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P02708 (ACHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholine receptor subunit alpha
Gene names
Name:CHRNA1
Synonyms:ACHRA, CHNRA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 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.

Subunit structure

Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.

Subcellular location

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

Tissue specificity

Isoform 1 is only expressed in skeletal muscle. Isoform 2 is constitutively expressed in skeletal muscle, brain, heart, kidney, liver, lung and thymus.

Involvement in disease

Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]: Multiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia, and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies are frequent.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

The alpha subunit is the main focus for antibody binding in myasthenia gravis. Myasthenia gravis is characterized by sporadic muscular fatigability and weakness, occurring chiefly in muscles innervated by cranial nerves, and characteristically improved by cholinesterase-inhibiting drugs.

Myasthenic syndrome, congenital, slow-channel (SCCMS) [MIM:601462]: A common congenital myasthenic syndrome. Congenital myasthenic syndromes are characterized by muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. Congenital myasthenic syndrome slow-channel type is caused by kinetic abnormalities of the AChR, resulting in prolonged endplate currents and prolonged AChR channel opening episodes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.17

Myasthenic syndrome, congenital, fast-channel (FCCMS) [MIM:608930]: A congenital myasthenic syndrome characterized by kinetic abnormalities of the AChR. Due in most cases to mutations that decrease activity of the AChR by slowing the rate of opening of the receptor channel, speeding the rate of closure of the channel, or decreasing the number of openings of the channel during ACh occupancy. The result is failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.15 Ref.16

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DiseaseCongenital myasthenic syndrome
Disease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcation transport

Inferred from mutant phenotype Ref.12. Source: GOC

ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

muscle cell cellular homeostasis

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

musculoskeletal movement

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

neuromuscular junction development

Inferred from mutant phenotype Ref.12. Source: MGI

neuromuscular process

Inferred from mutant phenotype PubMed 9546329. Source: BHF-UCL

neuromuscular synaptic transmission

Inferred from mutant phenotype Ref.12. Source: MGI

neuron cellular homeostasis

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

neuronal action potential

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

regulation of membrane potential

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

signal transduction

Traceable author statement Ref.9. Source: ProtInc

skeletal muscle contraction

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

skeletal muscle tissue growth

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

synaptic transmission

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.9. Source: ProtInc

   Cellular_componentacetylcholine-gated channel complex

Inferred from sequence or structural similarity Ref.10. Source: BHF-UCL

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 12928480. Source: BHF-UCL

neuromuscular junction

Inferred from sequence or structural similarity Ref.10. Source: BHF-UCL

plasma membrane

Inferred from sequence or structural similarity Ref.10. Source: BHF-UCL

postsynaptic membrane

Non-traceable author statement Ref.18. Source: BHF-UCL

   Molecular_functionacetylcholine binding

Inferred from electronic annotation. Source: Ensembl

acetylcholine receptor activity

Traceable author statement Ref.9. Source: ProtInc

acetylcholine-activated cation-selective channel activity

Inferred from mutant phenotype Ref.12. Source: MGI

ion channel activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P02708-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P02708-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-103: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.7
Chain21 – 482462Acetylcholine receptor subunit alpha
PRO_0000000305

Regions

Topological domain21 – 255235Extracellular
Transmembrane256 – 28025Helical
Transmembrane288 – 30619Helical
Transmembrane322 – 34120Helical
Topological domain342 – 453112Cytoplasmic
Transmembrane454 – 47219Helical

Amino acid modifications

Glycosylation1861N-linked (GlcNAc...) Potential
Disulfide bond173 ↔ 187
Disulfide bond237 ↔ 238Associated with receptor activation

Natural variations

Alternative sequence79 – 10325Missing in isoform 1.
VSP_000071
Natural variant1771V → L in FCCMS; mutant channel shows an approximately 30-fold decrease of ACh binding affinity for the second of 2 closed-state binding sites but only a 2-fold decrease in gating efficiency. Ref.15
VAR_038599
Natural variant1981G → S in SCCMS. Ref.9 Ref.11
VAR_000282
Natural variant2011V → M in SCCMS. Ref.11
VAR_000283
Natural variant2541R → L in LMPS. Ref.18
VAR_043904
Natural variant2621N → K in SCCMS. Ref.10
VAR_000284
Natural variant2781F → V in FCCMS; markedly reduced protein expression. Ref.13
VAR_021206
Natural variant2941V → F in SCCMS; causes increased channel opening in absence of ACh; prolonged opening in presence of ACh; increased affinity for ACh and enhanced desensitization. Ref.12
VAR_021207
Natural variant2991T → I in SCCMS. Ref.11
VAR_000285
Natural variant3011F → L in FCCMS; fewer and shorter ion channel activations with decreased channel opening rate and increased channel closing rate. Ref.16
VAR_021208
Natural variant3141S → I in SCCMS. Ref.11
VAR_000286
Natural variant3301V → I in FCCMS; abnormally slow channel opening and closing resulting in abnormally brief current. Ref.13
VAR_021209
Natural variant3831D → V.
Corresponds to variant rs6739001 [ dbSNP | Ensembl ].
VAR_038600
Natural variant4631C → W in SCCMS; increases the rate of channel opening and slows the rate of channel closing but has no effect on agonist binding. Ref.17
VAR_038601

Experimental info

Sequence conflict4151P → F in AAD14247. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 8B307AD69B91A28B

FASTA48254,546
        10         20         30         40         50         60 
MEPWPLLLLF SLCSAGLVLG SEHETRLVAK LFKDYSSVVR PVEDHRQVVE VTVGLQLIQL 

        70         80         90        100        110        120 
INVDEVNQIV TTNVRLKQGD MVDLPRPSCV TLGVPLFSHL QNEQWVDYNL KWNPDDYGGV 

       130        140        150        160        170        180 
KKIHIPSEKI WRPDLVLYNN ADGDFAIVKF TKVLLQYTGH ITWTPPAIFK SYCEIIVTHF 

       190        200        210        220        230        240 
PFDEQNCSMK LGTWTYDGSV VAINPESDQP DLSNFMESGE WVIKESRGWK HSVTYSCCPD 

       250        260        270        280        290        300 
TPYLDITYHF VMQRLPLYFI VNVIIPCLLF SFLTGLVFYL PTDSGEKMTL SISVLLSLTV 

       310        320        330        340        350        360 
FLLVIVELIP STSSAVPLIG KYMLFTMVFV IASIIITVIV INTHHRSPST HVMPNWVRKV 

       370        380        390        400        410        420 
FIDTIPNIMF FSTMKRPSRE KQDKKIFTED IDISDISGKP GPPPMGFHSP LIKHPEVKSA 

       430        440        450        460        470        480 
IEGIKYIAET MKSDQESNNA AAEWKYVAMV MDHILLGVFM LVCIIGTLAV FAGRLIELNQ 


QG 

« Hide

Isoform 1 [UniParc].

Checksum: 89480567D85C15B8
Show »

FASTA45751,839

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of calf cDNA and human genomic DNA encoding alpha-subunit precursor of muscle acetylcholine receptor."
Noda M., Furutani Y., Takahashi H., Toyosato M., Tanabe T., Shimizu S., Kikyotani S., Kayano T., Hirose T., Inayama S., Numa S.
Nature 305:818-823(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The human medulloblastoma cell line TE671 expresses a muscle-like acetylcholine receptor. Cloning of the alpha-subunit cDNA."
Schoepfer R., Luther M., Lindstrom J.M.
FEBS Lett. 226:235-240(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The human muscle nicotinic acetylcholine receptor alpha-subunit exist as two isoforms: a novel exon."
Beeson D., Morris A., Vincent A., Newsom-Davis J.
EMBO J. 9:2101-2106(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
Tissue: Muscle.
[4]"Cloning of a cDNA coding for the acetylcholine receptor alpha-subunit from a thymoma associated with myasthenia gravis."
Gattenloehner S., Brabletz T., Schultz A., Marx A., Mueller-Hermelink H.-K., Kirchner T.
Thymus 23:103-113(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Thymus.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Tongue.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Amphipathic segment of the nicotinic receptor alpha subunit contains epitopes recognized by T lymphocytes in myasthenia gravis."
Hohlfeld R., Toyka K.V., Miner L.L., Walgrave S.L., Conti-Tronconi B.M.
J. Clin. Invest. 81:657-660(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-482 (ISOFORM 1).
[8]"Differential expression of human nicotinic acetylcholine receptor alpha subunit variants in muscle and non-muscle tissues."
Talib S., Okarma T.B., Lebkowski J.S.
Nucleic Acids Res. 21:233-237(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-113.
[9]"Mutation of the acetylcholine receptor alpha subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity."
Sine S.M., Ohno K., Bouzat C., Auerbach A., Milone M., Pruitt J.N. II, Engel A.G.
Neuron 15:229-239(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCCMS SER-198.
[10]"New mutations in acetylcholine receptor subunit genes reveal heterogeneity in the slow-channel congenital myasthenic syndrome."
Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C., Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P., Sine S.M.
Hum. Mol. Genet. 5:1217-1227(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCCMS LYS-262.
[11]"Mutations in different functional domains of the human muscle acetylcholine receptor alpha subunit in patients with the slow-channel congenital myasthenic syndrome."
Croxen R., Newland C., Beeson D., Oosterhuis H., Chauplannaz G., Vincent A., Newsom-Davis J.
Hum. Mol. Genet. 6:767-774(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCCMS SER-198; MET-201; ILE-299 AND ILE-314.
[12]"Slow-channel myasthenic syndrome caused by enhanced activation, desensitization, and agonist binding affinity attributable to mutation in the M2 domain of the acetylcholine receptor alpha subunit."
Milone M., Wang H.-L., Ohno K., Fukudome T., Pruitt J.N. II, Bren N., Sine S.M., Engel A.G.
J. Neurosci. 17:5651-5665(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCCMS PHE-294, CHARACTERIZATION OF VARIANT SCCMS PHE-294.
[13]"Acetylcholine receptor M3 domain: stereochemical and volume contributions to channel gating."
Wang H.-L., Milone M., Ohno K., Shen X.-M., Tsujino A., Batocchi A.-P., Tonali P., Brengman J., Engel A.G., Sine S.M.
Nat. Neurosci. 2:226-233(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCCMS VAL-278 AND ILE-330, CHARACTERIZATION OF VARIANTS FCCMS VAL-278 AND ILE-330.
[14]Erratum
Wang H.-L., Milone M., Ohno K., Shen X.-M., Tsujino A., Batocchi A.-P., Tonali P., Brengman J., Engel A.G., Sine S.M.
Nat. Neurosci. 2:485-485(1999)
[15]"Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating."
Shen X.-M., Ohno K., Tsujino A., Brengman J.M., Gingold M., Sine S.M., Engel A.G.
J. Clin. Invest. 111:497-505(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FCCMS LEU-177, CHARACTERIZATION OF VARIANT FCCMS LEU-177.
[16]"Mutation in the AChR ion channel gate underlies a fast channel congenital myasthenic syndrome."
Webster R., Brydson M., Croxen R., Newsom-Davis J., Vincent A., Beeson D.
Neurology 62:1090-1096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FCCMS LEU-301, CHARACTERIZATION OF VARIANT FCCMS LEU-301.
[17]"Slow-channel mutation in acetylcholine receptor alphaM4 domain and its efficient knockdown."
Shen X.-M., Deymeer F., Sine S.M., Engel A.G.
Ann. Neurol. 60:128-136(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCCMS TRP-463, CHARACTERIZATION OF VARIANT SCCMS TRP-463.
[18]"Acetylcholine receptor pathway mutations explain various fetal akinesia deformation sequence disorders."
Michalk A., Stricker S., Becker J., Rupps R., Pantzar T., Miertus J., Botta G., Naretto V.G., Janetzki C., Yaqoob N., Ott C.-E., Seelow D., Wieczorek D., Fiebig B., Wirth B., Hoopmann M., Walther M., Koerber F. expand/collapse author list , Blankenburg M., Mundlos S., Heller R., Hoffmann K.
Am. J. Hum. Genet. 82:464-476(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LMPS LEU-254.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02502 expand/collapse EMBL AC list , X02503, X02504, X02505, X02506, X02507, X02508 Genomic DNA. Translation: CAA26344.1.
Y00762 mRNA. Translation: CAA68731.1.
X17104 Genomic DNA. Translation: CAA34960.1.
AK299445 mRNA. Translation: BAG61418.1.
CH471058 Genomic DNA. Translation: EAX11125.1.
CH471058 Genomic DNA. Translation: EAX11127.1.
S77094 mRNA. Translation: AAD14247.1.
X70108 Genomic DNA. Translation: CAA49705.1. Sequence problems.
CCDSCCDS2261.1. [P02708-2]
CCDS33331.1. [P02708-1]
PIRACHUA1. A03168.
S10148.
RefSeqNP_000070.1. NM_000079.3. [P02708-2]
NP_001034612.1. NM_001039523.2. [P02708-1]
UniGeneHs.434479.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y5Pmodel-B230-235[»]
1Y5Tmodel-B230-235[»]
1Y6Cmodel-B230-235[»]
ProteinModelPortalP02708.
SMRP02708. Positions 21-351, 448-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107556. 4 interactions.
STRING9606.ENSP00000261007.

Chemistry

BindingDBP02708.
ChEMBLCHEMBL1907588.
GuidetoPHARMACOLOGY462.

Protein family/group databases

TCDB1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

PTM databases

PhosphoSiteP02708.

Polymorphism databases

DMDM113071.

Proteomic databases

PaxDbP02708.
PRIDEP02708.

Protocols and materials databases

DNASU1134.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261007; ENSP00000261007; ENSG00000138435. [P02708-1]
ENST00000348749; ENSP00000261008; ENSG00000138435. [P02708-2]
GeneID1134.
KEGGhsa:1134.
UCSCuc002ujd.2. human. [P02708-1]

Organism-specific databases

CTD1134.
GeneCardsGC02M175612.
GeneReviewsCHRNA1.
HGNCHGNC:1955. CHRNA1.
HPACAB010902.
MIM100690. gene.
253290. phenotype.
254200. phenotype.
601462. phenotype.
608930. phenotype.
neXtProtNX_P02708.
Orphanet33108. Lethal multiple pterygium syndrome.
98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBPA26487.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314424.
HOGENOMHOG000006756.
HOVERGENHBG003756.
InParanoidP02708.
KOK04803.
OMATHVMPNW.
OrthoDBEOG72JWGV.
PhylomeDBP02708.
TreeFamTF315605.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressP02708.
BgeeP02708.
CleanExHS_CHRNA1.
GenevestigatorP02708.

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. 2 hits.
PF02932. Neur_chan_memb. 2 hits.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 2 hits.
SSF90112. SSF90112. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCholinergic_receptor,_nicotinic,_alpha_1.
GenomeRNAi1134.
NextBio4716.
PROP02708.
SOURCESearch...

Entry information

Entry nameACHA_HUMAN
AccessionPrimary (citable) accession number: P02708
Secondary accession number(s): B4DRV6, D3DPE8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 167 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM