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Protein

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2

Gene

Hcn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current.8 Publications

Enzyme regulationi

Activated by cAMP, and at 10-100 times higher concentrations, also by cGMP. cAMP binding causes a conformation change that leads to the assembly of an active tetramer and channel opening. Channel activity is modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi581 – 5844cAMP2 Publications
Nucleotide bindingi591 – 5922cAMP2 Publications
Nucleotide bindingi632 – 6354cAMP2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Potassium channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Sodium transport, Transport

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding, Potassium, Sodium

Enzyme and pathway databases

ReactomeiR-MMU-1296061. HCN channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
Alternative name(s):
Brain cyclic nucleotide-gated channel 2
Short name:
BCNG-2
Hyperpolarization-activated cation channel 1
Short name:
HAC-1
Gene namesi
Name:Hcn2
Synonyms:Bcng2, Hac1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1298210. Hcn2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 188188CytoplasmicSequence analysisAdd
BLAST
Transmembranei189 – 20921Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini210 – 2134ExtracellularSequence analysis
Transmembranei214 – 23421Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini235 – 26127CytoplasmicSequence analysisAdd
BLAST
Transmembranei262 – 28221Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini283 – 2908ExtracellularSequence analysis
Transmembranei291 – 31121Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini312 – 34231CytoplasmicSequence analysisAdd
BLAST
Transmembranei343 – 36321Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini364 – 38623ExtracellularSequence analysisAdd
BLAST
Intramembranei387 – 40822Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Topological domaini409 – 4135ExtracellularSequence analysis
Transmembranei414 – 43421Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini435 – 863429CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi225 – 2251D → N: Abolishes surface expression and channel activity. 1 Publication
Mutagenesisi231 – 2311D → N: Reduces surface expression and abolishes channel activity. 1 Publication
Mutagenesisi267 – 2671D → N: Reduces surface expression and abolishes channel activity. 1 Publication
Mutagenesisi275 – 2751D → N: Reduces surface expression and abolishes channel activity. 1 Publication
Mutagenesisi291 – 2911K → Q: Shifts voltage dependence of activation to more negative values. 1 Publication
Mutagenesisi294 – 2941R → Q: Shifts voltage dependence of activation to more negative values. 1 Publication
Mutagenesisi297 – 2971R → Q: Shifts voltage dependence of activation to more negative values. 1 Publication
Mutagenesisi300 – 3001R → Q: Shifts voltage dependence of activation to more negative values. 1 Publication
Mutagenesisi303 – 3031K → Q: Decreases current amplitude. 1 Publication
Mutagenesisi306 – 3061S → Q: Decreases current amplitude. 2 Publications
Mutagenesisi309 – 3091R → Q: Abolishes surface expression and channel activity. 1 Publication
Mutagenesisi312 – 3121R → Q: Reduces surface expression and decreases current amplitude. 1 Publication
Mutagenesisi315 – 3151R → Q: Reduces surface expression and abolishes channel activity. 1 Publication
Mutagenesisi318 – 3181R → Q: Reduces surface expression and disrupts channel closure. 2 Publications
Mutagenesisi321 – 3211H → E: Shifts voltage dependence of activation to more positive values and abolishes pH-sensitivity. 1 Publication
Mutagenesisi321 – 3211H → Q: Abolishes pH-sensitivity. 1 Publication
Mutagenesisi321 – 3211H → R: Abolishes pH-sensitivity. 1 Publication
Mutagenesisi324 – 3241E → Q: Disrupts channel closure. 1 Publication
Mutagenesisi331 – 3311Y → A: Disrupts channel closure. 1 Publication
Mutagenesisi331 – 3311Y → S: Disrupts channel closure. 1 Publication
Mutagenesisi339 – 3391R → Q: Disrupts channel closure. 1 Publication
Mutagenesisi594 – 5941S → R: Shifts channel activation to more negative voltage, slows channel opening and speeds up channel closure. Reduces sensitivity to activation by cAMP. 1 Publication

Chemistry

ChEMBLiCHEMBL1250408.
GuidetoPHARMACOLOGYi401.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 863863Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2PRO_0000054112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191PhosphoserineCombined sources
Modified residuei134 – 1341PhosphoserineBy similarity
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence analysis
Modified residuei641 – 6411Phosphoserine; by PKG/PRKG21 Publication
Modified residuei726 – 7261PhosphoserineBy similarity
Modified residuei743 – 7431PhosphoserineCombined sources
Modified residuei750 – 7501PhosphoserineCombined sources
Modified residuei757 – 7571PhosphoserineCombined sources
Modified residuei840 – 8401PhosphoserineCombined sources
Modified residuei842 – 8421PhosphoserineCombined sources
Modified residuei847 – 8471PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation at Ser-641 by PRKG2 shifts the voltage-dependence to more negative voltages, hence counteracting the stimulatory effect of cGMP on gating.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO88703.
PaxDbiO88703.
PRIDEiO88703.

PTM databases

iPTMnetiO88703.
PhosphoSiteiO88703.
SwissPalmiO88703.

Expressioni

Tissue specificityi

Highly expressed in brain. Detected at low levels in heart, in ventricle, atrium and in sinoatrial node (SAN).1 Publication

Gene expression databases

BgeeiO88703.
GenevisibleiO88703. MM.

Interactioni

Subunit structurei

Homotetramer. Heterotetramer with HCN1. The potassium channel is composed of a homo- or heterotetrameric complex of pore-forming subunits. Forms an obligate 4:4 complex with accessory subunit PEX5L. Interacts with KCNE2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SRCP005235EBI-771231,EBI-848039From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200253. 1 interaction.
DIPiDIP-29326N.
IntActiO88703. 3 interactions.
MINTiMINT-155013.
STRINGi10090.ENSMUSP00000020581.

Chemistry

BindingDBiO88703.

Structurei

Secondary structure

1
863
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi444 – 46219Combined sources
Helixi467 – 48115Combined sources
Helixi488 – 4947Combined sources
Helixi497 – 50711Combined sources
Helixi509 – 5135Combined sources
Helixi516 – 5194Combined sources
Helixi523 – 53210Combined sources
Beta strandi534 – 5385Combined sources
Beta strandi543 – 5453Combined sources
Beta strandi553 – 5597Combined sources
Beta strandi561 – 5655Combined sources
Beta strandi567 – 5693Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi579 – 5813Combined sources
Helixi582 – 5876Combined sources
Beta strandi592 – 5998Combined sources
Beta strandi601 – 6077Combined sources
Helixi608 – 61710Combined sources
Helixi619 – 6213Combined sources
Helixi622 – 63514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3EX-ray1.90A/B443-645[»]
1Q43X-ray2.00A/B443-645[»]
1Q5OX-ray2.30A443-645[»]
2Q0AX-ray2.25A/B443-640[»]
3BPZX-ray1.65A/B/C/D443-640[»]
3ETQX-ray1.90A/B443-640[»]
3FFQX-ray2.40A/B443-640[»]
4EQFX-ray3.00B857-863[»]
ProteinModelPortaliO88703.
SMRiO88703. Positions 443-677.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88703.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 18252Involved in subunit assemblyAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 5849Pro-richAdd
BLAST
Compositional biasi688 – 835148Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the potassium channel HCN family.Curated
Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000230717.
HOVERGENiHBG039489.
InParanoidiO88703.
KOiK04955.
OMAiAMSFCPP.
OrthoDBiEOG7VMP6X.
PhylomeDBiO88703.
TreeFamiTF318250.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR013621. Ion_trans_N.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08412. Ion_trans_N. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88703-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDARGGGGRP GDSPGTTPAP GPPPPPPPPA PPQPQPPPAP PPNPTTPSHP
60 70 80 90 100
ESADEPGPRA RLCSRDSACT PGAAKGGANG ECGRGEPQCS PEGPARGPKV
110 120 130 140 150
SFSCRGAASG PSAAEEAGSE EAGPAGEPRG SQASFLQRQF GALLQPGVNK
160 170 180 190 200
FSLRMFGSQK AVEREQERVK SAGAWIIHPY SDFRFYWDFT MLLFMVGNLI
210 220 230 240 250
IIPVGITFFK DETTAPWIVF NVVSDTFFLM DLVLNFRTGI VIEDNTEIIL
260 270 280 290 300
DPEKIKKKYL RTWFVVDFVS SIPVDYIFLI VEKGIDSEVY KTARALRIVR
310 320 330 340 350
FTKILSLLRL LRLSRLIRYI HQWEEIFHMT YDLASAVMRI CNLISMMLLL
360 370 380 390 400
CHWDGCLQFL VPMLQDFPSD CWVSINNMVN HSWSELYSFA LFKAMSHMLC
410 420 430 440 450
IGYGRQAPES MTDIWLTMLS MIVGATCYAM FIGHATALIQ SLDSSRRQYQ
460 470 480 490 500
EKYKQVEQYM SFHKLPADFR QKIHDYYEHR YQGKMFDEDS ILGELNGPLR
510 520 530 540 550
EEIVNFNCRK LVASMPLFAN ADPNFVTAML TKLKFEVFQP GDYIIREGTI
560 570 580 590 600
GKKMYFIQHG VVSVLTKGNK EMKLSDGSYF GEICLLTRGR RTASVRADTY
610 620 630 640 650
CRLYSLSVDN FNEVLEEYPM MRRAFETVAI DRLDRIGKKN SILLHKVQHD
660 670 680 690 700
LSSGVFNNQE NAIIQEIVKY DREMVQQAEL GQRVGLFPPP PPPQVTSAIA
710 720 730 740 750
TLQQAVAMSF CPQVARPLVG PLALGSPRLV RRAPPGPLPP AASPGPPAAS
760 770 780 790 800
PPAAPSSPRA PRTSPYGVPG SPATRVGPAL PARRLSRASR PLSASQPSLP
810 820 830 840 850
HGVPAPSPAA SARPASSSTP RLGPAPTART AAPSPDRRDS ASPGAASGLD
860
PLDSARSRLS SNL
Length:863
Mass (Da):94,722
Last modified:November 1, 1998 - v1
Checksum:i17CDC4DFF07AC039
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti486 – 4861F → S in AAC40125 (PubMed:9630217).Curated
Sequence conflicti642 – 6421I → T in AAC40125 (PubMed:9630217).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ225122 mRNA. Translation: CAA12406.1.
AF064873 mRNA. Translation: AAC40125.1.
CCDSiCCDS23986.1.
RefSeqiNP_032252.1. NM_008226.2.
UniGeneiMm.12956.

Genome annotation databases

EnsembliENSMUST00000020581; ENSMUSP00000020581; ENSMUSG00000020331.
ENSMUST00000099513; ENSMUSP00000097113; ENSMUSG00000020331.
GeneIDi15166.
KEGGimmu:15166.
UCSCiuc007fzn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ225122 mRNA. Translation: CAA12406.1.
AF064873 mRNA. Translation: AAC40125.1.
CCDSiCCDS23986.1.
RefSeqiNP_032252.1. NM_008226.2.
UniGeneiMm.12956.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3EX-ray1.90A/B443-645[»]
1Q43X-ray2.00A/B443-645[»]
1Q5OX-ray2.30A443-645[»]
2Q0AX-ray2.25A/B443-640[»]
3BPZX-ray1.65A/B/C/D443-640[»]
3ETQX-ray1.90A/B443-640[»]
3FFQX-ray2.40A/B443-640[»]
4EQFX-ray3.00B857-863[»]
ProteinModelPortaliO88703.
SMRiO88703. Positions 443-677.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200253. 1 interaction.
DIPiDIP-29326N.
IntActiO88703. 3 interactions.
MINTiMINT-155013.
STRINGi10090.ENSMUSP00000020581.

Chemistry

BindingDBiO88703.
ChEMBLiCHEMBL1250408.
GuidetoPHARMACOLOGYi401.

PTM databases

iPTMnetiO88703.
PhosphoSiteiO88703.
SwissPalmiO88703.

Proteomic databases

MaxQBiO88703.
PaxDbiO88703.
PRIDEiO88703.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020581; ENSMUSP00000020581; ENSMUSG00000020331.
ENSMUST00000099513; ENSMUSP00000097113; ENSMUSG00000020331.
GeneIDi15166.
KEGGimmu:15166.
UCSCiuc007fzn.1. mouse.

Organism-specific databases

CTDi610.
MGIiMGI:1298210. Hcn2.

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000230717.
HOVERGENiHBG039489.
InParanoidiO88703.
KOiK04955.
OMAiAMSFCPP.
OrthoDBiEOG7VMP6X.
PhylomeDBiO88703.
TreeFamiTF318250.

Enzyme and pathway databases

ReactomeiR-MMU-1296061. HCN channels.

Miscellaneous databases

EvolutionaryTraceiO88703.
PROiO88703.
SOURCEiSearch...

Gene expression databases

BgeeiO88703.
GenevisibleiO88703. MM.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR013621. Ion_trans_N.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08412. Ion_trans_N. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of hyperpolarization-activated cation channels."
    Ludwig A., Zong X., Jeglitsch M., Hofmann F., Biel M.
    Nature 393:587-591(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: BALB/cJ.
  2. "Identification of a gene encoding a hyperpolarization-activated 'pacemaker' channel of brain."
    Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R., Siegelbaum S.A., Tibbs G.R.
    Cell 93:717-729(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-653, TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Functional roles of charged residues in the putative voltage sensor of the HCN2 pacemaker channel."
    Chen J., Mitcheson J.S., Lin M., Sanguinetti M.C.
    J. Biol. Chem. 275:36465-36471(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-225; ASP-231; ASP-267; ASP-275; LYS-291; ARG-294; ARG-297; ARG-300; LYS-303; SER-306; ARG-309; ARG-312; ARG-315 AND ARG-318.
  4. "MinK-related peptide 1: a beta subunit for the HCN ion channel subunit family enhances expression and speeds activation."
    Yu H., Wu J., Potapova I., Wymore R.T., Holmes B., Zuckerman J., Pan Z., Wang H., Shi W., Robinson R.B., El-Maghrabi M.R., Benjamin W., Dixon J.E., McKinnon D., Cohen I.S., Wymore R.
    Circ. Res. 88:E84-E87(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNE2.
  5. "A single histidine residue determines the pH sensitivity of the pacemaker channel HCN2."
    Zong X., Stieber J., Ludwig A., Hofmann F., Biel M.
    J. Biol. Chem. 276:6313-6319(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-321.
  6. "The S4-S5 linker couples voltage sensing and activation of pacemaker channels."
    Chen J., Mitcheson J.S., Tristani-Firouzi M., Lin M., Sanguinetti M.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:11277-11282(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-318; GLU-324; TYR-331 AND ARG-339.
  7. Cited for: FUNCTION, MUTAGENESIS OF SER-306.
  8. "Different roles for the cyclic nucleotide binding domain and amino terminus in assembly and expression of hyperpolarization-activated, cyclic nucleotide-gated channels."
    Proenza C., Tran N., Angoli D., Zahynacz K., Balcar P., Accili E.A.
    J. Biol. Chem. 277:29634-29642(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCN1.
  9. "A conserved domain in the NH2 terminus important for assembly and functional expression of pacemaker channels."
    Tran N., Proenza C., Macri V., Petigara F., Sloan E., Samler S., Accili E.A.
    J. Biol. Chem. 277:43588-43592(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-743; SER-750; SER-757; SER-840; SER-842 AND SER-847, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  11. "The cGMP-dependent protein kinase II Is an inhibitory modulator of the hyperpolarization-activated HCN2 channel."
    Hammelmann V., Zong X., Hofmann F., Michalakis S., Biel M.
    PLoS ONE 6:E17078-E17078(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-641.
  12. "Local and global interpretations of a disease-causing mutation near the ligand entry path in hyperpolarization-activated cAMP-gated channel."
    Xu X., Marni F., Wu S., Su Z., Musayev F., Shrestha S., Xie C., Gao W., Liu Q., Zhou L.
    Structure 20:2116-2123(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-594.
  13. "Structural basis for modulation and agonist specificity of HCN pacemaker channels."
    Zagotta W.N., Olivier N.B., Black K.D., Young E.C., Olson R., Gouaux E.
    Nature 425:200-205(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 443-643 IN COMPLEXES WITH CAMP AND CGMP, FUNCTION, ENZYME REGULATION, NUCLEOTIDE-BINDING, SUBUNIT.
  14. "Structure and rearrangements in the carboxy-terminal region of SpIH channels."
    Flynn G.E., Black K.D., Islas L.D., Sankaran B., Zagotta W.N.
    Structure 15:671-682(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 443-640, FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, NUCEOTIDE-BINDING.
  15. "C-terminal movement during gating in cyclic nucleotide-modulated channels."
    Craven K.B., Olivier N.B., Zagotta W.N.
    J. Biol. Chem. 283:14728-14738(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 443-640 IN COMPLEX WITH CAMP, SUBUNIT, NUCLEOTIDE-BINDING.
  16. "Mapping the structure and conformational movements of proteins with transition metal ion FRET."
    Taraska J.W., Puljung M.C., Olivier N.B., Flynn G.E., Zagotta W.N.
    Nat. Methods 6:532-537(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 443-640 IN COMPLEX WITH CAMP, NUCLEOTIDE-BINDING.
  17. "Structure and stoichiometry of an accessory subunit TRIP8b interaction with hyperpolarization-activated cyclic nucleotide-gated channels."
    Bankston J.R., Camp S.S., DiMaio F., Lewis A.S., Chetkovich D.M., Zagotta W.N.
    Proc. Natl. Acad. Sci. U.S.A. 109:7899-7904(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 857-863 IN COMPLEX WITH PEX5L, SUBUNIT.

Entry informationi

Entry nameiHCN2_MOUSE
AccessioniPrimary (citable) accession number: O88703
Secondary accession number(s): O70506
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.