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P02708

- ACHA_HUMAN

UniProt

P02708 - ACHA_HUMAN

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Protein

Acetylcholine receptor subunit alpha

Gene

CHRNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 255235ExtracellularAdd
BLAST
Transmembranei256 – 28025HelicalAdd
BLAST
Transmembranei288 – 30619HelicalAdd
BLAST
Transmembranei322 – 34120HelicalAdd
BLAST
Topological domaini342 – 453112CytoplasmicAdd
BLAST
Transmembranei454 – 47219HelicalAdd
BLAST

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
Complete GO annotation...

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

BgeeiP02708.
CleanExiHS_CHRNA1.
ExpressionAtlasiP02708. baseline and differential.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y5Pmodel-B230-235[»]
1Y5Tmodel-B230-235[»]
1Y6Cmodel-B230-235[»]
ProteinModelPortaliP02708.
SMRiP02708. Positions 20-482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG314424.
GeneTreeiENSGT00760000118930.
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

        10         20         30         40         50
MEPWPLLLLF SLCSAGLVLG SEHETRLVAK LFKDYSSVVR PVEDHRQVVE
60 70 80 90 100
VTVGLQLIQL INVDEVNQIV TTNVRLKQGD MVDLPRPSCV TLGVPLFSHL
110 120 130 140 150
QNEQWVDYNL KWNPDDYGGV KKIHIPSEKI WRPDLVLYNN ADGDFAIVKF
160 170 180 190 200
TKVLLQYTGH ITWTPPAIFK SYCEIIVTHF PFDEQNCSMK LGTWTYDGSV
210 220 230 240 250
VAINPESDQP DLSNFMESGE WVIKESRGWK HSVTYSCCPD TPYLDITYHF
260 270 280 290 300
VMQRLPLYFI VNVIIPCLLF SFLTGLVFYL PTDSGEKMTL SISVLLSLTV
310 320 330 340 350
FLLVIVELIP STSSAVPLIG KYMLFTMVFV IASIIITVIV INTHHRSPST
360 370 380 390 400
HVMPNWVRKV FIDTIPNIMF FSTMKRPSRE KQDKKIFTED IDISDISGKP
410 420 430 440 450
GPPPMGFHSP LIKHPEVKSA IEGIKYIAET MKSDQESNNA AAEWKYVAMV
460 470 480
MDHILLGVFM LVCIIGTLAV FAGRLIELNQ QG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 20-482.
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.
GeneTreei ENSGT00760000118930.
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

Bgeei P02708.
CleanExi HS_CHRNA1.
ExpressionAtlasi P02708. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 171 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