Q12809 (KCNH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1159 AA.
Sequence status	Complete.
Protein existence	Evidence 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). Isoform 3 has no channel activity by itself, but modulates channel characteristics when associated with isoform 1.
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. Ref.15 Ref.16
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Highly expressed in heart and brain.
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.14 Ref.17
Involvement in disease	Defects in KCNH2 are the cause of long QT syndrome type 2 (LQT2) [MIM:613688]. Long QT syndromes are heart disorders 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. Deafness is often associated with LQT2. Ref.2 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.36 Ref.38 Ref.39 Ref.41 Defects in KCNH2 are the cause of short QT syndrome type 1 (SQT1) [MIM:609620]. Short QT syndromes are heart disorders characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. They cause syncope and sudden death. Ref.40 Ref.42
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 AAC69709.1 differs from that shown. Reason: Cloning artifact. The sequence AAH01914.2 differs from that shown. Reason: Cloning artifact. The sequence BAB19682.1 differs from that shown. Reason: Cloning artifact. The sequence CAA09232.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness Disease mutation Long QT syndrome Short QT syndrome
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ionic channel Potassium channel Voltage-gated channel
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood circulation Non-traceable author statement. Source: ProtInc muscle contraction Traceable author statement. Source: ProtInc regulation of heart contraction Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro synaptic transmission Traceable author statement. Source: Reactome
Cellular component	voltage-gated potassium channel complex Traceable author statement. Source: ProtInc
Molecular function	delayed rectifier potassium channel activity Traceable author statement. Source: ProtInc two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (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 2 (identifier: Q12809-2)

Also known as: B;

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1159

1159

Potassium voltage-gated channel subfamily H member 2

PRO_0000053999

Regions

Topological domain

1 – 403

403

Cytoplasmic Potential

Transmembrane

404 – 424

21

Helical; Name=Segment S1; Potential

Topological domain

425 – 450

26

Extracellular Potential

Transmembrane

451 – 471

21

Helical; Name=Segment S2; Potential

Topological domain

472 – 495

24

Cytoplasmic Potential

Transmembrane

496 – 516

21

Helical; Name=Segment S3; Potential

Topological domain

517 – 520

4

Extracellular Potential

Transmembrane

521 – 541

21

Helical; Voltage-sensor; Name=Segment S4; Potential

Topological domain

542 – 547

6

Cytoplasmic Potential

Transmembrane

548 – 568

21

Helical; Name=Segment S5; Potential

Topological domain

569 – 611

43

Extracellular Potential

Intramembrane

612 – 632

21

Pore-forming; Name=Segment H5; Potential

Topological domain

633 – 638

6

Extracellular Potential

Transmembrane

639 – 659

21

Helical; Name=Segment S6; Potential

Topological domain

660 – 1159

500

Cytoplasmic Potential

Domain

41 – 70

30

PAS

Domain

92 – 144

53

PAC

Nucleotide binding

742 – 842

101

cNMP

Motif

624 – 629

6

Selectivity filter By similarity

Compositional bias

297 – 300

4

Poly-Pro

Amino acid modifications

Modified residue

320

1

Phosphoserine Ref.17

Glycosylation

598

1

N-linked (GlcNAc...) Ref.13

Natural variations

Alternative sequence

1 – 376

376

MPVRR…EKVTQ → MAAPAGKASRTGALRPRAQK GRVRRAVRISSLVAQE in isoform 2.

VSP_000965

Alternative sequence

139 – 195

57

Missing in isoform 4.

VSP_000966

Natural variant

29

1

F → L in LQT2. Ref.29

VAR_008907

Natural variant

33

1

N → T in LQT2. Ref.29

VAR_008908

Natural variant

47

1

G → V in LQT2.

VAR_009909

Natural variant

53

1

G → R in LQT2. Ref.29

VAR_008909

Natural variant

56

1

R → Q in LQT2. Ref.29

VAR_008910

Natural variant

65

1

T → P in LQT2. Ref.38
Corresponds to variant rs28933095 [ dbSNP | Ensembl ].

VAR_014371

Natural variant

66

1

C → G in LQT2. Ref.29

VAR_008911

Natural variant

70

1

H → R in LQT2. Ref.29

VAR_008912

Natural variant

72

1

P → Q in LQT2.

VAR_009910

Natural variant

78

1

A → P in LQT2. Ref.29

VAR_008913

Natural variant

86

1

L → R in LQT2. Ref.29

VAR_008914

Natural variant

100

1

R → G in LQT2; digenic; associated with the Asn-1819 mutation on the SCN5A gene. Ref.43

VAR_036669

Natural variant

176

1

R → W in LQT2. Ref.34
Corresponds to variant rs36210422 [ dbSNP | Ensembl ].

VAR_008915

Natural variant

181

1

R → Q.
Corresponds to variant rs41308954 [ dbSNP | Ensembl ].

VAR_036670

Natural variant

189

1

G → GGAG. Ref.33

VAR_014372

Natural variant

312

1

R → C in LQT2.

VAR_009911

Natural variant

347

1

P → S in LQT2.

VAR_009912

Natural variant

436

1

T → M in LQT2.

VAR_008916

Natural variant

451

1

P → L in LQT2. Ref.34

VAR_014373

Natural variant

470

1

N → D in LQT2. Ref.19

VAR_008578

Natural variant

474

1

T → I in LQT2. Ref.23

VAR_008917

Natural variant

490

1

A → T in long QT syndrome; bradycardia-induced. Ref.35
Corresponds to variant rs28928905 [ dbSNP | Ensembl ].

VAR_036671

Natural variant

500 – 508

9

Missing in LQT2.

VAR_009178

Natural variant

525

1

K → N in long QT syndrome 2/3; located on the same allele as Pro-528. Ref.43

VAR_036672

Natural variant

528

1

R → P in long QT syndrome 2/3; located on the same allele as Asn-525. Ref.43

VAR_036673

Natural variant

531

1

R → Q in LQT2.

VAR_009913

Natural variant

534

1

R → C in LQT2. Ref.2

VAR_008579

Natural variant

552

1

L → S in LQT2.

VAR_008918

Natural variant

558

1

A → P in LQT2. Ref.28

VAR_008919

Natural variant

561

1

A → T in LQT2. Ref.22

VAR_014374

Natural variant

561

1

A → V in LQT2. Ref.19

VAR_008580

Natural variant

564

1

L → P in LQT2.

VAR_008920

Natural variant

569

1

Y → H in LQT2. Ref.34

VAR_008921

Natural variant

572

1

G → C in LQT2. Ref.24

VAR_008923

Natural variant

572

1

G → R in LQT2; severe form. Ref.31

VAR_008922

Natural variant

582

1

R → C in LQT2. Ref.28

VAR_008581

Natural variant

584

1

G → S in LQT2. Ref.34

VAR_008924

Natural variant

585

1

W → C in LQT2.

VAR_009914

Natural variant

588

1

N → D in LQT2. Ref.24

VAR_008925

Natural variant

588

1

N → K in SQT1. Ref.40 Ref.42

VAR_023840

Natural variant

593

1

I → R in LQT2. Ref.21
Corresponds to variant rs28928904 [ dbSNP | Ensembl ].

VAR_008582

Natural variant

593

1

I → T in LQT2.

VAR_009915

Natural variant

601

1

G → S in LQT2. Ref.26 Ref.34

VAR_008926

Natural variant

604

1

G → S in LQT2. Ref.28

VAR_008927

Natural variant

609

1

D → N in LQT2.

VAR_009916

Natural variant

611

1

Y → H in LQT2. Ref.23

VAR_008928

Natural variant

612

1

V → L in LQT2. Ref.25

VAR_008929

Natural variant

613

1

T → M in LQT2. Ref.28 Ref.34

VAR_008930

Natural variant

614

1

A → V in LQT2. Ref.23 Ref.24 Ref.25

VAR_008931

Natural variant

615

1

L → V in LQT2.

VAR_014375

Natural variant

626

1

G → S in LQT2.

VAR_014376

Natural variant

627

1

F → L in LQT2.

VAR_014377

Natural variant

628

1

G → S in LQT2. Ref.19

VAR_008583

Natural variant

629

1

N → D in LQT2. Ref.25

VAR_008932

Natural variant

629

1

N → K in LQT2. Ref.30

VAR_008933

Natural variant

629

1

N → S in LQT2. Ref.25

VAR_009179

Natural variant

630

1

V → A in LQT2. Ref.24

VAR_008935

Natural variant

630

1

V → L in LQT2. Ref.23

VAR_008934

Natural variant

632

1

P → S in LQT2.

VAR_014378

Natural variant

633

1

N → S in LQT2. Ref.25

VAR_008936

Natural variant

637

1

E → K in LQT2. Ref.36

VAR_014379

Natural variant

638

1

K → E in LQT2.

