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O08962 (KCNH2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily H member 2
Alternative name(s):
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=RERG
Short name=r-ERG
Voltage-gated potassium channel subunit Kv11.1
Gene names
Name:Kcnh2
Synonyms:Erg
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1163 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) By similarity.

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. Heteromultimer with KCNE1 and KCNE2 By similarity. Interacts with ALG10B. Interacts with CANX By similarity. Ref.4 Ref.5

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Highly expressed in brain and testis, slightly less so in heart, adrenal, retina and thymus. Detected at lower levels in lung, soleus, tibialis, and at very low levels in cornea and lens. A shorter transcript is detected in skeletal muscle. Found in pituitary. Ref.3

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 By similarity.

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.

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from expression pattern PubMed 15365256. Source: RGD

potassium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium ion transport

Inferred from direct assay PubMed 9390998. Source: RGD

protein heterooligomerization

Inferred from direct assay Ref.4. Source: RGD

regulation of heart rate by cardiac conduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of membrane potential

Inferred from direct assay PubMed 11804849. Source: RGD

spinal cord development

Inferred from expression pattern PubMed 15365256. Source: RGD

   Cellular_componentintegral component of plasma membrane

Inferred from direct assay PubMed 11804849. Source: RGD

   Molecular_functioninward rectifier potassium channel activity

Inferred from direct assay PubMed 15677682. Source: RGD

ion channel activity

Inferred from direct assay PubMed 11804849. Source: RGD

phosphorelay sensor kinase activity

Inferred from electronic annotation. Source: InterPro

potassium channel activity

Inferred from direct assay PubMed 11804849. Source: RGD

voltage-gated potassium channel activity

Inferred from direct assay PubMed 15677682. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11631163Potassium voltage-gated channel subfamily H member 2
PRO_0000054003

Regions

Topological domain1 – 405405Cytoplasmic Potential
Transmembrane406 – 42621Helical; Name=Segment S1; Potential
Topological domain427 – 45226Extracellular Potential
Transmembrane453 – 47321Helical; Name=Segment S2; Potential
Topological domain474 – 49724Cytoplasmic Potential
Transmembrane498 – 51821Helical; Name=Segment S3; Potential
Topological domain519 – 5224Extracellular Potential
Transmembrane523 – 54321Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain544 – 5496Cytoplasmic Potential
Transmembrane550 – 57021Helical; Name=Segment S5; Potential
Topological domain571 – 61343Extracellular Potential
Intramembrane614 – 63421Pore-forming; Name=Segment H5; Potential
Topological domain635 – 6406Extracellular Potential
Transmembrane641 – 66121Helical; Name=Segment S6; Potential
Topological domain662 – 1163502Cytoplasmic Potential
Domain17 – 8872PAS
Domain92 – 14453PAC
Nucleotide binding744 – 861118cNMP
Motif626 – 6316Selectivity filter By similarity

Amino acid modifications

Modified residue3221Phosphoserine By similarity
Glycosylation6001N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis6301G → S: Dominant negative mutant; abolishes ERG current. Ref.4
Sequence conflict4111V → A in AAC53160. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08962 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: F0D75B0B532D9EA2

FASTA1,163126,952
        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 STSWLASGRA KTFRLKLPAL LALTARESPM 

       190        200        210        220        230        240 
RTGSTGSPGA PGAVVVDVDL TPAAPSSESL ALDEVSAMDN HVAGLGPAEE RRALVGPASA 

       250        260        270        280        290        300 
SPVASIPGPH PSPRAQSLNP DASGSSCSLA RTRSRESCAS VRRASSADDI EAMRAGALPL 

       310        320        330        340        350        360 
PPRHASTGAM HPLRSGLLNS TSDSDLVRYR TISKIPQITL NFVDLKGDPF LASPTSDREI 

       370        380        390        400        410        420 
IAPKIKERTH NVTEKVTQVL SLGADVLPEY KLQAPRIHRW TILHYSPFKA VWDWLILLLV 

       430        440        450        460        470        480 
IYTAVFTPYS AAFLLKETED GSQAPDCGYA CQPLAVVDLL VDIMFIVDIL INFRTTYVNA 

       490        500        510        520        530        540 
NEEVVSHPGR IAVHYFKGWF LIDMVAAIPF DLLIFGSGSE ELIGLLKTAR LLRLVRVARK 

       550        560        570        580        590        600 
LDRYSEYGAA VLFLLMCTFA LIAHWLACIW YAIGNMEQPH MDSHIGWLHN LGDQIGKPYN 

       610        620        630        640        650        660 
SSGLGGPSIK DKYVTALYFT FSSLTSVGFG NVSPNTNSEK IFSICVMLIG SLMYASIFGN 

       670        680        690        700        710        720 
VSAIIQRLYS GTARYHTQML RVREFIRFHQ IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK 

       730        740        750        760        770        780 
GFPECLQADI CLHLNRSLLQ HCKPFRGATK GCLRALAMKF KTTHAPPGDT LVHAGDLLTA 

       790        800        810        820        830        840 
LYFISRGSIE ILRGDVVVAI LGKNDIFGEP LNLYARPGKS NGDVRALTYC DLHKIHRDDL 

       850        860        870        880        890        900 
LEVLDMYPEF SDHFWSSLEI TFNLRDTNMI PGSPSSAELE SGFNRQRKRK LSFRRRTDKD 

       910        920        930        940        950        960 
TEQPGEVSAL GQGPARVGPG PSCRGQPGGP WGESPSSGPS SPESSEDEGP GRSSSPLRLV 

       970        980        990       1000       1010       1020 
PFSSPRPPGD SPGGEPLTED GEKSSDTCNP LSGAFSGVSN IFSFWGDSRG RQYQELPRCP 

      1030       1040       1050       1060       1070       1080 
APAPSLLNIP LSSPGRRSRG DVESRLDALQ RQLNRLETRL SADMATVLQL LQRQMTLVPP 

      1090       1100       1110       1120       1130       1140 
AYSAVTTPGP GPTSTSPLLP VGPVPTLTLD SLSQVSQFVA FEELPAGAPE LPQDGPTRRL 

      1150       1160 
SLPGQLGALT SQPLHRHGSD PGS 

« Hide

References

[1]"RERG is a molecular correlate of the inward-rectifying K current in clonal rat pituitary cells."
Bauer C.K., Engeland B., Wulfsen I., Ludwig J., Pongs O., Schwarz J.R.
Recept. Channels 6:19-29(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain cortex.
[2]"Tissue and species distribution of mRNA for the IKr-like K+ channel, erg."
Wymore R.S., Gintant G.A., Wymore R.T., Dixon J.E., McKinnon D., Cohen I.S.
Circ. Res. 80:261-268(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 409-568.
[3]"Expression of mRNA for voltage-dependent and inward-rectifying K channels in GH3/B6 cells and rat pituitary."
Wulfsen I., Hauber H.-P., Schiemann D., Bauer C.K., Schwarz J.R.
J. Neuroendocrinol. 12:263-272(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Erg1, erg2 and erg3 K channel subunits are able to form heteromultimers."
Wimmers S., Wulfsen I., Bauer C.K., Schwarz J.R.
Pflugers Arch. 441:450-455(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNH6 AND KCNH7, MUTAGENESIS OF GLY-630.
[5]"The IKr drug response is modulated by KCR1 in transfected cardiac and noncardiac cell lines."
Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S., Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R.
FASEB J. 17:2263-2265(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALG10B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z96106 mRNA. Translation: CAB09536.1.
U75210 mRNA. Translation: AAC53160.1.
RefSeqNP_446401.1. NM_053949.1.
UniGeneRn.10970.

3D structure databases

ProteinModelPortalO08962.
SMRO08962. Positions 26-135, 572-613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250619. 1 interaction.
STRING10116.ENSRNOP00000013800.

Chemistry

GuidetoPHARMACOLOGY572.

PTM databases

PhosphoSiteO08962.

Proteomic databases

PaxDbO08962.
PRIDEO08962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID117018.
KEGGrno:117018.

Organism-specific databases

CTD3757.
RGD621414. Kcnh2.

Phylogenomic databases

eggNOGCOG2202.
HOGENOMHOG000230793.
HOVERGENHBG052232.
InParanoidO08962.
KOK04905.
PhylomeDBO08962.

Gene expression databases

GenevestigatorO08962.

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

NextBio619763.
PROO08962.

Entry information

Entry nameKCNH2_RAT
AccessionPrimary (citable) accession number: O08962
Secondary accession number(s): O08720
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families