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Q12809 (KCNH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily H member 2
Alternative name(s):
Eag homolog
Ether-a-go-go-related gene potassium channel 1
Short name=ERG-1
Short name=Eag-related protein 1
Short name=Ether-a-go-go-related protein 1
Short name=H-ERG
Short name=hERG-1
Short name=hERG1
Voltage-gated potassium channel subunit Kv11.1
Gene names
Name:KCNH2
Synonyms:ERG, ERG1, HERG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1159 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoforms USO have no channel activity by themself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation. Ref.6

Subunit structure

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 KCNH6/ERG2 and KCNH7/ERG3. Interacts with ALG10B By similarity. Heteromultimer with KCNE1 and KCNE2. Interacts with CANX. Ref.18 Ref.19 Ref.20

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.6 Ref.7.

Tissue specificity

Highly expressed in heart and brain. Isoforms USO are frequently overexpressed in cancer cells. Ref.6

Domain

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.

Post-translational modification

Phosphorylated on serine and threonine residues. Phosphorylation by PKA inhibits ion conduction. Ref.17

Involvement in disease

Long QT syndrome 2 (LQT2) [MIM:613688]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Deafness is often associated with long QT syndrome type 2.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.40 Ref.42 Ref.43 Ref.45 Ref.46 Ref.49

Short QT syndrome 1 (SQT1) [MIM:609620]: A heart disorder characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. It causes syncope and sudden death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.44 Ref.47

Sequence similarities

Belongs to the potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. [View classification]

Contains 1 cyclic nucleotide-binding domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Sequence caution

The sequence CAA09232.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
Long QT syndrome
Short QT syndrome
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle contraction

Inferred from mutant phenotype PubMed 21536673. Source: BHF-UCL

cellular response to drug

Inferred from direct assay PubMed 7604285. Source: BHF-UCL

membrane depolarization during action potential

Inferred from direct assay PubMed 7604285. Source: BHF-UCL

negative regulation of potassium ion export

Inferred from direct assay PubMed 7604285PubMed 8587608. Source: BHF-UCL

peptidyl-histidine phosphorylation

Inferred from electronic annotation. Source: GOC

positive regulation of potassium ion transmembrane transport

Inferred from direct assay PubMed 7736582. Source: BHF-UCL

potassium ion export

Inferred from direct assay PubMed 7604285. Source: BHF-UCL

potassium ion homeostasis

Inferred from direct assay PubMed 7604285PubMed 8587608. Source: BHF-UCL

regulation of heart rate by cardiac conduction

Inferred from mutant phenotype PubMed 21536673. Source: BHF-UCL

regulation of heart rate by hormone

Traceable author statement PubMed 11953308. Source: BHF-UCL

regulation of ventricular cardiac muscle cell membrane repolarization

Inferred from mutant phenotype PubMed 21536673. Source: BHF-UCL

signal transduction by phosphorylation

Inferred from electronic annotation. Source: GOC

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcell surface

Inferred from direct assay PubMed 21536673. Source: BHF-UCL

cytoplasm

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from electronic annotation. Source: Ensembl

voltage-gated potassium channel complex

Inferred from direct assay PubMed 7604285PubMed 7736582PubMed 8587608. Source: BHF-UCL

   Molecular_functiondelayed rectifier potassium channel activity

Inferred from direct assay PubMed 7736582. Source: BHF-UCL

inward rectifier potassium channel activity

Inferred from direct assay PubMed 7604285PubMed 8587608. Source: BHF-UCL

phosphorelay sensor kinase activity

Inferred from electronic annotation. Source: InterPro

voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization

Inferred from mutant phenotype PubMed 21536673. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-720643,EBI-720643

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform A (identifier: Q12809-1)

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.
Isoform B (identifier: Q12809-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-376: MPVRRGHVAP...THNVTEKVTQ → MAAPAGKASR...VRISSLVAQE
Isoform 4 (identifier: Q12809-4)

The sequence of this isoform differs from the canonical sequence as follows:
     139-195: Missing.
Note: No experimental confirmation available.
Isoform A-USO (identifier: Q12809-5)

The sequence of this isoform differs from the canonical sequence as follows:
     801-888: KNDIFGEPLN...GGFSRQRKRK → MGWGAGTGLE...HKQTLFASLK
     889-1159: Missing.
Note: Twice more abundant than isoform 1 in heart.
Isoform B-USO (identifier: Q12809-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARV → MAAPAGKASRTGALRPRAQKGRVRRAVRISSLVAQE
     37-376: Missing.
     801-888: KNDIFGEPLN...GGFSRQRKRK → MGWGAGTGLE...HKQTLFASLK
     889-1159: Missing.
Isoform 3.1 (identifier: Q12809-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: MPVRRGHVAP...KVEIAFYRKD → MSSHSA
Note: Primate-specific. Lacks a domain that is crucial for slow channel deactivation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11591159Potassium voltage-gated channel subfamily H member 2
PRO_0000053999

Regions

Topological domain1 – 403403Cytoplasmic Potential
Transmembrane404 – 42421Helical; Name=Segment S1; Potential
Topological domain425 – 45026Extracellular Potential
Transmembrane451 – 47121Helical; Name=Segment S2; Potential
Topological domain472 – 49524Cytoplasmic Potential
Transmembrane496 – 51621Helical; Name=Segment S3; Potential
Topological domain517 – 5204Extracellular Potential
Transmembrane521 – 54121Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain542 – 5476Cytoplasmic Potential
Transmembrane548 – 56821Helical; Name=Segment S5; Potential
Topological domain569 – 61143Extracellular Potential
Intramembrane612 – 63221Pore-forming; Name=Segment H5; Potential
Topological domain633 – 6386Extracellular Potential
Transmembrane639 – 65921Helical; Name=Segment S6; Potential
Topological domain660 – 1159500Cytoplasmic Potential
Domain41 – 7030PAS
Domain92 – 14453PAC
Nucleotide binding742 – 842101cNMP
Motif624 – 6296Selectivity filter By similarity
Compositional bias297 – 3004Poly-Pro

Amino acid modifications

Modified residue3201Phosphoserine Ref.21
Glycosylation5981N-linked (GlcNAc...) Ref.16

Natural variations

Alternative sequence1 – 376376MPVRR…EKVTQ → MAAPAGKASRTGALRPRAQK GRVRRAVRISSLVAQE in isoform B.
VSP_000965
Alternative sequence1 – 102102MPVRR…FYRKD → MSSHSA in isoform 3.1.
VSP_047877
Alternative sequence1 – 3636MPVRR…ANARV → MAAPAGKASRTGALRPRAQK GRVRRAVRISSLVAQE in isoform B-USO.
VSP_047878
Alternative sequence37 – 376340Missing in isoform B-USO.
VSP_047879
Alternative sequence139 – 19557Missing in isoform 4.
VSP_000966
Alternative sequence801 – 88888KNDIF…QRKRK → MGWGAGTGLEMPSAASRGAS LLNMQSLGLWTWDCLQGHWA PLIHLNSGPPSGAMERSPTW GEAAELWGSHILLPFRIRHK QTLFASLK in isoform A-USO and isoform B-USO.
VSP_047880
Alternative sequence889 – 1159271Missing in isoform A-USO and isoform B-USO.
VSP_047881
Natural variant261S → I in LQT2. Ref.46
VAR_068249
Natural variant291F → L in LQT2. Ref.33 Ref.46
VAR_008907
Natural variant311I → S in LQT2. Ref.46
VAR_068250
Natural variant331N → T in LQT2. Ref.33
VAR_008908
Natural variant471G → V in LQT2.
VAR_009909
Natural variant531G → R in LQT2. Ref.33 Ref.46
VAR_008909
Natural variant551S → L in LQT2. Ref.46
VAR_068251
Natural variant561R → Q in LQT2. Ref.33
VAR_008910
Natural variant651T → P in LQT2. Ref.42 Ref.46
Corresponds to variant rs28933095 [ dbSNP | Ensembl ].
VAR_014371
Natural variant661C → G in LQT2. Ref.33
VAR_008911
Natural variant701H → R in LQT2. Ref.33 Ref.46
VAR_008912
Natural variant721P → Q in LQT2.
VAR_009910
Natural variant781A → P in LQT2. Ref.33 Ref.46
VAR_008913
Natural variant851A → V in LQT2. Ref.46
VAR_068252
Natural variant861L → R in LQT2. Ref.33
VAR_008914
Natural variant1001R → G in LQT2; digenic; associated with the Asn-1819 mutation on the SCN5A gene. Ref.48
VAR_036669
Natural variant1001R → Q in LQT2. Ref.46
VAR_068253
Natural variant1761R → W in LQT2. Ref.37
Corresponds to variant rs36210422 [ dbSNP | Ensembl ].
VAR_008915
Natural variant1811R → Q.
Corresponds to variant rs41308954 [ dbSNP | Ensembl ].
VAR_036670
Natural variant1891G → GGAG. Ref.13
VAR_014372
Natural variant2381G → S in LQT2. Ref.46
VAR_068254
Natural variant3061G → W in LQT2. Ref.46
VAR_068255
Natural variant3121R → C in LQT2.
VAR_009911
Natural variant3201S → L in LQT2. Ref.46
VAR_068256
Natural variant3281R → C in LQT2. Ref.46
VAR_068257
Natural variant3471P → S in LQT2.
VAR_009912
Natural variant4201Y → C in LQT2. Ref.46
VAR_068258
Natural variant4211T → M in LQT2. Ref.46
VAR_068259
Natural variant4221A → T in LQT2. Ref.46
VAR_068260
Natural variant4271Y → S in LQT2. Ref.46
VAR_068261
Natural variant4361T → M in LQT2.
VAR_008916
Natural variant4511P → L in LQT2. Ref.37
VAR_014373
Natural variant4561D → Y in LQT2. Ref.46
VAR_068262
Natural variant4701N → D in LQT2; aberrant protein folding increases the association of mutant KCNH2 with CANX and results in defective protein trafficking. Ref.20 Ref.23
VAR_008578
Natural variant4741T → I in LQT2. Ref.27
VAR_008917
Natural variant4751Missing in LQT2. Ref.46
VAR_068263
Natural variant4901A → T in long QT syndrome; bradycardia-induced. Ref.39
Corresponds to variant rs28928905 [ dbSNP | Ensembl ].
VAR_036671
Natural variant500 – 5089Missing in LQT2.
VAR_009178
Natural variant5251K → N in long QT syndrome 2/3; located on the same allele as Pro-528. Ref.48
VAR_036672
Natural variant5281R → P in long QT syndrome 2/3; located on the same allele as Asn-525. Ref.48
VAR_036673
Natural variant5311R → Q in LQT2.
VAR_009913
Natural variant5341R → C in LQT2. Ref.2 Ref.46
VAR_008579
Natural variant5521L → S in LQT2. Ref.46
VAR_008918
Natural variant5581A → P in LQT2. Ref.32
VAR_008919
Natural variant5611A → T in LQT2. Ref.26 Ref.46
VAR_014374
Natural variant5611A → V in LQT2; the mutation reduces wild-type channel expression. Ref.23 Ref.38 Ref.46