VAR_014380

Natural variant

638

1

Missing in LQT2.

VAR_014381

Natural variant

640

1

F → L in LQT2. Ref.28

VAR_008937

Natural variant

645

1

M → L in LQT2.

VAR_014382

Natural variant

696

1

R → C in long QT syndrome 2/3. Ref.43

VAR_036674

Natural variant

752

1

R → Q in LQT2. Ref.39

VAR_036675

Natural variant

752

1

R → W in LQT2.

VAR_014383

Natural variant

784

1

R → 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.37

VAR_036676

Natural variant

805

1

F → C in LQT2.

VAR_014384

Natural variant

805

1

F → S in LQT2.

VAR_014385

Natural variant

818

1

S → L in LQT2. Ref.27

VAR_008938

Natural variant

822

1

V → M in LQT2. Ref.20

VAR_008584

Natural variant

823

1

R → W in LQT2.

VAR_014386

Natural variant

861

1

N → I in LQT2. Ref.41

VAR_014387

Natural variant

897

1

K → T. Ref.34 Ref.37
Corresponds to variant rs1805123 [ dbSNP | Ensembl ].

VAR_014388

Natural variant

917

1

P → L in LQT2.

VAR_014389

Natural variant

922

1

R → W in LQT2.

VAR_014390

Natural variant

948

1

R → C in long QT syndrome 2/3. Ref.43

VAR_036677

Natural variant

1016

1

P → L.
Corresponds to variant rs41313074 [ dbSNP | Ensembl ].

VAR_036679

Natural variant

1016

1

P → S.
Corresponds to variant rs41307280 [ dbSNP | Ensembl ].

VAR_036678

Natural variant

1020

1

P → S.
Corresponds to variant rs41307274 [ dbSNP | Ensembl ].

VAR_036680

Natural variant

1026

1

P → L.
Corresponds to variant rs41307271 [ dbSNP | Ensembl ].

VAR_036681

Natural variant

1055

1

R → Q.
Corresponds to variant rs41307270 [ dbSNP | Ensembl ].

VAR_036682

Experimental info

Mutagenesis

29

1

F → A: Slows down deactivation. Ref.18

Mutagenesis

43

1

Y → A: Slows down deactivation. Ref.18

Mutagenesis

283

1

S → A: Abolishes phosphorylation; when associated with A-890; A-895 and A-1137. Ref.14

Mutagenesis

598

1

N → Q: No effect on cell surface expression, but changes inactivation kinetics; when associated with A-631. Ref.13

Mutagenesis

629

1

N → Q: Abolishes cell surface expression; has no effect on N-glycosylation. Ref.13

Mutagenesis

631

1

S → A: No effect on cell surface expression, but changes inactivation kinetics; when associated with Q-598. Ref.13

Mutagenesis

890

1

S → A: Abolishes phosphorylation; when associated with A-283; A-895 and A-1137. Ref.14

Mutagenesis

895

1

T → A: Abolishes phosphorylation; when associated with A-283; A-890 and A-1137. Ref.14

Mutagenesis

1137

1

S → A: Abolishes phosphorylation; when associated with A-283; A-890 and A-895. Ref.14

Secondary structure

1

.

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1159

Helix Strand Turn

Details...

