFGNIA PSTDIEKIFA VAIMMIGSLL YATIFGNVTT
510 520 530 540 550
IFQQMYANTN RYHEMLNSVR DFLKLYQVPK GLSERVMDYI VSTWSMSRGI
560 570 580 590 600
DTEKVLQICP KDMRADICVH LNRKVFKEHP AFRLASDGCL RALAMEFQTV
610 620 630 640 650
HCAPGDLIYH AGESVDSLCF VVSGSLEVIQ DDEVVAILGK GDVFGDVFWK
660 670 680 690 700
EATLAQSCAN VRALTYCDLH VIKRDALQKV LEFYTAFSHS FSRNLILTYN
710 720 730 740 750
LRKRIVFRKI SDVKREEEER MKRKNEAPLI LPPDHPVRRL FQRFRQQKEA
760 770 780 790 800
RLAAERGGRD LDDLDVEKGN VLTEHASANH SLVKASVVTV RESPATPVSF
810 820 830 840 850
QAASTSGVPD HAKLQAPGSE CLGPKGGGGD CAKRKSWARF KDACGKSEDW
860 870 880 890 900
NKVSKAESME TLPERTKASG EATLKKTDSC DSGITKSDLR LDNVGEARSP
910 920 930 940 950
QDRSPILAEV KHSFYPIPEQ TLQATVLEVR HELKEDIKAL NAKMTNIEKQ
960 970 980
LSEILRILTS RRSSQSPQEL FEISRPQSPE SERDIFGAS
Length:989
Mass (Da):111,423
Last modified:May 1, 1999 - v1
Checksum:iCAA8CB251300C7E5
GO
Isoform 1 (identifier: O95259-2) [UniParc]FASTAAdd to basket
Also known as: hEAG

The sequence of this isoform differs from the canonical sequence as follows:
     318-344: Missing.

Show »
Length:962
Mass (Da):108,597
Checksum:i9CC995AFF156582D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072612217K → N in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 PublicationCorresponds to variant rs727502822dbSNPEnsembl.1
Natural variantiVAR_073957352S → Y in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with L-383. 1 PublicationCorresponds to variant rs730882172dbSNPEnsembl.1
Natural variantiVAR_073958375G → R in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation. 1 PublicationCorresponds to variant rs730882174dbSNPEnsembl.1
Natural variantiVAR_073959379L → V in ZLS1. 1 PublicationCorresponds to variant rs730882176dbSNPEnsembl.1
Natural variantiVAR_073960383V → L in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with Y-352. 1 PublicationCorresponds to variant rs730882173dbSNPEnsembl.1
Natural variantiVAR_072613489L → F in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication1
Natural variantiVAR_072614494I → V in TMBTS and ZLS1; gain-of-function effect; resulting in a decreased threshold of channel activation and slower deactivation. 2 PublicationsCorresponds to variant rs727502819dbSNPEnsembl.1
Natural variantiVAR_073961496G → R in ZLS1; gain-of-function effect; increased conductance at negative potentials. 1 PublicationCorresponds to variant rs730882175dbSNPEnsembl.1
Natural variantiVAR_072615503Q → R in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 PublicationCorresponds to variant rs727502821dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000964318 – 344Missing in isoform 1. 2 PublicationsAdd BLAST27

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001366 mRNA. Translation: CAA04700.1.
AF078741 mRNA. Translation: AAC68668.1.
AF078742 mRNA. Translation: AAC68669.1.
AL590132
, AC092017, AC096636, AC099755 Genomic DNA. Translation: CAH71752.1.
AL590132
, AC092017, AC096636, AC099755 Genomic DNA. Translation: CAH71753.1.
CH471100 Genomic DNA. Translation: EAW93424.1.
CH471100 Genomic DNA. Translation: EAW93425.1.
BC113709 mRNA. Translation: AAI13710.1.
BC143599 mRNA. Translation: AAI43600.1.
CCDSiCCDS1496.1. [O95259-1]
CCDS31015.1. [O95259-2]
RefSeqiNP_002229.1. NM_002238.3. [O95259-2]
NP_758872.1. NM_172362.2. [O95259-1]
UniGeneiHs.553187.

Genome annotation databases

EnsembliENST00000271751; ENSP00000271751; ENSG00000143473. [O95259-1]
ENST00000367007; ENSP00000355974; ENSG00000143473. [O95259-2]
GeneIDi3756.
KEGGihsa:3756.
UCSCiuc001hib.3. human. [O95259-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001366 mRNA. Translation: CAA04700.1.
AF078741 mRNA. Translation: AAC68668.1.
AF078742 mRNA. Translation: AAC68669.1.
AL590132
, AC092017, AC096636, AC099755 Genomic DNA. Translation: CAH71752.1.
AL590132
, AC092017, AC096636, AC099755 Genomic DNA. Translation: CAH71753.1.
CH471100 Genomic DNA. Translation: EAW93424.1.
CH471100 Genomic DNA. Translation: EAW93425.1.
BC113709 mRNA. Translation: AAI13710.1.
BC143599 mRNA. Translation: AAI43600.1.
CCDSiCCDS1496.1. [O95259-1]
CCDS31015.1. [O95259-2]
RefSeqiNP_002229.1. NM_002238.3. [O95259-2]
NP_758872.1. NM_172362.2. [O95259-1]
UniGeneiHs.553187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5J7EX-ray1.90A/B/C/D/E/F1-146[»]
ProteinModelPortaliO95259.
SMRiO95259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109958. 7 interactors.
IntActiO95259. 10 interactors.
MINTiMINT-138319.
STRINGi9606.ENSP00000271751.

Chemistry databases

ChEMBLiCHEMBL2362996.
GuidetoPHARMACOLOGYi570.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiO95259.
PhosphoSitePlusiO95259.

Polymorphism and mutation databases

BioMutaiKCNH1.

Proteomic databases

MaxQBiO95259.
PaxDbiO95259.
PeptideAtlasiO95259.
PRIDEiO95259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271751; ENSP00000271751; ENSG00000143473. [O95259-1]
ENST00000367007; ENSP00000355974; ENSG00000143473. [O95259-2]
GeneIDi3756.
KEGGihsa:3756.
UCSCiuc001hib.3. human. [O95259-1]

Organism-specific databases

CTDi3756.
DisGeNETi3756.
GeneCardsiKCNH1.
HGNCiHGNC:6250. KCNH1.
HPAiHPA019445.
MalaCardsiKCNH1.
MIMi135500. phenotype.
603305. gene.
611816. phenotype.
neXtProtiNX_O95259.
OpenTargetsiENSG00000143473.
PharmGKBiPA30037.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000230794.
HOVERGENiHBG101348.
InParanoidiO95259.
KOiK04904.
OMAiIRTESWL.
OrthoDBiEOG091G0OXR.
PhylomeDBiO95259.
TreeFamiTF313130.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143473-MONOMER.
ReactomeiR-HSA-1296072. Voltage gated Potassium channels.

Miscellaneous databases

GeneWikiiKCNH1.
GenomeRNAii3756.
PROiO95259.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143473.
CleanExiHS_KCNH1.
GenevisibleiO95259. HS.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR003949. K_chnl_volt-dep_EAG.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF13426. PAS_9. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
PR01464. EAGCHANNEL.
SMARTiSM00100. cNMP. 1 hit.
SM00086. PAC. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
SSF55785. SSF55785. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
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Entry informationi

Entry nameiKCNH1_HUMAN
AccessioniPrimary (citable) accession number: O95259
Secondary accession number(s): B1AQ26, O76035, Q14CL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.