Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 175 (17 Jun 2020)
Sequence version 2 (30 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Neuronal acetylcholine receptor subunit beta-2

Gene

Chrnb2

Organism
Rattus norvegicus (Rat)
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

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodiun ions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei83Key residue that may interfere with effective access of the conotoxin BuIA to the channel binding site1 Publication1
Sitei118Key residue that may play an important stabilizing role for the interaction with alpha-conotoxins PnIA, GID and MII, allowing them to bind deep into the nAChR cleft1 Publication1
Sitei135Key residue for a rapid dissociation (K(off)) from the conotoxin BuIA1 Publication1
Sitei143Key residue for a rapid dissociation (K(off)) from the conotoxin BuIA1 Publication1

<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, Receptor
Biological processIon transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-629587 Highly sodium permeable acetylcholine nicotinic receptors
R-RNO-629594 Highly calcium permeable postsynaptic nicotinic acetylcholine receptors
R-RNO-629597 Highly calcium permeable nicotinic acetylcholine receptors

<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%5Fand%5Ftaxonomy%5Fsection">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:
Neuronal acetylcholine receptor subunit beta-2
Alternative name(s):
Neuronal acetylcholine receptor non-alpha-1 chain
Short name:
N-alpha 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Chrnb2
Synonyms:Acrb2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 2

Organism-specific databases

Rat genome database

More...
RGDi
2350 Chrnb2

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 domaini25 – 237ExtracellularSequence analysisAdd BLAST213
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Topological domaini259 – 266CytoplasmicSequence analysis8
Transmembranei267 – 287HelicalSequence analysisAdd BLAST21
Topological domaini288 – 299ExtracellularSequence analysisAdd BLAST12
Transmembranei300 – 320HelicalSequence analysisAdd BLAST21
Topological domaini321 – 458CytoplasmicSequence analysisAdd BLAST138
Transmembranei459 – 479HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi83T → D: 9-fold increase in affinity to the conotoxin BuIA (15-fold decrease in K(off)). 1 Publication1
Mutagenesisi83T → G: 12-fold increase in affinity to the conotoxin BuIA (11-fold decrease in K(off)). 1 Publication1
Mutagenesisi83T → K: 20-fold increase in affinity to the conotoxin BuIA (37-fold decrease in K(off)); 2-fold decrease in affinity to the conotoxin MII (no change in K(off), but 2-fold decrease in K(on)). 1 Publication1
Mutagenesisi83T → S: 19-fold increase in affinity to the conotoxin BuIA (7-fold decrease in K(off)). 1 Publication1
Mutagenesisi83T → V: 3-fold increase in affinity to the conotoxin BuIA (2-fold decrease in K(off)). 1 Publication1
Mutagenesisi118L → Q: 40-fold, 165-fold, and 300-fold decrease in inhibition of alpha-3-beta-2(L118Q) nAChR by alpha-conotoxins PnIA, GID and MII, respectively. 1 Publication1
Mutagenesisi135V → A: Very small decrease or no change in inhibition of alpha-3-beta-2(V135A) nAChR by alpha-conotoxins PnIA, GID and MII. 1 Publication1
Mutagenesisi135V → G: No change in inhibition of alpha-3-beta-2(V135G) nAChR by alpha-conotoxins GID and MII. 4.4-fold decrease in inhibition of alpha-3-beta-2(V135G) nAChR by alpha-conotoxins PnIA. 1 Publication1
Mutagenesisi135V → I: 8.3-fold decrease in affinity to the conotoxin BuIA (4-fold increase in K(off) and a 2-fold decrease in K(on)). 1 Publication1
Mutagenesisi143F → A: No change in inhibition of alpha-3-beta-2(F143A) nAChR by alpha-conotoxins PnIA, GID and MII. 12-fold and 6.6-fold increase in inhibition of alpha-4-beta-2(F143A) nAChR by alpha-conotoxins GID and MII, respectively, but no change in inhibition of the same receptor by alpha-conotoxin PnIA. 1 Publication1
Mutagenesisi143F → Q: 6.6-fold increase in affinity to the conotoxin BuIA (7-fold decrease in K(off)). 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1907587
CHEMBL1907592
CHEMBL1907596
CHEMBL3137275

DrugCentral

More...
DrugCentrali
P12390

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000038125 – 500Neuronal acetylcholine receptor subunit beta-2Add BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi50N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi154 ↔ 168By similarity
Glycosylationi167N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...
PaxDbi
P12390

PRoteomics IDEntifications database

More...
PRIDEi
P12390

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P12390

<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

Expressed in most regions of the CNS.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000020778 Expressed in brain and 6 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P12390 RN

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Neuronal AChR is composed of two different types of subunits: alpha and beta. Beta-2 subunit can be combined to alpha-2, alpha-3 or alpha-4 to give rise to functional receptors, complexes with beta-2 may be heteropentamers. Alpha-2/4:beta-2 nAChR complexes are proposed to exist in two subtypes: LS (low agonist sensitivity) with a (alpha-2/4)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2/4)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding.

Interacts with RIC3; which is required for proper folding and assembly.

Interacts with LYPD6. The heteropentamer alpha3-beta-2 interacts with alpha-conotoxins BuIA, MII, ImI, ImII, PnIA and GID (PubMed:15609996, PubMed:15929983, PubMed:16964981). The heteropentamer alpha-4-beta-2 interacts with the alpha-conotoxins PnIA, GID and MII (PubMed:15929983).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-170 Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2
CPX-171 Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2
CPX-178 Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2
CPX-190 Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2
CPX-191 Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2
CPX-203 Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3
CPX-215 Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2
CPX-237 Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P12390

Protein interaction database and analysis system

More...
IntActi
P12390, 6 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000028200

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P12390

<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

3D structure databases

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

More...
SMRi
P12390

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

<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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3645 Eukaryota
ENOG410XQGR LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158417

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_018074_1_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P12390

KEGG Orthology (KO)

More...
KOi
K04813

Identification of Orthologs from Complete Genome Data

More...
OMAi
TWIPEEF

Database of Orthologous Groups

More...
OrthoDBi
381858at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P12390

TreeFam database of animal gene trees

More...
TreeFami
TF315605

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.70.170.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032932 CHRNB2
IPR006202 Neur_chan_lig-bd
IPR036734 Neur_chan_lig-bd_sf
IPR006201 Neur_channel
IPR036719 Neuro-gated_channel_TM_sf
IPR006029 Neurotrans-gated_channel_TM
IPR018000 Neurotransmitter_ion_chnl_CS
IPR002394 Nicotinic_acetylcholine_rcpt

The PANTHER Classification System

More...
PANTHERi
PTHR18945 PTHR18945, 1 hit
PTHR18945:SF80 PTHR18945:SF80, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02931 Neur_chan_LBD, 1 hit
PF02932 Neur_chan_memb, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00254 NICOTINICR
PR00252 NRIONCHANNEL

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63712 SSF63712, 1 hit
SSF90112 SSF90112, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00860 LIC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00236 NEUROTR_ION_CHANNEL, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P12390-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGHSNSMAL FSFSLLWLCS GVLGTDTEER LVEHLLDPSR YNKLIRPATN
60 70 80 90 100
GSELVTVQLM VSLAQLISVH EREQIMTTNV WLTQEWEDYR LTWKPEDFDN
110 120 130 140 150
MKKVRLPSKH IWLPDVVLYN NADGMYEVSF YSNAVVSYDG SIFWLPPAIY
160 170 180 190 200
KSACKIEVKH FPFDQQNCTM KFRSWTYDRT EIDLVLKSDV ASLDDFTPSG
210 220 230 240 250
EWDIIALPGR RNENPDDSTY VDITYDFIIR RKPLFYTINL IIPCVLITSL
260 270 280 290 300
AILVFYLPSD CGEKMTLCIS VLLALTVFLL LISKIVPPTS LDVPLVGKYL
310 320 330 340 350
MFTMVLVTFS IVTSVCVLNV HHRSPTTHTM APWVKVVFLE KLPTLLFLQQ
360 370 380 390 400
PRHRCARQRL RLRRRQRERE GAGALFFREG PAADPCTCFV NPASVQGLAG
410 420 430 440 450
AFRAEPTAAG PGRSVGPCSC GLREAVDGVR FIADHMRSED DDQSVREDWK
460 470 480 490 500
YVAMVIDRLF LWIFVFVCVF GTVGMFLQPL FQNYTATTFL HPDHSAPSSK
Length:500
Mass (Da):56,909
Last modified:May 30, 2000 - v2
<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:i54C007A48225931C
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L31622 mRNA Translation: AAC78724.1
AY574258 mRNA Translation: AAS90354.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JH0174