Beta strand

28 – 33

6

Beta strand

36 – 38

3

Beta strand

40 – 44

5

Helix

46 – 52

7

Helix

56 – 59

4

Helix

67 – 69

3

Helix

76 – 87

12

Beta strand

92 – 99

8

Beta strand

105 – 116

12

Beta strand

122 – 134

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D03BD4F657641FBA	FASTA	1,159	126,655
	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
	Isoform 2 (B) [UniParc]. Checksum: 6C3F360C310C178A	FASTA	819	90,108
	10 20 30 40 50 60 MAAPAGKASR TGALRPRAQK GRVRRAVRIS SLVAQEVLSL GADVLPEYKL QAPRIHRWTI 70 80 90 100 110 120 LHYSPFKAVW DWLILLLVIY TAVFTPYSAA FLLKETEEGP PATECGYACQ PLAVVDLIVD 130 140 150 160 170 180 IMFIVDILIN FRTTYVNANE EVVSHPGRIA VHYFKGWFLI DMVAAIPFDL LIFGSGSEEL 190 200 210 220 230 240 IGLLKTARLL RLVRVARKLD RYSEYGAAVL FLLMCTFALI AHWLACIWYA IGNMEQPHMD 250 260 270 280 290 300 SRIGWLHNLG DQIGKPYNSS GLGGPSIKDK YVTALYFTFS SLTSVGFGNV SPNTNSEKIF 310 320 330 340 350 360 SICVMLIGSL MYASIFGNVS AIIQRLYSGT ARYHTQMLRV REFIRFHQIP NPLRQRLEEY 370 380 390 400 410 420 FQHAWSYTNG IDMNAVLKGF PECLQADICL HLNRSLLQHC KPFRGATKGC LRALAMKFKT 430 440 450 460 470 480 THAPPGDTLV HAGDLLTALY FISRGSIEIL RGDVVVAILG KNDIFGEPLN LYARPGKSNG 490 500 510 520 530 540 DVRALTYCDL HKIHRDDLLE VLDMYPEFSD HFWSSLEITF NLRDTNMIPG SPGSTELEGG 550 560 570 580 590 600 FSRQRKRKLS FRRRTDKDTE QPGEVSALGP GRAGAGPSSR GRPGGPWGES PSSGPSSPES 610 620 630 640 650 660 SEDEGPGRSS SPLRLVPFSS PRPPGEPPGG EPLMEDCEKS SDTCNPLSGA FSGVSNIFSF 670 680 690 700 710 720 WGDSRGRQYQ ELPRCPAPTP SLLNIPLSSP GRRPRGDVES RLDALQRQLN RLETRLSADM 730 740 750 760 770 780 ATVLQLLQRQ MTLVPPAYSA VTTPGPGPTS TSPLLPVSPL PTLTLDSLSQ VSQFMACEEL 790 800 810 PPGAPELPQE GPTRRLSLPG QLGALTSQPL HRHGSDPGS
	Isoform 4 [UniParc]. Checksum: 9501F6136737A384	FASTA	1,102	121,029
	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 VVMEKDMVVD VDLTPAAPSS ESLALDEVTA MDNHVAGLGP AEERRALVGP 190 200 210 220 230 240 GSPPRSAPGQ LPSPRAHSLN PDASGSSCSL ARTRSRESCA SVRRASSADD IEAMRAGVLP 250 260 270 280 290 300 PPPRHASTGA MHPLRSGLLN STSDSDLVRY RTISKIPQIT LNFVDLKGDP FLASPTSDRE 310 320 330 340 350 360 IIAPKIKERT HNVTEKVTQV LSLGADVLPE YKLQAPRIHR WTILHYSPFK AVWDWLILLL 370 380 390 400 410 420 VIYTAVFTPY SAAFLLKETE EGPPATECGY ACQPLAVVDL IVDIMFIVDI LINFRTTYVN 430 440 450 460 470 480 ANEEVVSHPG RIAVHYFKGW FLIDMVAAIP FDLLIFGSGS EELIGLLKTA RLLRLVRVAR 490 500 510 520 530 540 KLDRYSEYGA AVLFLLMCTF ALIAHWLACI WYAIGNMEQP HMDSRIGWLH NLGDQIGKPY 550 560 570 580 590 600 NSSGLGGPSI KDKYVTALYF TFSSLTSVGF GNVSPNTNSE KIFSICVMLI GSLMYASIFG 610 620 630 640 650 660 NVSAIIQRLY SGTARYHTQM LRVREFIRFH QIPNPLRQRL EEYFQHAWSY TNGIDMNAVL 670 680 690 700 710 720 KGFPECLQAD ICLHLNRSLL QHCKPFRGAT KGCLRALAMK FKTTHAPPGD TLVHAGDLLT 730 740 750 760 770 780 ALYFISRGSI EILRGDVVVA ILGKNDIFGE PLNLYARPGK SNGDVRALTY CDLHKIHRDD 790 800 810 820 830 840 LLEVLDMYPE FSDHFWSSLE ITFNLRDTNM IPGSPGSTEL EGGFSRQRKR KLSFRRRTDK 850 860 870 880 890 900 DTEQPGEVSA LGPGRAGAGP SSRGRPGGPW GESPSSGPSS PESSEDEGPG RSSSPLRLVP 910 920 930 940 950 960 FSSPRPPGEP PGGEPLMEDC EKSSDTCNPL SGAFSGVSNI FSFWGDSRGR QYQELPRCPA 970 980 990 1000 1010 1020 PTPSLLNIPL SSPGRRPRGD VESRLDALQR QLNRLETRLS ADMATVLQLL QRQMTLVPPA 1030 1040 1050 1060 1070 1080 YSAVTTPGPG PTSTSPLLPV SPLPTLTLDS LSQVSQFMAC EELPPGAPEL PQEGPTRRLS 1090 1100 LPGQLGALTS QPLHRHGSDP GS

References

	« Hide 'large scale' referencesShow '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: 8159766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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: 9600240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT LQT2 CYS-534.
[3]	"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 1).
[4]	"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: 12431979] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	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. , 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].
[7]	"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: 11374908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-800 (ISOFORM 1). Tissue: Heart.
[8]	"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: 9351462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-376 (ISOFORM 2). Tissue: Heart.
[9]	"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: 9351446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-376 (ISOFORM 2). Tissue: Heart atrium.
[10]	"Analysis of the human HERG gene: intron localisation and identification of a novel inherited mutation associated with long QT." Yang P., Paulussen A., Verhasselt P., Crabbe R., Luyten W., Armstrong M. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-1159 (ISOFORM 1).
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-800 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 716-1159 (ISOFORMS 1/2). Tissue: Brain.
[12]	"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: 9765245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 795-800 (ISOFORMS 1/2). Tissue: Heart ventricle.
[13]	"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: 12063277] [Abstract] Cited for: MUTAGENESIS OF ASN-598; ASN-629 AND SER-631, GLYCOSYLATION AT ASN-598.
[14]	"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: 10837251] [Abstract] Cited for: MUTAGENESIS OF SER-283; SER-890; THR-895 AND SER-1137, PHOSPHORYLATION.
[15]	"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: 9230439] [Abstract] Cited for: INTERACTION WITH KCNE1.
[16]	"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: 10219239] [Abstract] Cited for: INTERACTION WITH KCNE2.
[17]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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: 9845367] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-135, MUTAGENESIS OF PHE-29 AND TYR-43.
[19]	"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: 7889573] [Abstract] Cited for: VARIANTS LQT2 ASP-470; VAL-561 AND SER-628.
[20]	"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: 8914737] [Abstract] Cited for: VARIANT LQT2 MET-822.
[21]	"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: 8635257] [Abstract] Cited for: VARIANT LQT2 ARG-593.
[22]	"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: 8877771] [Abstract] Cited for: VARIANT LQT2 THR-561.
[23]	"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: 9024139] [Abstract] Cited for: VARIANTS LQT2 ILE-474; HIS-611; VAL-614 AND LEU-630.
[24]	"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: 9693036] [Abstract] Cited for: VARIANTS LQT2 CYS-572; ASP-588; VAL-614 AND ALA-630.
[25]	"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: 9544837] [Abstract] Cited for: VARIANTS LQT2 LEU-612; VAL-614; ASP-629; SER-629 AND SER-633.
[26]	"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: 9452080] [Abstract] Cited for: VARIANT LQT2 SER-601.
[27]	"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: 10086971] [Abstract] Cited for: VARIANT LQT2 LEU-818.
[28]	"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: 10220144] [Abstract] Cited for: VARIANTS LQT2 PRO-558; CYS-582; SER-604; MET-613 AND LEU-640.
[29]	"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: 10187793] [Abstract] Cited for: VARIANTS LQT2 LEU-29; THR-33; ARG-53; GLN-56; GLY-66; ARG-70; PRO-78 AND ARG-86.
[30]	"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: 10517660] [Abstract] Cited for: VARIANT LQT2 LYS-629.
[31]	"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: 10735633] [Abstract] Cited for: VARIANT LQT2 ARG-572.
[32]	"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: 10973849] [Abstract] Cited for: VARIANTS LQT2, REVIEW ON VARIANTS.
[33]	"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: 10790218] [Abstract] Cited for: VARIANT GLY-ALA-GLY-189 INS.
[34]	"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: 10862094] [Abstract] Cited for: VARIANTS LQT2 TRP-176; LEU-451; HIS-569; SER-584; SER-601 AND MET-613, VARIANT THR-897.
[35]	"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: 11170080] [Abstract] Cited for: VARIANT LONG QT SYNDROME THR-490.
[36]	"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: 12062363] [Abstract] Cited for: VARIANT LQT2 LYS-637.
[37]	"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: 11997281] [Abstract] Cited for: VARIANTS TRP-784 AND THR-897, CHARACTERIZATION OF VARIANT TRP-784.
[38]	"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: 12354768] [Abstract] Cited for: VARIANT LQT2 PRO-65.
[39]	"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: 12621127] [Abstract] Cited for: VARIANT LQT2 GLN-752.
[40]	"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: 14676148] [Abstract] Cited for: VARIANT SQT1 LYS-588.
[41]	"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: 15051636] [Abstract] Cited for: VARIANT LQT2 ILE-861.
[42]	"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: 15828882] [Abstract] Cited for: VARIANT SQT1 LYS-588.
[43]	"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: 16922724] [Abstract] Cited for: VARIANTS LONG QT SYNDROME 2/3 GLY-100; ASN-525; PRO-528; CYS-696 AND CYS-948.
+	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.
AF363636 mRNA. Translation: AAL37559.1.
AJ512214 mRNA. Translation: CAD54447.1.
DQ784808 Genomic DNA. Translation: ABQ01243.1.
CH471173 Genomic DNA. Translation: EAW54072.1.
AB044806 mRNA. Translation: BAB19682.1. Sequence problems.
AJ010538 , 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. Sequence problems.
BC004311 mRNA. Translation: AAH04311.2.
AF052728 mRNA. Translation: AAC69709.1. Sequence problems.

IPI

IPI00029662.
IPI00172614.
IPI00221191.

PIR

I38465.

RefSeq

NP_000229.1. NM_000238.3.
NP_001191727.1. NM_001204798.1.
NP_742053.1. NM_172056.2.
NP_742054.1. NM_172057.2.

UniGene

Hs.647099.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BYW	X-ray	2.60	A	26-135	[»]
1UJL	NMR	-	A	570-611	[»]
2L0W	NMR	-	A	1-135	[»]
2L1M	NMR	-	A	1-135	[»]
2L4R	NMR	-	A	1-135	[»]

ProteinModelPortal

Q12809.

SMR

Q12809. Positions 1-135, 570-664, 667-866.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48929N.

IntAct

Q12809. 5 interactions.

MINT

MINT-1427435.

STRING

Q12809.

Protein family/group databases

TCDB

1.A.1.20.1. voltage-gated ion channel (VIC) superfamily.

PTM databases

PhosphoSite

Q12809.

Polymorphism databases

DMDM

7531135.

Proteomic databases

PRIDE

Q12809.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262186; ENSP00000262186; ENSG00000055118.

GeneID

3757.

KEGG

hsa:3757.

UCSC

uc003wib.1. human.
uc003wic.1. human.
uc003wie.1. human.

Organism-specific databases

CTD

3757.

GeneCards

GC07M150642.

H-InvDB

HIX0007217.

HGNC

HGNC:6251. KCNH2.

HPA

CAB006838.

MIM

152427. gene.
609620. phenotype.
613688. phenotype.

neXtProt

NX_Q12809.

Orphanet

51083. Familial short QT syndrome.
101016. Romano-Ward syndrome.

PharmGKB

PA212.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG717083.

HOVERGEN

HBG052232.

InParanoid

Q12809.

OMA

PARDTNH.

OrthoDB

EOG4RJG0T.

PhylomeDB

Q12809.

Enzyme and pathway databases

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q12809.

Bgee

Q12809.

CleanEx

HS_ERG.
HS_KCNH2.

Genevestigator

Q12809.

GermOnline

ENSG00000055118. Homo sapiens.

Family and domain databases

InterPro

IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR003967. K_chnl_volt-dep_ERG.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
IPR014710. RmlC-like_jellyroll.
[Graphical view]

Gene3D

G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.

KO

K04905.

Pfam

PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]

PRINTS

PR01463. EAGCHANLFMLY.
PR01470. ERGCHANNEL.

SMART

SM00100. cNMP. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]

SUPFAM

SSF51206. cNMP_binding. 1 hit.

TIGRFAMs

TIGR00229. Sensory_box. 1 hit.

PROSITE

PS00888. CNMP_BINDING_1. False negative.
PS00889. CNMP_BINDING_2. False negative.
PS50042. CNMP_BINDING_3. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01118. 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.

NextBio

14717.

SOURCE

Search...

Entry information

Entry name

KCNH2_HUMAN

Accession

Primary (citable) accession number: Q12809
Secondary accession number(s): A5H1P7 , D3DX04, O75418, O75680, Q9BT72, Q9BUT7, Q9H3P0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.