VAR_008580
Natural variant5621H → P in LQT2. Ref.46
VAR_068264
Natural variant5641L → P in LQT2.
VAR_008920
Natural variant5691Y → H in LQT2. Ref.37
VAR_008921
Natural variant5711I → L in LQT2. Ref.46
VAR_068265
Natural variant5721G → C in LQT2. Ref.28
VAR_008923
Natural variant5721G → R in LQT2; severe form. Ref.35
VAR_008922
Natural variant5721G → S in LQT2. Ref.46
VAR_068266
Natural variant5821R → C in LQT2. Ref.32 Ref.46
VAR_008581
Natural variant5841G → S in LQT2. Ref.37 Ref.46
VAR_008924
Natural variant5851W → C in LQT2.
VAR_009914
Natural variant5881N → D in LQT2. Ref.28 Ref.46
VAR_008925
Natural variant5881N → K in SQT1. Ref.44 Ref.47
VAR_023840
Natural variant5931I → R in LQT2. Ref.25
Corresponds to variant rs28928904 [ dbSNP | Ensembl ].
VAR_008582
Natural variant5931I → T in LQT2.
VAR_009915
Natural variant5961P → R in LQT2. Ref.46
VAR_068267
Natural variant6011G → S in LQT2. Ref.30 Ref.37
VAR_008926
Natural variant6041G → S in LQT2. Ref.32 Ref.46
VAR_008927
Natural variant6091D → N in LQT2.
VAR_009916
Natural variant6111Y → H in LQT2. Ref.27
VAR_008928
Natural variant6121V → L in LQT2. Ref.29
VAR_008929
Natural variant6131T → M in LQT2. Ref.32 Ref.37 Ref.46
VAR_008930
Natural variant6141A → V in LQT2. Ref.27 Ref.28 Ref.29 Ref.46
VAR_008931
Natural variant6151L → V in LQT2.
VAR_014375
Natural variant6221L → F in LQT2. Ref.46
VAR_068268
Natural variant6231T → I in LQT2. Ref.46
VAR_068269
Natural variant6261G → S in LQT2.
VAR_014376
Natural variant6271F → L in LQT2.
VAR_014377
Natural variant6281G → S in LQT2. Ref.23 Ref.46
VAR_008583
Natural variant6281G → V in LQT2. Ref.46
VAR_068270
Natural variant6291N → D in LQT2. Ref.29
VAR_008932
Natural variant6291N → K in LQT2. Ref.34
VAR_008933
Natural variant6291N → S in LQT2. Ref.29
VAR_009179
Natural variant6301V → A in LQT2. Ref.28 Ref.46
VAR_008935
Natural variant6301V → L in LQT2. Ref.27
VAR_008934
Natural variant6321P → S in LQT2.
VAR_014378
Natural variant6331N → S in LQT2. Ref.29 Ref.46
VAR_008936
Natural variant6351N → I in LQT2. Ref.46
VAR_068271
Natural variant6371E → K in LQT2. Ref.40
VAR_014379
Natural variant6381K → E in LQT2.
VAR_014380
Natural variant6381Missing in LQT2.
VAR_014381
Natural variant6401F → L in LQT2. Ref.32
VAR_008937
Natural variant6401F → V in LQT2. Ref.46
VAR_068272
Natural variant6411S → F in LQT2. Ref.46
VAR_068273
Natural variant6451M → L in LQT2.
VAR_014382
Natural variant671 – 6755Missing in LQT2.
VAR_068274
Natural variant6961R → C in long QT syndrome 2/3. Ref.48
VAR_036674
Natural variant7211P → L in LQT2. Ref.46
VAR_068275
Natural variant7441R → P in LQT2; impairs channel function; exhibits reduced activating currents compared to wild-type; cell surface trafficking is not impaired; does not exert dominant-negative effects on wild-type channel; the half-maximal activation voltage is not significantly affected by the mutation. Ref.49
VAR_068276
Natural variant7521R → Q in LQT2. Ref.43
VAR_036675
Natural variant7521R → W in LQT2.
VAR_014383
Natural variant7741D → Y in LQT2. Ref.46
VAR_068277
Natural variant7841R → W Predisposes to LQT2 and torsades de pointes while taking the drug amiodarone; in vitro studies confirmed a significant reduction in potassium currents; the ECG abnormalities reversed on drug withdrawal. Ref.41 Ref.46
VAR_036676
Natural variant7881E → D in LQT2. Ref.46
VAR_068278
Natural variant8051F → C in LQT2. Ref.46
VAR_014384
Natural variant8051F → S in LQT2.
VAR_014385
Natural variant8181S → L in LQT2. Ref.31
VAR_008938
Natural variant8201G → R in LQT2. Ref.46
VAR_068279
Natural variant8221V → M in LQT2. Ref.24 Ref.46
VAR_008584
Natural variant8231R → W in LQT2.
VAR_014386
Natural variant8371D → G in LQT2. Ref.46
VAR_068280
Natural variant8611N → I in LQT2. Ref.45
VAR_014387
Natural variant8871R → H in LQT2. Ref.46
VAR_068281
Natural variant8971K → T. Ref.37 Ref.41
Corresponds to variant rs1805123 [ dbSNP | Ensembl ].
VAR_014388
Natural variant9131A → V in LQT2. Ref.46
VAR_068282
Natural variant9171P → L in LQT2.
VAR_014389
Natural variant9221R → W in LQT2.
VAR_014390
Natural variant9251G → R in LQT2. Ref.46
VAR_068283
Natural variant9481R → C in long QT syndrome 2/3. Ref.48
VAR_036677
Natural variant9831T → I in LQT2. Ref.46
VAR_068284
Natural variant9961N → I in LQT2. Ref.46
VAR_068285
Natural variant10161P → L.
Corresponds to variant rs41313074 [ dbSNP | Ensembl ].
VAR_036679
Natural variant10161P → S.
Corresponds to variant rs41307280 [ dbSNP | Ensembl ].
VAR_036678
Natural variant10201P → S.
Corresponds to variant rs41307274 [ dbSNP | Ensembl ].
VAR_036680
Natural variant10261P → L.
Corresponds to variant rs41307271 [ dbSNP | Ensembl ].
VAR_036681
Natural variant10361G → D in LQT2. Ref.46
VAR_068286
Natural variant10551R → Q.
Corresponds to variant rs41307270 [ dbSNP | Ensembl ].
VAR_036682

