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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:22732247). Channel properties may be modulated by subunit assembly, but not by cyclic nucleotides (By similarity). 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).By similarity3 Publications

GO - Molecular functioni

GO - Biological processi

  • myoblast fusion Source: ProtInc
  • potassium ion transmembrane transport Source: UniProtKB
  • potassium ion transport Source: ProtInc
  • regulation of cell proliferation Source: UniProtKB
  • regulation of membrane potential Source: GO_Central
  • synaptic transmission Source: Reactome
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, Potassium

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily H member 1
Alternative name(s):
Ether-a-go-go potassium channel 1
Short name:
EAG channel 1
Short name:
h-eag
Short name:
hEAG1
Voltage-gated potassium channel subunit Kv10.1
Gene namesi
Name:KCNH1
Synonyms:EAG, EAG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6250. KCNH1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 220220CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei221 – 24121Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Topological domaini242 – 2487ExtracellularSequence Analysis
Transmembranei249 – 26921Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Topological domaini270 – 29425CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei295 – 31521Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Topological domaini316 – 34934ExtracellularSequence AnalysisAdd
BLAST
Transmembranei350 – 37021Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Topological domaini371 – 3766CytoplasmicSequence Analysis
Transmembranei377 – 39721Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Topological domaini398 – 45053ExtracellularSequence AnalysisAdd
BLAST
Intramembranei451 – 47121Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Topological domaini472 – 4776ExtracellularSequence Analysis
Transmembranei478 – 49821Helical; Name=Segment S6Sequence AnalysisAdd
BLAST
Topological domaini499 – 989491CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: HPA
  • early endosome membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • plasma membrane Source: HPA
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171K → N in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072612
Natural varianti489 – 4891L → F in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072613
Natural varianti494 – 4941I → V in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072614
Natural varianti503 – 5031Q → R in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072615

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi699 – 7013YNL → ANA: Shifts the voltage-dependence of channel gating and decreases the rate of channel opening. 1 Publication

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

MIMi611816. phenotype.
PharmGKBiPA30037.

Polymorphism and mutation databases

BioMutaiKCNH1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 989989Potassium voltage-gated channel subfamily H member 1PRO_0000053994Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis

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

PaxDbiO95259.
PRIDEiO95259.

PTM databases

PhosphoSiteiO95259.

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

BgeeiO95259.
CleanExiHS_KCNH1.
GenevisibleiO95259. HS.

Organism-specific databases

HPAiHPA019445.

Interactioni

Subunit structurei

The potassium channel is probably 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).By similarity2 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 interactions.
IntActiO95259. 10 interactions.
MINTiMINT-138319.
STRINGi9606.ENSP00000271751.

Structurei

3D structure databases

ProteinModelPortaliO95259.
SMRiO95259. Positions 28-137, 509-720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 9481PASPROSITE-ProRule annotationAdd
BLAST
Domaini93 – 14553PACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni673 – 77098Calmodulin-binding1 PublicationAdd
BLAST
Regioni699 – 7013Interaction with cyclic nucleotide-binding pocketBy similarity
Regioni924 – 96441CAD (involved in subunit assembly)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi463 – 4686Selectivity filterBy similarity

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
The C-terminal region interacts with the cyclic nucleotide-binding domain and contributes to regulate channel gating.By similarity
The PAS domain interacts with the cyclic nucleotide-binding domain and contributes to regulate channel gating.By similarity
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

eggNOGiCOG2202.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000230794.
HOVERGENiHBG101348.
InParanoidiO95259.
KOiK04904.
OMAiHAKLHAP.
OrthoDBiEOG7QG43V.
PhylomeDBiO95259.
TreeFamiTF313130.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR030170. EAG1.
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]
PANTHERiPTHR10217:SF377. PTHR10217:SF377. 1 hit.
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.
SM00091. PAS. 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171K → N in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072612
Natural varianti489 – 4891L → F in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072613
Natural varianti494 – 4941I → V in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072614
Natural varianti503 – 5031Q → R in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type. 1 Publication
VAR_072615

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei318 – 34427Missing in isoform 1. 2 PublicationsVSP_000964Add
BLAST

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.2. human. [O95259-1]
uc001hic.2. human. [O95259-2]

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

ProteinModelPortaliO95259.
SMRiO95259. Positions 28-137, 509-720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2362996.
GuidetoPHARMACOLOGYi570.

PTM databases

PhosphoSiteiO95259.

Polymorphism and mutation databases

BioMutaiKCNH1.

Proteomic databases

PaxDbiO95259.
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.2. human. [O95259-1]
uc001hic.2. human. [O95259-2]

Organism-specific databases

CTDi3756.
GeneCardsiGC01M210851.
HGNCiHGNC:6250. KCNH1.
HPAiHPA019445.
MIMi603305. gene.
611816. phenotype.
neXtProtiNX_O95259.
PharmGKBiPA30037.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2202.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000230794.
HOVERGENiHBG101348.
InParanoidiO95259.
KOiK04904.
OMAiHAKLHAP.
OrthoDBiEOG7QG43V.
PhylomeDBiO95259.
TreeFamiTF313130.

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

GeneWikiiKCNH1.
GenomeRNAii3756.
NextBioi14711.
PROiO95259.
SOURCEiSearch...

Gene expression databases

BgeeiO95259.
CleanExiHS_KCNH1.
GenevisibleiO95259. HS.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR030170. EAG1.
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]
PANTHERiPTHR10217:SF377. PTHR10217:SF377. 1 hit.
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.
SM00091. PAS. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a human ether-a-go-go potassium channel expressed in myoblasts at the onset of fusion."
    Occhiodoro T., Bernheim L., Liu J.-H., Bijlenga P., Sinnreich M., Bader C.R., Fischer-Lougheed J.
    FEBS Lett. 434:177-182(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
    Tissue: Myoblast.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "Inhibition of human ether a go-go potassium channels by Ca(2+)/calmodulin."
    Schoenherr R., Lober K., Heinemann S.H.
    EMBO J. 19:3263-3271(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALMODULIN-BINDING DOMAIN.
  7. "Functional distinction of human EAG1 and EAG2 potassium channels."
    Schoenherr R., Gessner G., Loeber K., Heinemann S.H.
    FEBS Lett. 514:204-208(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNH5.
  8. "Functional K(v)10.1 channels localize to the inner nuclear membrane."
    Chen Y., Sanchez A., Rubio M.E., Kohl T., Pardo L.A., Stuhmer W.
    PLoS ONE 6:E19257-E19257(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking."
    Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.
    FEBS Lett. 586:3077-3084(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Cortactin controls surface expression of the voltage-gated potassium channel K(V)10.1."
    Herrmann S., Ninkovic M., Kohl T., Lorinczi E., Pardo L.A.
    J. Biol. Chem. 287:44151-44163(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTTN.
  11. "Structural, biochemical, and functional characterization of the cyclic nucleotide binding homology domain from the mouse EAG1 potassium channel."
    Marques-Carvalho M.J., Sahoo N., Muskett F.W., Vieira-Pires R.S., Gabant G., Cadene M., Schonherr R., Morais-Cabral J.H.
    J. Mol. Biol. 423:34-46(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 699-TYR--LEU-701.
  12. "BKCa and hEag1 channels regulate cell proliferation and differentiation in human bone marrow-derived mesenchymal stem cells."
    Zhang Y.Y., Yue J., Che H., Sun H.Y., Tse H.F., Li G.R.
    J. Cell. Physiol. 229:202-212(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Regulation of hERG and hEAG channels by Src and by SHP-1 tyrosine phosphatase via an ITIM region in the cyclic nucleotide binding domain."
    Schlichter L.C., Jiang J., Wang J., Newell E.W., Tsui F.W., Lam D.
    PLoS ONE 9:E90024-E90024(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  14. Cited for: INVOLVEMENT IN TMBTS, VARIANTS TMBTS ASN-217; PHE-489; VAL-494 AND ARG-503, CHARACTERIZATION OF VARIANTS TMBTS ASN-217; PHE-489; VAL-494 AND ARG-503.

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: June 24, 2015
This is version 149 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.