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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi581 – 584cAMP2 Publications4
Nucleotide bindingi591 – 592cAMP2 Publications2
Nucleotide bindingi632 – 635cAMP2 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Potassium channel, Sodium channel, Voltage-gated channel
Biological processIon transport, Potassium transport, Sodium transport, Transport
LigandcAMP, cAMP-binding, Nucleotide-binding, Potassium, Sodium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1296061 HCN channels

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Hcn2
Synonyms:Bcng2, Hac1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1298210 Hcn2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 188CytoplasmicSequence analysisAdd BLAST188
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei189 – 209Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini210 – 213ExtracellularSequence analysis4
Transmembranei214 – 234Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini235 – 261CytoplasmicSequence analysisAdd BLAST27
Transmembranei262 – 282Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini283 – 290ExtracellularSequence analysis8
Transmembranei291 – 311Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini312 – 342CytoplasmicSequence analysisAdd BLAST31
Transmembranei343 – 363Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini364 – 386ExtracellularSequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei387 – 408Pore-forming; Name=Segment H5Sequence analysisAdd BLAST22
Topological domaini409 – 413ExtracellularSequence analysis5
Transmembranei414 – 434Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini435 – 863CytoplasmicSequence analysisAdd BLAST429

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi225D → N: Abolishes surface expression and channel activity. 1 Publication1
Mutagenesisi231D → N: Reduces surface expression and abolishes channel activity. 1 Publication1
Mutagenesisi267D → N: Reduces surface expression and abolishes channel activity. 1 Publication1
Mutagenesisi275D → N: Reduces surface expression and abolishes channel activity. 1 Publication1
Mutagenesisi291K → Q: Shifts voltage dependence of activation to more negative values. 1 Publication1
Mutagenesisi294R → Q: Shifts voltage dependence of activation to more negative values. 1 Publication1
Mutagenesisi297R → Q: Shifts voltage dependence of activation to more negative values. 1 Publication1
Mutagenesisi300R → Q: Shifts voltage dependence of activation to more negative values. 1 Publication1
Mutagenesisi303K → Q: Decreases current amplitude. 1 Publication1
Mutagenesisi306S → Q: Decreases current amplitude. 2 Publications1
Mutagenesisi309R → Q: Abolishes surface expression and channel activity. 1 Publication1
Mutagenesisi312R → Q: Reduces surface expression and decreases current amplitude. 1 Publication1
Mutagenesisi315R → Q: Reduces surface expression and abolishes channel activity. 1 Publication1
Mutagenesisi318R → Q: Reduces surface expression and disrupts channel closure. 2 Publications1
Mutagenesisi321H → E: Shifts voltage dependence of activation to more positive values and abolishes pH-sensitivity. 1 Publication1
Mutagenesisi321H → Q: Abolishes pH-sensitivity. 1 Publication1
Mutagenesisi321H → R: Abolishes pH-sensitivity. 1 Publication1
Mutagenesisi324E → Q: Disrupts channel closure. 1 Publication1
Mutagenesisi331Y → A: Disrupts channel closure. 1 Publication1
Mutagenesisi331Y → S: Disrupts channel closure. 1 Publication1
Mutagenesisi339R → Q: Disrupts channel closure. 1 Publication1
Mutagenesisi594S → R: Shifts channel activation to more negative voltage, slows channel opening and speeds up channel closure. Reduces sensitivity to activation by cAMP. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1250408

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
401

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000541121 – 863Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2Add BLAST863

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei119PhosphoserineCombined sources1
Modified residuei134PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi380N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei641Phosphoserine; by PKG/PRKG21 Publication1
Modified residuei726PhosphoserineBy similarity1
Modified residuei728Omega-N-methylarginineCombined sources1
Modified residuei743PhosphoserineCombined sources1
Modified residuei750PhosphoserineCombined sources1
Modified residuei757PhosphoserineCombined sources1
Modified residuei840PhosphoserineCombined sources1
Modified residuei842PhosphoserineCombined sources1
Modified residuei847PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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, Methylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O88703

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O88703

PRoteomics IDEntifications database

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PRIDEi
O88703

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O88703

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O88703

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O88703

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020331 Expressed in 164 organ(s), highest expression level in cardiac ventricle

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O88703 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
200253, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-142 HCN2 channel complex

Database of interacting proteins

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DIPi
DIP-29326N

Protein interaction database and analysis system

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IntActi
O88703, 7 interactors

Molecular INTeraction database

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MINTi
O88703

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000020581

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O88703

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1863
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O88703

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O88703

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O88703

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni131 – 182Involved in subunit assemblyAdd BLAST52

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi10 – 58Pro-richAdd BLAST49
Compositional biasi688 – 835Pro-richAdd BLAST148

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the potassium channel HCN family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0498 Eukaryota
ENOG410XPSE LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156523

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230717

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG039489

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O88703

KEGG Orthology (KO)

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KOi
K04955

Identification of Orthologs from Complete Genome Data

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OMAi
HQMSVGA

Database of Orthologous Groups

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OrthoDBi
EOG091G0JQU

Database for complete collections of gene phylogenies

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PhylomeDBi
O88703

TreeFam database of animal gene trees

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TreeFami
TF318250

Family and domain databases

Conserved Domains Database

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CDDi
cd00038 CAP_ED, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR018490 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

Pfam protein domain database

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Pfami
View protein in Pfam
PF00027 cNMP_binding, 1 hit
PF00520 Ion_trans, 1 hit
PF08412 Ion_trans_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01463 EAGCHANLFMLY

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00100 cNMP, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51206 SSF51206, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00888 CNMP_BINDING_1, 1 hit
PS50042 CNMP_BINDING_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i17CDC4DFF07AC039
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti486F → S in AAC40125 (PubMed:9630217).Curated1
Sequence conflicti642I → T in AAC40125 (PubMed:9630217).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AJ225122 mRNA Translation: CAA12406.1
AF064873 mRNA Translation: AAC40125.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS23986.1

NCBI Reference Sequences

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RefSeqi
NP_032252.1, NM_008226.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.12956

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000020581; ENSMUSP00000020581; ENSMUSG00000020331
ENSMUST00000099513; ENSMUSP00000097113; ENSMUSG00000020331

Database of genes from NCBI RefSeq genomes

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GeneIDi
15166

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:15166

UCSC genome browser

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UCSCi
uc007fzn.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
5JONX-ray2.04A/B494-640[»]
5KHGX-ray2.24A443-643[»]
5KHHX-ray1.77A443-643[»]
5KHIX-ray2.10A443-643[»]
5KHJX-ray2.01A/B443-643[»]
5KHKX-ray2.07A443-643[»]
ProteinModelPortaliO88703
SMRiO88703
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200253, 3 interactors
ComplexPortaliCPX-142 HCN2 channel complex
DIPiDIP-29326N
IntActiO88703, 7 interactors
MINTiO88703
STRINGi10090.ENSMUSP00000020581

Chemistry databases

BindingDBiO88703
ChEMBLiCHEMBL1250408
GuidetoPHARMACOLOGYi401

PTM databases

iPTMnetiO88703
PhosphoSitePlusiO88703
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

Comparative Toxicogenomics Database

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CTDi
610
MGIiMGI:1298210 Hcn2

Phylogenomic databases

eggNOGiKOG0498 Eukaryota
ENOG410XPSE LUCA
GeneTreeiENSGT00940000156523
HOGENOMiHOG000230717
HOVERGENiHBG039489
InParanoidiO88703
KOiK04955
OMAiHQMSVGA
OrthoDBiEOG091G0JQU
PhylomeDBiO88703
TreeFamiTF318250

Enzyme and pathway databases

ReactomeiR-MMU-1296061 HCN channels

Miscellaneous databases

EvolutionaryTraceiO88703

Protein Ontology

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PROi
PR:O88703

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020331 Expressed in 164 organ(s), highest expression level in cardiac ventricle
GenevisibleiO88703 MM

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR018490 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
PfamiView protein in Pfam
PF00027 cNMP_binding, 1 hit
PF00520 Ion_trans, 1 hit
PF08412 Ion_trans_N, 1 hit
PRINTSiPR01463 EAGCHANLFMLY
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SUPFAMiSSF51206 SSF51206, 1 hit
PROSITEiView protein in PROSITE
PS00888 CNMP_BINDING_1, 1 hit
PS50042 CNMP_BINDING_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHCN2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O88703
Secondary accession number(s): O70506
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: November 1, 1998
Last modified: December 5, 2018
This is version 167 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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