Experimental info

Mutagenesis291F → A: Slows down deactivation. Ref.22
Mutagenesis431Y → A: Slows down deactivation. Ref.22
Mutagenesis2831S → A: Abolishes phosphorylation; when associated with A-890; A-895 and A-1137. Ref.17
Mutagenesis5981N → Q: No effect on cell surface expression, but changes inactivation kinetics; when associated with A-631. Ref.16
Mutagenesis6291N → Q: Abolishes cell surface expression; has no effect on N-glycosylation. Ref.16
Mutagenesis6311S → A: No effect on cell surface expression, but changes inactivation kinetics; when associated with Q-598. Ref.16
Mutagenesis8901S → A: Abolishes phosphorylation; when associated with A-283; A-895 and A-1137. Ref.17
Mutagenesis8951T → A: Abolishes phosphorylation; when associated with A-283; A-890 and A-1137. Ref.17
Mutagenesis11371S → A: Abolishes phosphorylation; when associated with A-283; A-890 and A-895. Ref.17

Secondary structure

...................................... 1159
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D03BD4F657641FBA

FASTA1,159126,655
        10         20         30         40         50         60 
MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM 

        70         80         90        100        110        120 
QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG 

       130        140        150        160        170        180 
AVIMFILNFE VVMEKDMVGS PAHDTNHRGP PTSWLAPGRA KTFRLKLPAL LALTARESSV 

       190        200        210        220        230        240 
RSGGAGGAGA PGAVVVDVDL TPAAPSSESL ALDEVTAMDN HVAGLGPAEE RRALVGPGSP 

       250        260        270        280        290        300 
PRSAPGQLPS PRAHSLNPDA SGSSCSLART RSRESCASVR RASSADDIEA MRAGVLPPPP 

       310        320        330        340        350        360 
RHASTGAMHP LRSGLLNSTS DSDLVRYRTI SKIPQITLNF VDLKGDPFLA SPTSDREIIA 

       370        380        390        400        410        420 
PKIKERTHNV TEKVTQVLSL GADVLPEYKL QAPRIHRWTI LHYSPFKAVW DWLILLLVIY 

       430        440        450        460        470        480 
TAVFTPYSAA FLLKETEEGP PATECGYACQ PLAVVDLIVD IMFIVDILIN FRTTYVNANE 

       490        500        510        520        530        540 
EVVSHPGRIA VHYFKGWFLI DMVAAIPFDL LIFGSGSEEL IGLLKTARLL RLVRVARKLD 

       550        560        570        580        590        600 
RYSEYGAAVL FLLMCTFALI AHWLACIWYA IGNMEQPHMD SRIGWLHNLG DQIGKPYNSS 

       610        620        630        640        650        660 
GLGGPSIKDK YVTALYFTFS SLTSVGFGNV SPNTNSEKIF SICVMLIGSL MYASIFGNVS 

       670        680        690        700        710        720 
AIIQRLYSGT ARYHTQMLRV REFIRFHQIP NPLRQRLEEY FQHAWSYTNG IDMNAVLKGF 

       730        740        750        760        770        780 
PECLQADICL HLNRSLLQHC KPFRGATKGC LRALAMKFKT THAPPGDTLV HAGDLLTALY 

       790        800        810        820        830        840 
FISRGSIEIL RGDVVVAILG KNDIFGEPLN LYARPGKSNG DVRALTYCDL HKIHRDDLLE 

       850        860        870        880        890        900 
VLDMYPEFSD HFWSSLEITF NLRDTNMIPG SPGSTELEGG FSRQRKRKLS FRRRTDKDTE 

       910        920        930        940        950        960 
QPGEVSALGP GRAGAGPSSR GRPGGPWGES PSSGPSSPES SEDEGPGRSS SPLRLVPFSS 

       970        980        990       1000       1010       1020 
PRPPGEPPGG EPLMEDCEKS SDTCNPLSGA FSGVSNIFSF WGDSRGRQYQ ELPRCPAPTP 

      1030       1040       1050       1060       1070       1080 
SLLNIPLSSP GRRPRGDVES RLDALQRQLN RLETRLSADM ATVLQLLQRQ MTLVPPAYSA 

      1090       1100       1110       1120       1130       1140 
VTTPGPGPTS TSPLLPVSPL PTLTLDSLSQ VSQFMACEEL PPGAPELPQE GPTRRLSLPG 

      1150 
QLGALTSQPL HRHGSDPGS 

« Hide

Isoform B [UniParc].

