P02708 (ACHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylcholine receptor subunit alpha

Gene names

Name:	CHRNA1
Synonyms:	ACHRA, CHNRA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › synapse › postsynaptic 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.19 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.10 Ref.11 Ref.12 Ref.13 Ref.18 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.14 Ref.16 Ref.17
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 process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Disease	Congenital myasthenic syndrome Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	muscle cell homeostasis Inferred from mutant phenotype Ref.11. Source: BHF-UCL neuromuscular junction development Inferred from mutant phenotype Ref.13. Source: MGI neuromuscular process Inferred from mutant phenotype PubMed 9546329. Source: BHF-UCL neuromuscular synaptic transmission Inferred from mutant phenotype Ref.13. Source: MGI neuron homeostasis Inferred from mutant phenotype Ref.11. Source: BHF-UCL regulation of action potential in neuron Inferred from mutant phenotype Ref.11. Source: BHF-UCL skeletal muscle contraction Inferred from mutant phenotype Ref.11. Source: BHF-UCL skeletal muscle tissue growth Inferred from mutant phenotype Ref.19. Source: BHF-UCL
Cellular_component	acetylcholine-gated channel complex Inferred from sequence or structural similarity Ref.11. 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.11. Source: BHF-UCL postsynaptic membrane Non-traceable author statement Ref.19. Source: BHF-UCL
Molecular_function	acetylcholine binding Inferred from electronic annotation. Source: Compara acetylcholine receptor activity Traceable author statement Ref.10. Source: ProtInc acetylcholine-activated cation-selective channel activity Inferred from mutant phenotype Ref.13. Source: MGI
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Ref.7
	Chain	21 – 482	462	Acetylcholine receptor subunit alpha		PRO_0000000305
Regions
	Topological domain	21 – 255	235	Extracellular
	Transmembrane	256 – 280	25	Helical
	Transmembrane	288 – 306	19	Helical
	Transmembrane	322 – 341	20	Helical
	Topological domain	342 – 453	112	Cytoplasmic
	Transmembrane	454 – 472	19	Helical
Amino acid modifications
	Glycosylation	186	1	N-linked (GlcNAc...) Potential
	Disulfide bond	173 ↔ 187
	Disulfide bond	237 ↔ 238		Associated with receptor activation
Natural variations
	Alternative sequence	79 – 103	25	Missing in isoform 1.		VSP_000071
	Natural variant	177	1	V → 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.16		VAR_038599
	Natural variant	198	1	G → S in SCCMS. Ref.10 Ref.12		VAR_000282
	Natural variant	201	1	V → M in SCCMS. Ref.12		VAR_000283
	Natural variant	254	1	R → L in LMPS. Ref.19		VAR_043904
	Natural variant	262	1	N → K in SCCMS. Ref.11		VAR_000284
	Natural variant	278	1	F → V in FCCMS; markedly reduced protein expression. Ref.14		VAR_021206
	Natural variant	294	1	V → 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.13		VAR_021207
	Natural variant	299	1	T → I in SCCMS. Ref.12		VAR_000285
	Natural variant	301	1	F → L in FCCMS; fewer and shorter ion channel activations with decreased channel opening rate and increased channel closing rate. Ref.17		VAR_021208
	Natural variant	314	1	S → I in SCCMS. Ref.12		VAR_000286
	Natural variant	330	1	V → I in FCCMS; abnormally slow channel opening and closing resulting in abnormally brief current. Ref.14		VAR_021209
	Natural variant	383	1	D → V. Corresponds to variant rs6739001 [ dbSNP | Ensembl ].		VAR_038600
	Natural variant	463	1	C → W in SCCMS; increases the rate of channel opening and slows the rate of channel closing but has no effect on agonist binding. Ref.18		VAR_038601
Experimental info
	Sequence conflict	415	1	P → F in AAD14247. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: 8B307AD69B91A28B	FASTA	482	54,546
	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
	Isoform 1 [UniParc]. Checksum: 89480567D85C15B8	FASTA	457	51,839
	10 20 30 40 50 60 MEPWPLLLLF SLCSAGLVLG SEHETRLVAK LFKDYSSVVR PVEDHRQVVE VTVGLQLIQL 70 80 90 100 110 120 INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPDL VLYNNADGDF 130 140 150 160 170 180 AIVKFTKVLL QYTGHITWTP PAIFKSYCEI IVTHFPFDEQ NCSMKLGTWT YDGSVVAINP 190 200 210 220 230 240 ESDQPDLSNF MESGEWVIKE SRGWKHSVTY SCCPDTPYLD ITYHFVMQRL PLYFIVNVII 250 260 270 280 290 300 PCLLFSFLTG LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF 310 320 330 340 350 360 TMVFVIASII ITVIVINTHH RSPSTHVMPN WVRKVFIDTI PNIMFFSTMK RPSREKQDKK 370 380 390 400 410 420 IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGIK YIAETMKSDQ ESNNAAAEWK 430 440 450 YVAMVMDHIL LGVFMLVCII GTLAVFAGRL IELNQQG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	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)
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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. , 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.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00022298.
IPI00218234.

PIR

ACHUA1. A03168.
S10148.

RefSeq

NP_000070.1. NM_000079.3.
NP_001034612.1. NM_001039523.2.

UniGene

Hs.434479.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y5P	model	-	B	230-235	[»]
1Y5T	model	-	B	230-235	[»]
1Y6C	model	-	B	230-235	[»]

ProteinModelPortal

P02708.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000261007.

PTM databases

PhosphoSite

P02708.

Polymorphism databases

DMDM

113071.

Proteomic databases

PaxDb

P02708.

PRIDE

P02708.

Protocols and materials databases

DNASU

1134.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261007; ENSP00000261007; ENSG00000138435.
ENST00000348749; ENSP00000261008; ENSG00000138435.

GeneID

1134.

KEGG

hsa:1134.

UCSC

uc002ujd.2. human.

Organism-specific databases

CTD

1134.

GeneCards

GC02M175612.

HGNC

HGNC:1955. CHRNA1.

HPA

CAB010902.

MIM

100690. gene.
253290. phenotype.
254200. phenotype.
601462. phenotype.
608930. phenotype.

neXtProt

NX_P02708.

Orphanet

33108. Lethal multiple pterygium syndrome.
98913. Postsynaptic congenital myasthenic syndromes.

PharmGKB

PA26487.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG314424.

HOGENOM

HOG000006756.

HOVERGEN

HBG003756.

InParanoid

P02708.

KO

K04803.

OMA

YSCCPDT.

PhylomeDB

P02708.

Enzyme and pathway databases

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

P02708.

Bgee

P02708.

CleanEx

HS_CHRNA1.

Genevestigator

P02708.

GermOnline

ENSG00000138435. Homo sapiens.

Family and domain databases

Gene3D

1.20.120.370. 2 hits.
2.70.170.10. 1 hit.

InterPro

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]

PANTHER

PTHR18945. PTHR18945. 1 hit.

Pfam

PF02931. Neur_chan_LBD. 2 hits.
PF02932. Neur_chan_memb. 2 hits.
[Graphical view]

PRINTS

PR00254. NICOTINICR.
PR00252. NRIONCHANNEL.

SUPFAM

SSF90112. Neu_channel_TM. 1 hit.
SSF63712. Neur_chan_LBD. 1 hit.

PROSITE

PS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02708.

ChEMBL

CHEMBL4808.

GenomeRNAi

1134.

NextBio

4716.

SOURCE

Search...

Entry information

Entry name

ACHA_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 155 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.