NCBI Reference Sequences

More...
RefSeqi
NP_062170.1, NM_019297.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000028200; ENSRNOP00000028200; ENSRNOG00000020778

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
54239

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:54239

UCSC genome browser

More...
UCSCi
RGD:2350 rat

<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
L31622 mRNA Translation: AAC78724.1
AY574258 mRNA Translation: AAS90354.1
PIRiJH0174
RefSeqiNP_062170.1, NM_019297.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OLEmodel-B/D/E27-233[»]
1OLFmodel-B/D/E27-233[»]
SMRiP12390
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-170 Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2
CPX-171 Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2
CPX-178 Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2
CPX-190 Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2
CPX-191 Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2
CPX-203 Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3
CPX-215 Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2
CPX-237 Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2
CORUMiP12390
IntActiP12390, 6 interactors
STRINGi10116.ENSRNOP00000028200

Chemistry databases

BindingDBiP12390
ChEMBLiCHEMBL1907587
CHEMBL1907592
CHEMBL1907596
CHEMBL3137275
DrugCentraliP12390

PTM databases

SwissPalmiP12390

Proteomic databases

PaxDbiP12390
PRIDEiP12390

Genome annotation databases

EnsembliENSRNOT00000028200; ENSRNOP00000028200; ENSRNOG00000020778
GeneIDi54239
KEGGirno:54239
UCSCiRGD:2350 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1141
RGDi2350 Chrnb2

Phylogenomic databases

eggNOGiKOG3645 Eukaryota
ENOG410XQGR LUCA
GeneTreeiENSGT00940000158417
HOGENOMiCLU_018074_1_3_1
InParanoidiP12390
KOiK04813
OMAiTWIPEEF
OrthoDBi381858at2759
PhylomeDBiP12390
TreeFamiTF315605

Enzyme and pathway databases

ReactomeiR-RNO-629587 Highly sodium permeable acetylcholine nicotinic receptors
R-RNO-629594 Highly calcium permeable postsynaptic nicotinic acetylcholine receptors
R-RNO-629597 Highly calcium permeable nicotinic acetylcholine receptors

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P12390

Gene expression databases

BgeeiENSRNOG00000020778 Expressed in brain and 6 other tissues
GenevisibleiP12390 RN

Family and domain databases

Gene3Di2.70.170.10, 1 hit
InterProiView protein in InterPro
IPR032932 CHRNB2
IPR006202 Neur_chan_lig-bd
IPR036734 Neur_chan_lig-bd_sf
IPR006201 Neur_channel
IPR036719 Neuro-gated_channel_TM_sf
IPR006029 Neurotrans-gated_channel_TM
IPR018000 Neurotransmitter_ion_chnl_CS
IPR002394 Nicotinic_acetylcholine_rcpt
PANTHERiPTHR18945 PTHR18945, 1 hit
PTHR18945:SF80 PTHR18945:SF80, 1 hit
PfamiView protein in Pfam
PF02931 Neur_chan_LBD, 1 hit
PF02932 Neur_chan_memb, 1 hit
PRINTSiPR00254 NICOTINICR
PR00252 NRIONCHANNEL
SUPFAMiSSF63712 SSF63712, 1 hit
SSF90112 SSF90112, 1 hit
TIGRFAMsiTIGR00860 LIC, 1 hit
PROSITEiView protein in PROSITE
PS00236 NEUROTR_ION_CHANNEL, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiACHB2_RAT
<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: P12390
Secondary accession number(s): Q53YK1
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 30, 2000
Last modified: June 17, 2020
This is version 175 of the entry and version 2 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again