Checksum: 6C3F360C310C178A
Show »

FASTA81990,108
Isoform 4 [UniParc].

Checksum: 9501F6136737A384
Show »

FASTA1,102121,029
Isoform A-USO [UniParc].

Checksum: 2C9582876D520E39
Show »

FASTA88897,542
Isoform B-USO [UniParc].

Checksum: B479DEA5B3163A13
Show »

FASTA54860,995
Isoform 3.1 [UniParc].

Checksum: 6C9DFEF9A38A3034
Show »

FASTA1,063115,636

References

« Hide 'large scale' references
[1]"A family of potassium channel genes related to eag in Drosophila and mammals."
Warmke J.W., Ganetzky B.
Proc. Natl. Acad. Sci. U.S.A. 91:3438-3442(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Hippocampus.
[2]"Genomic organization and mutational analysis of HERG, a gene responsible for familial long QT syndrome."
Itoh T., Tanaka T., Nagai R., Kamiya T., Sawayama T., Nakayama T., Tomoike H., Sakurada H., Yazaki Y., Nakamura Y.
Hum. Genet. 102:435-439(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), VARIANT LQT2 CYS-534.
[3]"Isolation of novel heart-specific genes using the BodyMap database."
Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T., Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.
Genomics 74:115-120(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A-USO).
Tissue: Heart.
[4]"Potent inhibition of HERG K+ channels by the neuroprotective agent Sipatrigine."
Downie D., Chapman C.G., Punia P., Rice S., Bahmani F., Murdock P., Pearson N., Randall A.D., Meadows H.J.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[5]"Cell cycle-dependent expression of HERG1 and HERG1B isoforms in tumor cells."
Crociani O., Guasti L., Balzi M., Becchetti A., Wanke E., Olivotto M., Wymore R.S., Arcangeli A.
J. Biol. Chem. 278:2947-2955(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[6]"Identification of a posttranslational mechanism for the regulation of hERG1 K+ channel expression and hERG1 current density in tumor cells."
Guasti L., Crociani O., Redaelli E., Pillozzi S., Polvani S., Masselli M., Mello T., Galli A., Amedei A., Wymore R.S., Wanke E., Arcangeli A.
Mol. Cell. Biol. 28:5043-5060(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B-USO), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]"A primate-specific, brain isoform of KCNH2 affects cortical physiology, cognition, neuronal repolarization and risk of schizophrenia."
Huffaker S.J., Chen J., Nicodemus K.K., Sambataro F., Yang F., Mattay V., Lipska B.K., Hyde T.M., Song J., Rujescu D., Giegling I., Mayilyan K., Proust M.J., Soghoyan A., Caforio G., Callicott J.H., Bertolino A., Meyer-Lindenberg A. expand/collapse author list , Chang J., Ji Y., Egan M.F., Goldberg T.E., Kleinman J.E., Lu B., Weinberger D.R.
Nat. Medicines 15:509-518(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3.1), SUBCELLULAR LOCATION.
Tissue: Brain.
[8]NHLBI resequencing and genotyping service (RS&G)
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"Two isoforms of the mouse ether-a-go-go-related gene coassemble to form channels with properties similar to the rapidly activating component of the cardiac delayed rectifier K+ current."
London B., Trudeau M.C., Newton K.P., Beyer A.K., Copeland N.G., Gilbert D.J., Jenkins N.A., Satler C.A., Robertson G.A.
Circ. Res. 81:870-878(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-376 (ISOFORM B).
Tissue: Heart.
[12]"Electrophysiological characterization of an alternatively processed ERG K+ channel in mouse and human hearts."
Lees-Miller J.P., Kondo C., Wang L., Duff H.J.
Circ. Res. 81:719-726(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-376 (ISOFORM B).
Tissue: Heart atrium.
[13]"Analysis of the human KCNH2(HERG) gene: identification and characterization of a novel mutation Y667X associated with long QT syndrome and a non-pathological 9 bp insertion."
Paulussen A., Yang P., Pangalos M., Verhasselt P., Marrannes R., Verfaille C., Vandenberk I., Crabbe R., Konings F., Luyten W., Armstrong M.
Hum. Mutat. 15:483-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-1159 (ISOFORM A), VARIANT GLY-ALA-GLY-189 INS.
[14]"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] OF 59-800 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 716-1159 (ISOFORMS A/B).
Tissue: Brain.
[15]"A K+ channel splice variant common in human heart lacks a C-terminal domain required for expression of rapidly activating delayed rectifier current."
Kupershmidt S., Snyders D.J., Raes A., Roden D.M.
J. Biol. Chem. 273:27231-27235(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 795-888 (ISOFORM A-USO).
Tissue: Heart ventricle.
[16]"Role of glycosylation in cell surface expression and stability of HERG potassium channels."
Gong Q., Anderson C.L., January C.T., Zhou Z.
Am. J. Physiol. 283:H77-H84(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-598; ASN-629 AND SER-631, GLYCOSYLATION AT ASN-598.
[17]"Cyclic AMP regulates the HERG K(+) channel by dual pathways."
Cui J., Melman Y., Palma E., Fishman G.I., McDonald T.V.
Curr. Biol. 10:671-674(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-283; SER-890; THR-895 AND SER-1137, PHOSPHORYLATION.
[18]"A minK-HERG complex regulates the cardiac potassium current I(Kr)."
McDonald T.V., Yu Z., Ming Z., Palma E., Meyers M.B., Wang K.-W., Goldstein S.A.N., Fishman G.I.
Nature 388:289-292(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNE1.
[19]"MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia."
Abbott G.W., Sesti F., Splawski I., Buck M.E., Lehmann M.H., Timothy K.W., Keating M.T., Goldstein S.A.N.
Cell 97:175-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNE2.
[20]"Mechanisms of pharmacological rescue of trafficking-defective hERG mutant channels in human long QT syndrome."
Gong Q., Jones M.A., Zhou Z.
J. Biol. Chem. 281:4069-4074(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CANX, CHARACTERIZATION OF VARIANT LQT2 ASP-470.
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Crystal structure and functional analysis of the HERG potassium channel N-terminus: a eukaryotic PAS domain."
Morais Cabral J.H., Lee A., Cohen S.L., Chait B.T., Li M., Mackinnon R.
Cell 95:649-655(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-135, MUTAGENESIS OF PHE-29 AND TYR-43.
[23]"A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome."
Curran M.E., Splawski I., Timothy K.W., Vincent G.M., Green E.D., Keating M.T.
Cell 80:795-803(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 ASP-470; VAL-561 AND SER-628.
[24]"Novel missense mutation in the cyclic nucleotide-binding domain of HERG causes long QT syndrome."
Satler C.A., Walsh E.P., Vesely M.R., Plummer M.H., Ginsburg G.S., Jacob H.J.
Am. J. Med. Genet. 65:27-35(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 MET-822.
[25]"Missense mutation in the pore region of HERG causes familial long QT syndrome."
Benson D.W., MacRae C.A., Vesely M.R., Walsh E.P., Seidman J.G., Seidman C.E., Satler C.A.
Circulation 93:1791-1795(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 ARG-593.
[26]"A mutation in HERG associated with notched T waves in long QT syndrome."
Dausse E., Berthet M., Denjoy I., Andre-Fouet X., Cruaud C., Bennaceur M., Faure S., Coumel P., Schwartz K., Guicheney P.
J. Mol. Cell. Cardiol. 28:1609-1615(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 THR-561.
[27]"Four novel KVLQT1 and four novel HERG mutations in familial long-QT syndrome."
Tanaka T., Nagai R., Tomoike H., Takata S., Yano K., Yabuta K., Haneda N., Nakano O., Shibata A., Sawayama T., Kasai H., Yazaki Y., Nakamura Y.
Circulation 95:565-567(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 ILE-474; HIS-611; VAL-614 AND LEU-630.
[28]"Genomic structure of three long QT syndrome genes: KVLQT1, HERG, and KCNE1."
Splawski I., Shen J., Timothy K.W., Vincent G.M., Lehmann M.H., Keating M.T.
Genomics 51:86-97(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 CYS-572; ASP-588; VAL-614 AND ALA-630.
[29]"Multiple different missense mutations in the pore region of HERG in patients with long QT syndrome."
Satler C.A., Vesely M.R., Duggal P., Ginsburg G.S., Beggs A.H.
Hum. Genet. 102:265-272(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 LEU-612; VAL-614; ASP-629; SER-629 AND SER-633.
[30]"Novel missense mutation (G601S) of HERG in a Japanese long QT syndrome family."
Akimoto K., Furutani M., Imamura S., Furutani Y., Kasanuki H., Takao A., Momma K., Matsuoka R.
Hum. Mutat. Suppl. 1:S184-S186(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 SER-601.
[31]"C-terminal HERG mutations: the role of hypokalemia and a KCNQ1-associated mutation in cardiac event occurrence."
Berthet M., Denjoy I., Donger C., Demay L., Hammoude H., Klug D., Schulze-Bahr E., Richard P., Funke H., Schwartz K., Coumel P., Hainque B., Guicheney P.
Circulation 99:1464-1470(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 LEU-818.
[32]"Novel KCNQ1 and HERG missense mutations in Dutch long-QT families."
Jongbloed R.J.E., Wilde A.A.M., Geelen J.L.M.C., Doevendans P., Schaap C., van Langen I., van Tintelen J.P., Cobben J.M., Beaufort-Krol G.C.M., Geraedts J.P.M., Smeets H.J.M.
Hum. Mutat. 13:301-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 PRO-558; CYS-582; SER-604; MET-613 AND LEU-640.
[33]"Long QT syndrome-associated mutations in the Per-Arnt-Sim (PAS) domain of HERG potassium channels accelerate channel deactivation."
Chen J., Zou A., Splawski I., Keating M.T., Sanguinetti M.C.
J. Biol. Chem. 274:10113-10118(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 LEU-29; THR-33; ARG-53; GLN-56; GLY-66; ARG-70; PRO-78 AND ARG-86.
[34]"Characterization of a novel missense mutation in the pore of HERG in a patient with long QT syndrome."
Yoshida H., Horie M., Otani H., Takano M., Tsuji K., Kubota T., Fukunami M., Sasayama S.
J. Cardiovasc. Electrophysiol. 10:1262-1270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 LYS-629.
[35]"Long QT syndrome with a high mortality rate caused by a novel G572R missense mutation in KCNH2."
Larsen L.A., Svendsen I.H., Jensen A.M., Kanters J.K., Andersen P.S., Moeller M., Soerensen S.A., Sandoee E., Jacobsen J.R., Vuust J., Christiansen M.
Clin. Genet. 57:125-130(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 ARG-572.
[36]"Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2."
Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S.G., Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M., Keating M.T.
Circulation 102:1178-1185(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2, REVIEW ON VARIANTS.
[37]"Survey of the coding region of the HERG gene in long QT syndrome reveals six novel mutations and an amino acid polymorphism with possible phenotypic effects."
Laitinen P., Fodstad H., Piippo K., Swan H., Toivonen L., Viitasalo M., Kaprio J., Kontula K.
Hum. Mutat. 15:580-581(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 TRP-176; LEU-451; HIS-569; SER-584; SER-601 AND MET-613, VARIANT THR-897.
[38]"The dominant negative LQT2 mutation A561V reduces wild-type HERG expression."
Kagan A., Yu Z., Fishman G.I., McDonald T.V.
J. Biol. Chem. 275:11241-11248(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT LQT2 VAL-561.
[39]"Bradycardia-induced long QT syndrome caused by a de novo missense mutation in the S2-S3 inner loop of HERG."
Yoshida H., Horie M., Otani H., Kawashima T., Onishi Y., Sasayama S.
