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P17787 (ACHB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal acetylcholine receptor subunit beta-2
Gene names
Name:CHRNB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Subunit structure

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. Interacts with RIC3; which is required for proper folding and assembly. Ref.7 Ref.9

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.

Involvement in disease

Epilepsy, nocturnal frontal lobe, 3 (ENFL3) [MIM:605375]: An autosomal dominant focal epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-2/CHRNB2 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Epilepsy
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

action potential

Inferred from electronic annotation. Source: Ensembl

associative learning

Inferred from sequence or structural similarity. Source: UniProtKB

behavioral response to nicotine

Inferred from mutant phenotype PubMed 17559419. Source: UniProtKB

calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system projection neuron axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cognition

Inferred from mutant phenotype PubMed 17559419. Source: UniProtKB

conditioned taste aversion

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement PubMed 20438829. Source: GOC

ion transport

Non-traceable author statement Ref.2. Source: UniProtKB

lateral geniculate nucleus development

Inferred from sequence or structural similarity. Source: UniProtKB

learning

Inferred from mutant phenotype PubMed 15964197. Source: UniProtKB

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

membrane depolarization

Inferred from sequence or structural similarity. Source: UniProtKB

memory

Inferred from mutant phenotype PubMed 15964197. Source: UniProtKB

negative regulation of action potential

Inferred from sequence or structural similarity. Source: UniProtKB

neurological system process

Inferred from mutant phenotype PubMed 17900292. Source: UniProtKB

optic nerve morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of B cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dopamine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of circadian sleep/wake cycle, REM sleep

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from electronic annotation. Source: Ensembl

regulation of dendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dopamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dopamine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synaptic transmission, dopaminergic

Inferred from sequence or structural similarity. Source: UniProtKB

response to cocaine

Inferred from sequence or structural similarity. Source: UniProtKB

response to ethanol

Inferred from sequence or structural similarity. Source: UniProtKB

response to hypoxia

Inferred from direct assay PubMed 12189247. Source: UniProtKB

response to nicotine

Inferred from direct assay PubMed 12189247. Source: UniProtKB

sensory perception of pain

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from direct assay Ref.2. Source: UniProtKB

smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

social behavior

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission involved in micturition

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission, cholinergic

Inferred from sequence or structural similarity. Source: UniProtKB

vestibulocochlear nerve development

Inferred from sequence or structural similarity. Source: UniProtKB

visual learning

Inferred from mutant phenotype PubMed 15964197. Source: UniProtKB

visual perception

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentacetylcholine-gated channel complex

Inferred from direct assay Ref.2. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholine binding

Inferred from mutant phenotype PubMed 15964197. Source: UniProtKB

acetylcholine receptor activity

Inferred from direct assay Ref.2. Source: UniProtKB

acetylcholine-activated cation-selective channel activity

Inferred from direct assay Ref.2. Source: UniProtKB

drug binding

Inferred from electronic annotation. Source: Ensembl

ligand-gated ion channel activity

Traceable author statement PubMed 20438829. Source: DFLAT

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 502477Neuronal acetylcholine receptor subunit beta-2
PRO_0000000379

Regions

Topological domain26 – 233208Extracellular Potential
Transmembrane234 – 25825Helical; Potential
Topological domain259 – 2657Cytoplasmic Potential
Transmembrane266 – 28419Helical; Potential
Topological domain285 – 29915Extracellular Potential
Transmembrane300 – 32122Helical; Potential
Topological domain322 – 458137Cytoplasmic Potential
Transmembrane459 – 47820Helical; Potential

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Disulfide bond155 ↔ 169 By similarity

Natural variations

Natural variant2871V → L in ENFL3. Ref.10
VAR_012714
Natural variant2871V → M in ENFL3; approximately 10-fold increase in acetylcholine sensitivity. Ref.11
VAR_012715
Natural variant3971Q → H. Ref.12
Corresponds to variant rs55685423 [ dbSNP | Ensembl ].
VAR_021564

Experimental info

Sequence conflict261T → A in CAA05108. Ref.4
Sequence conflict4261E → A in CAA05108. Ref.4
Sequence conflict4461S → SVR in CAA05108. Ref.4

Secondary structure

................ 502
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17787 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 7EEDEF6ADFDC9F23

FASTA50257,019
        10         20         30         40         50         60 
MARRCGPVAL LLGFGLLRLC SGVWGTDTEE RLVEHLLDPS RYNKLIRPAT NGSELVTVQL 

        70         80         90        100        110        120 
MVSLAQLISV HEREQIMTTN VWLTQEWEDY RLTWKPEEFD NMKKVRLPSK HIWLPDVVLY 

       130        140        150        160        170        180 
NNADGMYEVS FYSNAVVSYD GSIFWLPPAI YKSACKIEVK HFPFDQQNCT MKFRSWTYDR 

       190        200        210        220        230        240 
TEIDLVLKSE VASLDDFTPS GEWDIVALPG RRNENPDDST YVDITYDFII RRKPLFYTIN 

       250        260        270        280        290        300 
LIIPCVLITS LAILVFYLPS DCGEKMTLCI SVLLALTVFL LLISKIVPPT SLDVPLVGKY 

       310        320        330        340        350        360 
LMFTMVLVTF SIVTSVCVLN VHHRSPTTHT MAPWVKVVFL EKLPALLFMQ QPRHHCARQR 

       370        380        390        400        410        420 
LRLRRRQRER EGAGALFFRE APGADSCTCF VNRASVQGLA GAFGAEPAPV AGPGRSGEPC 

       430        440        450        460        470        480 
GCGLREAVDG VRFIADHMRS EDDDQSVSED WKYVAMVIDR LFLWIFVFVC VFGTIGMFLQ 

       490        500 
PLFQNYTTTT FLHSDHSAPS SK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the human nicotinic acetylcholine receptor beta 2 subunit gene."
Anand R., Lindstrom J.
Nucleic Acids Res. 18:4272-4272(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits."
Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E., Johnson E.C., Velicelebi G., Harpold M.M.
J. Mol. Neurosci. 7:217-228(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Cloning and sequence of full-length cDNAs encoding the human neuronal nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and expression of seven nAChR subunits in the human neuroblastoma cell line SH-SY5Y and/or IMR-32."
Groot Kormelink P.J., Luyten W.H.M.L.
FEBS Lett. 400:309-314(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Frontal cortex.
[4]"The structures of the human neuronal nicotinic acetylcholine receptor beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3)."
Rempel N., Heyers S., Engels H., Sleegers E., Steinlein O.K.
Hum. Genet. 103:645-653(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Genomic organization and mapping of the human and mouse neuronal beta2-nicotinic acetylcholine receptor genes."
Lueders K.K., Elliott R.W., Marenholz I., Mischke D., DuPree M., Hamer D.
Mamm. Genome 10:900-905(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells."
Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S.
Mol. Pharmacol. 68:1431-1438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIC3.
[8]"NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit."
Bondarenko V., Tillman T., Xu Y., Tang P.
Biochim. Biophys. Acta 1798:1608-1614(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 231-486.
[9]"NMR structures of the transmembrane domains of the alpha4beta2 nAChR."
Bondarenko V., Mowrey D., Tillman T., Cui T., Liu L.T., Xu Y., Tang P.
Biochim. Biophys. Acta 1818:1261-1268(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 234-484, SUBUNIT, FUNCTION.
[10]"The nicotinic receptor beta-2 subunit is mutant in nocturnal frontal lobe epilepsy."
De Fusco M., Becchetti A., Patrignani A., Annesi G., Gambardella A., Quattrone A., Ballabio A., Wanke E., Casari G.
Nat. Genet. 26:275-276(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENFL3 LEU-287.
[11]"CHRNB2 is the second acetylcholine receptor subunit associated with autosomal dominant nocturnal frontal lobe epilepsy."
Phillips H.A., Favre I., Kirkpatrick M., Zuberi S.M., Goudie D., Heron S.E., Scheffer I.E., Sutherland G.R., Berkovic S.F., Bertrand D., Mulley J.C.
Am. J. Hum. Genet. 68:225-231(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENFL3 MET-287.
[12]"Genetic and functional analysis of single nucleotide polymorphisms in the beta2-neuronal nicotinic acetylcholine receptor gene (CHRNB2)."
Lueders K.K., Hu S., McHugh L., Myakishev M.V., Sirota L.A., Hamer D.H.
Nicotine Tob. Res. 4:115-125(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-397.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53179 mRNA. Translation: CAA37320.1.
U62437 mRNA. Translation: AAB40115.1.
Y08415 mRNA. Translation: CAA69692.1.
AJ001935 expand/collapse EMBL AC list , AJ001936, AJ001937, AJ001938, AJ001939 Genomic DNA. Translation: CAA05108.1.
AF077186 Genomic DNA. Translation: AAD45422.1.
BC075040 mRNA. Translation: AAH75040.1.
BC075041 mRNA. Translation: AAH75041.1.
CCDSCCDS1070.1.
PIRS10505.
RefSeqNP_000739.1. NM_000748.2.
XP_006711206.1. XM_006711143.1.
UniGeneHs.2306.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GVTmodel-B/D/E30-233[»]
2K58NMR-B231-265[»]
2K59NMR-B264-291[»]
2KSRNMR-A231-330[»]
A453-486[»]
2LM2NMR-A231-330[»]
A458-485[»]
ProteinModelPortalP17787.
SMRP17787. Positions 26-338, 426-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-6629945.
STRING9606.ENSP00000357461.

Chemistry

BindingDBP17787.
ChEMBLCHEMBL2109233.
DrugBankDB00184. Nicotine.
GuidetoPHARMACOLOGY472.

Protein family/group databases

TCDB1.A.9.1.6. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Polymorphism databases

DMDM113105.

Proteomic databases

PaxDbP17787.
PRIDEP17787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368476; ENSP00000357461; ENSG00000160716.
GeneID1141.
KEGGhsa:1141.
UCSCuc001ffg.3. human.

Organism-specific databases

CTD1141.
GeneCardsGC01P154540.
GeneReviewsCHRNB2.
HGNCHGNC:1962. CHRNB2.
MIM118507. gene.
605375. phenotype.
neXtProtNX_P17787.
Orphanet98784. Autosomal dominant nocturnal frontal lobe epilepsy.
PharmGKBPA115.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290206.
HOGENOMHOG000006757.
HOVERGENHBG003756.
InParanoidP17787.
KOK04813.
OMADPTYVDI.
OrthoDBEOG72JWGV.
PhylomeDBP17787.
TreeFamTF315605.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressP17787.
BgeeP17787.
CleanExHS_CHRNB2.
GenevestigatorP17787.

Family and domain databases

Gene3D1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17787.
GeneWikiCHRNB2.
GenomeRNAi1141.
NextBio4748.
PROP17787.
SOURCESearch...

Entry information

Entry nameACHB2_HUMAN
AccessionPrimary (citable) accession number: P17787
Secondary accession number(s): Q9UEH9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM