Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Potassium voltage-gated channel subfamily H member 1

Gene

KCNH1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. Channel properties may be modulated by subunit assembly, but not by cyclic nucleotides (By similarity). Mediates IK(NI) current in myoblasts (By similarity). Involved in the regulation of cell proliferation and differentiation, as adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calmodulin-binding, Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily H member 1
Alternative name(s):
Ether-a-go-go potassium channel 1
Short name:
EAG channel 1
Short name:
bEAG
Voltage-gated potassium channel subunit Kv10.1
Gene namesi
Name:KCNH1
Synonyms:EAG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Nucleus inner membrane By similarity; Multi-pass membrane protein By similarity
  • Early endosome membrane By similarity

  • Note: Perinuclear KCNH1 is located to NPC-free islands.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 220220CytoplasmicSequence analysisAdd
BLAST
Transmembranei221 – 24121Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini242 – 2487ExtracellularSequence analysis
Transmembranei249 – 26921Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini270 – 29425CytoplasmicSequence analysisAdd
BLAST
Transmembranei295 – 31521Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini316 – 34934ExtracellularSequence analysisAdd
BLAST
Transmembranei350 – 37021Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini371 – 3766CytoplasmicSequence analysis
Transmembranei377 – 39721Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini398 – 45053ExtracellularSequence analysisAdd
BLAST
Intramembranei451 – 47121Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Topological domaini472 – 4776ExtracellularSequence analysis
Transmembranei478 – 49821Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini499 – 987489CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 987987Potassium voltage-gated channel subfamily H member 1PRO_0000053993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence analysis
Modified residuei897 – 8971PhosphoserineBy similarity
Modified residuei972 – 9721PhosphoserineBy similarity
Modified residuei976 – 9761PhosphoserineBy similarity
Modified residuei979 – 9791PhosphoserineBy similarity

Post-translational modificationi

Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO18965.

Expressioni

Tissue specificityi

Detected in cerebellum, cortex and retina.

Interactioni

Subunit structurei

The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Heteromultimer with KCNH5/EAG2 (By similarity). Interacts with ALG10B (By similarity). Interacts with RABEP1 (By similarity). Interacts (via C-terminus) with CTTN (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO18965.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni673 – 77098Calmodulin-bindingBy similarityAdd
BLAST
Regioni699 – 7013Interaction with cyclic nucleotide-binding pocketBy similarity
Regioni922 – 96241CAD (involved in subunit assembly)By similarityAdd
BLAST

Motif

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

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
The C-terminal region interacts with the cyclic nucleotide-binding domain and contributes to regulate channel gating.By similarity
The PAS domain interacts with the cyclic nucleotide-binding domain and contributes to regulate channel gating.By similarity
The cyclic nucleotide-binding domain lacks residues that are essential for nucleotide-binding and cannot bind cyclic nucleotides. Instead, residues from the C-terminal domain (the so-called intrinsic ligand) bind in the cavity that would be expected to bind cyclic nucleotides. Interaction with the C-terminal region hinders interaction with CALM and reduces the affinity for CALM.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG101348.
InParanoidiO18965.
KOiK04904.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 2 (identifier: O18965-1) [UniParc]FASTAAdd to basket

Also known as: EAG2

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

« Hide

        10         20         30         40         50
MTMAGGRKGL VAPQNTFLEN IVRRSNDTNF VLGNAQIVDW PIVYSNDGFC
60 70 80 90 100
KLSGYHRAEV MQKSSTCSFM YGELTDKDTI EKVRQTFENY EMNSFEILMY
110 120 130 140 150
KKNRTPVWFF VKIAPIRNEQ DKVVLFLCTF SDITAFKQPI EDDSCKGWGK
160 170 180 190 200
FARLTRALTS SRGVLQQLAP SVQKGENVHK HSRLAEVLQL GSDILPQYKQ
210 220 230 240 250
EAPKTPPHII LHYCVFKTTW DWIILILTFY TAILVPYNVS FKTRQNNVAW
260 270 280 290 300
LVVDSIVDVI FLVDIVLNFH TTFVGPAGEV ISDPKLIRMN YLKTWFVIDL
310 320 330 340 350
LSCLPYDVIN AFENVDEVSA FMGDPGKIGF ADQIPPPLEG RESQGISSLF
360 370 380 390 400
SSLKVVRLLR LGRVARKLDH YIEYGAAVLV LLVCVFGLAA HWMACIWYSI
410 420 430 440 450
GDYEIFDEDT KTIRNNSWLY QLAMDIGTPY QFNGSGSGKW EGGPSKNSVY
460 470 480 490 500
ISSLYFTMTS LTSVGFGNIA PSTDIEKIFA VAIMMIGSLL YATIFGNVTT
510 520 530 540 550
IFQQMYANTN RYHEMLNSVR DFLKLYQVPK GLSERVMDYI VSTWSMSRGI
560 570 580 590 600
DTEKVLQICP KDMRADICVH LNRKVFKEHP AFRLASDGCL RALAMEFQTV
610 620 630 640 650
HCAPGDLIYH AGESVDSLCF VVSGSLEVIQ DDEVVAILGK GDVFGDVFWK
660 670 680 690 700
EATLAQSCAN VRALTYCDLH VIKRDALQKV LEFYTAFSHS FSRNLILTYN
710 720 730 740 750
LRKRIVFRKI SDVKREEEER MKRKNEAPLI LPPDHPVRRL FQRFRQQKEA
760 770 780 790 800
RLAAERGGRD LDDLDVEKGS VLTEHSHHGL AKASVVTVRE SPATPVAFPA
810 820 830 840 850
AAAPAGLDHA RLQAPGAEGL GPKAGGADCA KRKGWARFKD ACGQAEDWSK
860 870 880 890 900
VSKAESMETL PERTKAAGEA TLKKTDSCDS GITKSDLRLD NVGEARSPQD
910 920 930 940 950
RSPILAEVKH SFYPIPEQTL QAAVLEVKHE LKEDIKALST KMTSIEKQLS
960 970 980
EILRILTSRR SSQSPQELFE ISRPQSPESE RDIFGAS
Length:987
Mass (Da):110,918
Last modified:November 28, 2002 - v2
Checksum:i0EF9FB866297DC4F
GO
Isoform 1 (identifier: O18965-2) [UniParc]FASTAAdd to basket

Also known as: EAG1

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

Show »
Length:960
Mass (Da):108,092
Checksum:i86FCD3303A3E3B08
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei318 – 34427Missing in isoform 1. 1 PublicationVSP_000963Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13430 mRNA. Translation: CAA73842.1.
Y13431 mRNA. Translation: CAA73843.1.
RefSeqiNP_776797.1. NM_174372.2. [O18965-1]
UniGeneiBt.91775.

Genome annotation databases

GeneIDi281881.
KEGGibta:281881.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13430 mRNA. Translation: CAA73842.1.
Y13431 mRNA. Translation: CAA73843.1.
RefSeqiNP_776797.1. NM_174372.2. [O18965-1]
UniGeneiBt.91775.

3D structure databases

ProteinModelPortaliO18965.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO18965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281881.
KEGGibta:281881.

Organism-specific databases

CTDi3756.

Phylogenomic databases

HOVERGENiHBG101348.
InParanoidiO18965.
KOiK04904.

Family and domain databases

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

Publicationsi

  1. "Characterization of ether-a-go-go channels present in photoreceptors reveals similarity to IKx, a K current in rod inner segments."
    Frings S., Bruell N., Dzeja C., Angele A., Hagen V., Kaupp U.B., Baumann A.
    J. Gen. Physiol. 111:583-599(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Retina.

Entry informationi

Entry nameiKCNH1_BOVIN
AccessioniPrimary (citable) accession number: O18965
Secondary accession number(s): O18966
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 28, 2002
Last modified: June 8, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Extracellular magnesium ion concentrations up to 4 mM modulate channel activity by slowing down current activation in a reversible fashion.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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