Am. J. Med. Genet. 98:348-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LONG QT SYNDROME THR-490.
[40]"Characterization of a novel missense mutation E637K in the pore-S6 loop of HERG in a patient with long QT syndrome."
Hayashi K., Shimizu M., Ino H., Yamaguchi M., Mabuchi H., Hoshi N., Higashida H.
Cardiovasc. Res. 54:67-76(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 LYS-637.
[41]"Allelic variants in long-QT disease genes in patients with drug-associated torsades de pointes."
Yang P., Kanki H., Drolet B., Yang T., Wei J., Viswanathan P.C., Hohnloser S.H., Shimizu W., Schwartz P.J., Stanton M., Murray K.T., Norris K., George A.L. Jr., Roden D.M.
Circulation 105:1943-1948(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TRP-784 AND THR-897, CHARACTERIZATION OF VARIANT TRP-784.
[42]"A novel mutation (T65P) in the PAS domain of the human potassium channel HERG results in the long QT syndrome by trafficking deficiency."
Paulussen A., Raes A., Matthijs G., Snyders D.J., Cohen N., Aerssens J.
J. Biol. Chem. 277:48610-48616(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 PRO-65.
[43]"Clinical, genetic, and biophysical characterization of a homozygous HERG mutation causing severe neonatal long QT syndrome."
Johnson W.H. Jr., Yang P., Yang T., Lau Y.R., Mostella B.A., Wolff D.J., Roden D.M., Benson D.W.
Pediatr. Res. 53:744-748(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 GLN-752.
[44]"Sudden death associated with short-QT syndrome linked to mutations in HERG."
Brugada R., Hong K., Dumaine R., Cordeiro J., Gaita F., Borggrefe M., Menendez T.M., Brugada J., Pollevick G.D., Wolpert C., Burashnikov E., Matsuo K., Wu Y.S., Guerchicoff A., Bianchi F., Giustetto C., Schimpf R., Brugada P., Antzelevitch C.
Circulation 109:30-35(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SQT1 LYS-588.
[45]"Compound mutations: a common cause of severe long-QT syndrome."
Westenskow P., Splawski I., Timothy K.W., Keating M.T., Sanguinetti M.C.
Circulation 109:1834-1841(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 ILE-861.
[46]"Compendium of cardiac channel mutations in 541 consecutive unrelated patients referred for long QT syndrome genetic testing."
Tester D.J., Will M.L., Haglund C.M., Ackerman M.J.
Heart Rhythm 2:507-517(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT2 ILE-26; LEU-29; SER-31; ARG-53; LEU-55; PRO-65; ARG-70; PRO-78; VAL-85; GLN-100; SER-238; TRP-306; LEU-320; CYS-328; CYS-420; MET-421; THR-422; SER-427; TYR-456; TYR-475 DEL; CYS-534; SER-552; THR-561; VAL-561; PRO-562; LEU-571; SER-572; CYS-582; SER-584; ASP-588; ARG-596; SER-604; MET-613; VAL-614; PHE-622; ILE-623; SER-628; VAL-628; ALA-630; SER-633; ILE-635; VAL-640; PHE-641; 671-ALA--THR-675 DEL; LEU-721; TYR-774; TRP-784; ASP-788; CYS-805; ARG-820; MET-822; GLY-837; HIS-887; VAL-913; ARG-925; ILE-983; ILE-996 AND ASP-1036.
[47]"Short QT syndrome and atrial fibrillation caused by mutation in KCNH2."
Hong K., Bjerregaard P., Gussak I., Brugada R.
J. Cardiovasc. Electrophysiol. 16:394-396(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SQT1 LYS-588.
[48]"Spectrum of pathogenic mutations and associated polymorphisms in a cohort of 44 unrelated patients with long QT syndrome."
Millat G., Chevalier P., Restier-Miron L., Da Costa A., Bouvagnet P., Kugener B., Fayol L., Gonzalez Armengod C., Oddou B., Chanavat V., Froidefond E., Perraudin R., Rousson R., Rodriguez-Lafrasse C.
Clin. Genet. 70:214-227(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LONG QT SYNDROME 2/3 GLY-100; ASN-525; PRO-528; CYS-696 AND CYS-948.
[49]"Identification and functional characterization of the novel human ether-a-go-go-related gene (hERG) R744P mutant associated with hereditary long QT syndrome 2."
Aidery P., Kisselbach J., Gaspar H., Baldea I., Schweizer P.A., Becker R., Katus H.A., Thomas D.
Biochem. Biophys. Res. Commun. 418:830-835(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT2 PRO-744, CHARACTERIZATION OF VARIANT LQT2 PRO-744.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Ether-a-go-go potassium channels entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04270 mRNA. Translation: AAA62473.1.
AB009071 Genomic DNA. Translation: BAA37096.1.
AB044806 mRNA. Translation: BAB19682.1.
AF363636 mRNA. Translation: AAL37559.1.
AJ512214 mRNA. Translation: CAD54447.1.
AJ609614 mRNA. Translation: CAE82156.1.
FJ938021 mRNA. Translation: ACR24650.1.
DQ784808 Genomic DNA. Translation: ABQ01243.1.
AC006343 Genomic DNA. No translation available.
AC011234 Genomic DNA. No translation available.
CH471173 Genomic DNA. Translation: EAW54072.1.
AJ010538 expand/collapse EMBL AC list , AJ010539, AJ010540, AJ010541, AJ010542, AJ010543, AJ010544, AJ010545, AJ010546, AJ010547, AJ010548, AJ010549, AJ010550, AJ010551 Genomic DNA. Translation: CAA09232.1. Sequence problems.
CH471173 Genomic DNA. Translation: EAW54075.1.
BC001914 mRNA. Translation: AAH01914.2.
BC004311 mRNA. Translation: AAH04311.2.
AF052728 mRNA. Translation: AAC69709.1.
PIRI38465.
RefSeqNP_000229.1. NM_000238.3.
NP_001191727.1. NM_001204798.1.
NP_742053.1. NM_172056.2.
NP_742054.1. NM_172057.2.
UniGeneHs.647099.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BYWX-ray2.60A26-135[»]
1UJLNMR-A570-611[»]
2L0WNMR-A1-135[»]
2L1MNMR-A1-135[»]
2L4RNMR-A1-135[»]
2LE7NMR-A532-551[»]
4HP9X-ray2.12A10-135[»]
4HQAX-ray1.96A1-135[»]
ProteinModelPortalQ12809.
SMRQ12809. Positions 1-135, 570-664, 670-864.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109959. 20 interactions.
DIPDIP-48929N.
IntActQ12809. 6 interactions.
MINTMINT-1427435.
STRING9606.ENSP00000262186.

Chemistry

BindingDBQ12809.
ChEMBLCHEMBL2362996.
DrugBankDB01118. Amiodarone.
DB00276. Amsacrine.
DB00637. Astemizole.
DB01136. Carvedilol.
DB00604. Cisapride.
DB00204. Dofetilide.
DB01218. Halofantrine.
DB00308. Ibutilide.
DB01100. Pimozide.
DB01182. Propafenone.
DB00908. Quinidine.
DB06144. Sertindole.
DB00489. Sotalol.
DB00342. Terfenadine.
DB00661. Verapamil.
GuidetoPHARMACOLOGY572.

Protein family/group databases

TCDB1.A.1.20.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ12809.

Polymorphism databases

DMDM7531135.

Proteomic databases

PaxDbQ12809.
PRIDEQ12809.

Protocols and materials databases

DNASU3757.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262186; ENSP00000262186; ENSG00000055118. [Q12809-1]
ENST00000330883; ENSP00000328531; ENSG00000055118. [Q12809-2]
ENST00000392968; ENSP00000376695; ENSG00000055118. [Q12809-7]
ENST00000430723; ENSP00000387657; ENSG00000055118. [Q12809-5]
GeneID3757.
KEGGhsa:3757.
UCSCuc003wib.3. human. [Q12809-2]
uc003wic.3. human. [Q12809-1]

Organism-specific databases

CTD3757.
GeneCardsGC07M150642.
HGNCHGNC:6251. KCNH2.
HPACAB006838.
MIM152427. gene.
609620. phenotype.
613688. phenotype.
neXtProtNX_Q12809.
Orphanet51083. Familial short QT syndrome.
101016. Romano-Ward syndrome.
PharmGKBPA212.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2202.
HOVERGENHBG052232.
InParanoidQ12809.
KOK04905.
OMAPARDTNH.
OrthoDBEOG75B879.
PhylomeDBQ12809.
TreeFamTF313130.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkQ12809.

Gene expression databases

ArrayExpressQ12809.
BgeeQ12809.
CleanExHS_ERG.
HS_KCNH2.
GenevestigatorQ12809.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR003967. K_chnl_volt-dep_ERG.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF13426. PAS_9. 1 hit.
[Graphical view]
PRINTSPR01463. EAGCHANLFMLY.
PR01470. ERGCHANNEL.
SMARTSM00100. cNMP. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
SSF55785. SSF55785. 1 hit.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKCNH2. human.
EvolutionaryTraceQ12809.
GeneWikiHERG.
GenomeRNAi3757.
NextBio14717.
PROQ12809.
SOURCESearch...

Entry information

Entry nameKCNH2_HUMAN
AccessionPrimary (citable) accession number: Q12809
Secondary accession number(s): A5H1P7 expand/collapse secondary AC list , C4PFH9, D3DX04, O75418, O75680, Q708S9, Q9BT72, Q9BUT7, Q9H3P0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM