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P02708

- ACHA_HUMAN

UniProt

P02708 - ACHA_HUMAN

Protein

Acetylcholine receptor subunit alpha

Gene

CHRNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. acetylcholine-activated cation-selective channel activity Source: MGI
    2. acetylcholine binding Source: Ensembl
    3. acetylcholine receptor activity Source: ProtInc
    4. ion channel activity Source: ProtInc

    GO - Biological processi

    1. cation transport Source: GOC
    2. ion transmembrane transport Source: GOC
    3. muscle cell cellular homeostasis Source: BHF-UCL
    4. musculoskeletal movement Source: BHF-UCL
    5. neuromuscular junction development Source: MGI
    6. neuromuscular process Source: BHF-UCL
    7. neuromuscular synaptic transmission Source: MGI
    8. neuronal action potential Source: BHF-UCL
    9. neuron cellular homeostasis Source: BHF-UCL
    10. regulation of membrane potential Source: BHF-UCL
    11. signal transduction Source: ProtInc
    12. skeletal muscle contraction Source: BHF-UCL
    13. skeletal muscle tissue growth Source: BHF-UCL
    14. synaptic transmission Source: Reactome
    15. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_22303. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
    REACT_22352. Highly calcium permeable nicotinic acetylcholine receptors.

    Protein family/group databases

    TCDBi1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholine receptor subunit alpha
    Gene namesi
    Name:CHRNA1
    Synonyms:ACHRA, CHNRA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1955. CHRNA1.

    Subcellular locationi

    GO - Cellular componenti

    1. acetylcholine-gated channel complex Source: BHF-UCL
    2. cell junction Source: UniProtKB-KW
    3. cell surface Source: BHF-UCL
    4. neuromuscular junction Source: BHF-UCL
    5. plasma membrane Source: BHF-UCL
    6. postsynaptic membrane Source: BHF-UCL

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti254 – 2541R → L in LMPS. 1 Publication
    VAR_043904
    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981G → S in SCCMS. 2 Publications
    VAR_000282
    Natural varianti201 – 2011V → M in SCCMS. 1 Publication
    VAR_000283
    Natural varianti262 – 2621N → K in SCCMS. 1 Publication
    VAR_000284
    Natural varianti294 – 2941V → F in SCCMS; causes increased channel opening in absence of ACh; prolonged opening in presence of ACh; increased affinity for ACh and enhanced desensitization. 1 Publication
    VAR_021207
    Natural varianti299 – 2991T → I in SCCMS. 1 Publication
    VAR_000285
    Natural varianti314 – 3141S → I in SCCMS. 1 Publication
    VAR_000286
    Natural varianti463 – 4631C → W in SCCMS; increases the rate of channel opening and slows the rate of channel closing but has no effect on agonist binding. 1 Publication
    VAR_038601
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771V → 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. 1 Publication
    VAR_038599
    Natural varianti278 – 2781F → V in FCCMS; markedly reduced protein expression. 1 Publication
    VAR_021206
    Natural varianti301 – 3011F → L in FCCMS; fewer and shorter ion channel activations with decreased channel opening rate and increased channel closing rate. 1 Publication
    VAR_021208
    Natural varianti330 – 3301V → I in FCCMS; abnormally slow channel opening and closing resulting in abnormally brief current. 1 Publication
    VAR_021209

    Keywords - Diseasei

    Congenital myasthenic syndrome, Disease mutation

    Organism-specific databases

    MIMi253290. phenotype.
    254200. phenotype.
    601462. phenotype.
    608930. phenotype.
    Orphaneti33108. Lethal multiple pterygium syndrome.
    98913. Postsynaptic congenital myasthenic syndromes.
    PharmGKBiPA26487.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 482462Acetylcholine receptor subunit alphaPRO_0000000305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi173 ↔ 187
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi237 ↔ 238Associated with receptor activation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP02708.
    PRIDEiP02708.

    PTM databases

    PhosphoSiteiP02708.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP02708.
    BgeeiP02708.
    CleanExiHS_CHRNA1.
    GenevestigatoriP02708.

    Organism-specific databases

    HPAiCAB010902.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi107556. 4 interactions.
    STRINGi9606.ENSP00000261007.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y5Pmodel-B230-235[»]
    1Y5Tmodel-B230-235[»]
    1Y6Cmodel-B230-235[»]
    ProteinModelPortaliP02708.
    SMRiP02708. Positions 21-351, 448-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 255235ExtracellularAdd
    BLAST
    Topological domaini342 – 453112CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei256 – 28025HelicalAdd
    BLAST
    Transmembranei288 – 30619HelicalAdd
    BLAST
    Transmembranei322 – 34120HelicalAdd
    BLAST
    Transmembranei454 – 47219HelicalAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG314424.
    HOGENOMiHOG000006756.
    HOVERGENiHBG003756.
    InParanoidiP02708.
    KOiK04803.
    OMAiTHVMPNW.
    OrthoDBiEOG72JWGV.
    PhylomeDBiP02708.
    TreeFamiTF315605.

    Family and domain databases

    Gene3Di1.20.120.370. 2 hits.
    2.70.170.10. 1 hit.
    InterProiIPR027361. 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]
    PANTHERiPTHR18945. PTHR18945. 1 hit.
    PfamiPF02931. Neur_chan_LBD. 2 hits.
    PF02932. Neur_chan_memb. 2 hits.
    [Graphical view]
    PRINTSiPR00254. NICOTINICR.
    PR00252. NRIONCHANNEL.
    SUPFAMiSSF63712. SSF63712. 2 hits.
    SSF90112. SSF90112. 1 hit.
    PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P02708-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEPWPLLLLF SLCSAGLVLG SEHETRLVAK LFKDYSSVVR PVEDHRQVVE    50
    VTVGLQLIQL INVDEVNQIV TTNVRLKQGD MVDLPRPSCV TLGVPLFSHL 100
    QNEQWVDYNL KWNPDDYGGV KKIHIPSEKI WRPDLVLYNN ADGDFAIVKF 150
    TKVLLQYTGH ITWTPPAIFK SYCEIIVTHF PFDEQNCSMK LGTWTYDGSV 200
    VAINPESDQP DLSNFMESGE WVIKESRGWK HSVTYSCCPD TPYLDITYHF 250
    VMQRLPLYFI VNVIIPCLLF SFLTGLVFYL PTDSGEKMTL SISVLLSLTV 300
    FLLVIVELIP STSSAVPLIG KYMLFTMVFV IASIIITVIV INTHHRSPST 350
    HVMPNWVRKV FIDTIPNIMF FSTMKRPSRE KQDKKIFTED IDISDISGKP 400
    GPPPMGFHSP LIKHPEVKSA IEGIKYIAET MKSDQESNNA AAEWKYVAMV 450
    MDHILLGVFM LVCIIGTLAV FAGRLIELNQ QG 482
    Length:482
    Mass (Da):54,546
    Last modified:August 1, 1990 - v2
    Checksum:i8B307AD69B91A28B
    GO
    Isoform 1 (identifier: P02708-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:457
    Mass (Da):51,839
    Checksum:i89480567D85C15B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti415 – 4151P → F in AAD14247. (PubMed:7725386)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771V → 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. 1 Publication
    VAR_038599
    Natural varianti198 – 1981G → S in SCCMS. 2 Publications
    VAR_000282
    Natural varianti201 – 2011V → M in SCCMS. 1 Publication
    VAR_000283
    Natural varianti254 – 2541R → L in LMPS. 1 Publication
    VAR_043904
    Natural varianti262 – 2621N → K in SCCMS. 1 Publication
    VAR_000284
    Natural varianti278 – 2781F → V in FCCMS; markedly reduced protein expression. 1 Publication
    VAR_021206
    Natural varianti294 – 2941V → F in SCCMS; causes increased channel opening in absence of ACh; prolonged opening in presence of ACh; increased affinity for ACh and enhanced desensitization. 1 Publication
    VAR_021207
    Natural varianti299 – 2991T → I in SCCMS. 1 Publication
    VAR_000285
    Natural varianti301 – 3011F → L in FCCMS; fewer and shorter ion channel activations with decreased channel opening rate and increased channel closing rate. 1 Publication
    VAR_021208
    Natural varianti314 – 3141S → I in SCCMS. 1 Publication
    VAR_000286
    Natural varianti330 – 3301V → I in FCCMS; abnormally slow channel opening and closing resulting in abnormally brief current. 1 Publication
    VAR_021209
    Natural varianti383 – 3831D → V.
    Corresponds to variant rs6739001 [ dbSNP | Ensembl ].
    VAR_038600
    Natural varianti463 – 4631C → W in SCCMS; increases the rate of channel opening and slows the rate of channel closing but has no effect on agonist binding. 1 Publication
    VAR_038601

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei79 – 10325Missing in isoform 1. 2 PublicationsVSP_000071Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02502
    , 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.
    CCDSiCCDS2261.1. [P02708-2]
    CCDS33331.1. [P02708-1]
    PIRiA03168. ACHUA1.
    S10148.
    RefSeqiNP_000070.1. NM_000079.3. [P02708-2]
    NP_001034612.1. NM_001039523.2. [P02708-1]
    UniGeneiHs.434479.

    Genome annotation databases

    EnsembliENST00000261007; ENSP00000261007; ENSG00000138435. [P02708-1]
    ENST00000348749; ENSP00000261008; ENSG00000138435. [P02708-2]
    GeneIDi1134.
    KEGGihsa:1134.
    UCSCiuc002ujd.2. human. [P02708-1]

    Polymorphism databases

    DMDMi113071.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02502
    , 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.
    CCDSi CCDS2261.1. [P02708-2 ]
    CCDS33331.1. [P02708-1 ]
    PIRi A03168. ACHUA1.
    S10148.
    RefSeqi NP_000070.1. NM_000079.3. [P02708-2 ]
    NP_001034612.1. NM_001039523.2. [P02708-1 ]
    UniGenei Hs.434479.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y5P model - B 230-235 [» ]
    1Y5T model - B 230-235 [» ]
    1Y6C model - B 230-235 [» ]
    ProteinModelPortali P02708.
    SMRi P02708. Positions 21-351, 448-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107556. 4 interactions.
    STRINGi 9606.ENSP00000261007.

    Chemistry

    BindingDBi P02708.
    ChEMBLi CHEMBL1907588.
    DrugBanki DB00674. Galantamine.
    GuidetoPHARMACOLOGYi 462.

    Protein family/group databases

    TCDBi 1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

    PTM databases

    PhosphoSitei P02708.

    Polymorphism databases

    DMDMi 113071.

    Proteomic databases

    PaxDbi P02708.
    PRIDEi P02708.

    Protocols and materials databases

    DNASUi 1134.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261007 ; ENSP00000261007 ; ENSG00000138435 . [P02708-1 ]
    ENST00000348749 ; ENSP00000261008 ; ENSG00000138435 . [P02708-2 ]
    GeneIDi 1134.
    KEGGi hsa:1134.
    UCSCi uc002ujd.2. human. [P02708-1 ]

    Organism-specific databases

    CTDi 1134.
    GeneCardsi GC02M175612.
    GeneReviewsi CHRNA1.
    HGNCi HGNC:1955. CHRNA1.
    HPAi CAB010902.
    MIMi 100690. gene.
    253290. phenotype.
    254200. phenotype.
    601462. phenotype.
    608930. phenotype.
    neXtProti NX_P02708.
    Orphaneti 33108. Lethal multiple pterygium syndrome.
    98913. Postsynaptic congenital myasthenic syndromes.
    PharmGKBi PA26487.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314424.
    HOGENOMi HOG000006756.
    HOVERGENi HBG003756.
    InParanoidi P02708.
    KOi K04803.
    OMAi THVMPNW.
    OrthoDBi EOG72JWGV.
    PhylomeDBi P02708.
    TreeFami TF315605.

    Enzyme and pathway databases

    Reactomei REACT_22303. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
    REACT_22352. Highly calcium permeable nicotinic acetylcholine receptors.

    Miscellaneous databases

    GeneWikii Cholinergic_receptor,_nicotinic,_alpha_1.
    GenomeRNAii 1134.
    NextBioi 4716.
    PROi P02708.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02708.
    Bgeei P02708.
    CleanExi HS_CHRNA1.
    Genevestigatori P02708.

    Family and domain databases

    Gene3Di 1.20.120.370. 2 hits.
    2.70.170.10. 1 hit.
    InterProi IPR027361. 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 ]
    PANTHERi PTHR18945. PTHR18945. 1 hit.
    Pfami PF02931. Neur_chan_LBD. 2 hits.
    PF02932. Neur_chan_memb. 2 hits.
    [Graphical view ]
    PRINTSi PR00254. NICOTINICR.
    PR00252. NRIONCHANNEL.
    SUPFAMi SSF63712. SSF63712. 2 hits.
    SSF90112. SSF90112. 1 hit.
    PROSITEi PS00236. NEUROTR_ION_CHANNEL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. "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.
    15. "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.
    16. "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.
    17. Cited for: VARIANT LMPS LEU-254.

    Entry informationi

    Entry nameiACHA_HUMAN
    AccessioniPrimary (citable) accession number: P02708
    Secondary accession number(s): B4DRV6, D3DPE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3