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P22303 (ACES_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase

Short name=AChE
EC=3.1.1.7
Gene names
Name:ACHE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. Ref.11 Ref.12 Ref.13 Ref.14

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subunit structure

Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers By similarity. Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. Isoform R may be monomeric.

Subcellular location

Cell junctionsynapse. Secreted By similarity. Cell membrane; Peripheral membrane protein By similarity Ref.12 Ref.14.

Isoform T: Nucleus. Note: Only observed in apoptotic nuclei. Ref.12 Ref.14

Isoform H: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side By similarity Ref.12 Ref.14.

Tissue specificity

Isoform H is highly expressed in erythrocytes. Ref.11

Polymorphism

ACHE is responsible for the Yt blood group system [MIM:112100]. The molecular basis of the Yt(a)=Yt1/Yt(b)=Yt2 blood group antigens is a single variation in position 353; His-353 corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b).

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Nucleus
Secreted
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionBlood group antigen
Hydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement PubMed 11283752. Source: UniProtKB

acetylcholine catabolic process

Inferred from direct assay Ref.13. Source: HGNC

acetylcholine catabolic process in synaptic cleft

Non-traceable author statement Ref.13. Source: UniProtKB

amyloid precursor protein metabolic process

Traceable author statement PubMed 12769797. Source: UniProtKB

cell adhesion

Traceable author statement PubMed 11283752. Source: UniProtKB

cell proliferation

Traceable author statement PubMed 11283752. Source: UniProtKB

choline metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

muscle organ development

Traceable author statement PubMed 11283752. Source: UniProtKB

negative regulation of synaptic transmission, cholinergic

Inferred by curator Ref.13. Source: HGNC

nervous system development

Traceable author statement PubMed 11283752. Source: UniProtKB

neurotransmitter biosynthetic process

Traceable author statement. Source: Reactome

neurotransmitter receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

osteoblast development

Inferred from expression pattern PubMed 15454088. Source: HGNC

phosphatidylcholine biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of protein secretion

Traceable author statement PubMed 11283752. Source: UniProtKB

protein tetramerization

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of dendrite morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of receptor recycling

Inferred from electronic annotation. Source: Ensembl

response to wounding

Traceable author statement PubMed 11283752. Source: UniProtKB

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

synapse assembly

Traceable author statement PubMed 11283752. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15454088. Source: HGNC

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

axon

Inferred from Biological aspect of Ancestor. Source: RefGenome

basal lamina

Non-traceable author statement PubMed 16289501. Source: HGNC

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from Biological aspect of Ancestor. Source: RefGenome

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum lumen

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular region

Traceable author statement PubMed 11283752. Source: UniProtKB

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay PubMed 16262697. Source: HGNC

neuromuscular junction

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 14766237. Source: HGNC

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from direct assay PubMed 8460160. Source: HGNC

   Molecular_functionacetylcholine binding

Non-traceable author statement Ref.13. Source: UniProtKB

acetylcholinesterase activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

beta-amyloid binding

Traceable author statement PubMed 11283752. Source: UniProtKB

cholinesterase activity

Inferred from direct assay Ref.13. Source: HGNC

collagen binding

Inferred from direct assay PubMed 12524166. Source: HGNC

hydrolase activity

Inferred from direct assay Ref.13. Source: HGNC

laminin binding

Inferred from direct assay PubMed 12524166. Source: BHF-UCL

protein homodimerization activity

Non-traceable author statement Ref.13. Source: UniProtKB

serine hydrolase activity

Inferred from direct assay PubMed 3954986. Source: HGNC

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform T (identifier: P22303-1)

Also known as: ACHE-S; synaptic;

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 H (identifier: P22303-2)

Also known as: ACHE-E; erythrocytic; E4-E5;

The sequence of this isoform differs from the canonical sequence as follows:
     575-614: DTLDEAERQW...YSKQDRCSDL → ASEAPSTCPG...LLFLSHLRRL
Note: GPI-anchor amidated glycine on Gly-588.
Isoform R (identifier: P22303-4)

Also known as: ACHE-R; readthrough;

The sequence of this isoform differs from the canonical sequence as follows:
     575-603: DTLDEAERQWKAEFHRWSSYMVHWKNQFD → GMQGPAGSAGRRGVGARQCNPSLLPLASE
     604-614: Missing.
Isoform 4 (identifier: P22303-3)

The sequence of this isoform differs from the canonical sequence as follows:
     357-444: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 614583Acetylcholinesterase
PRO_0000008587

Sites

Active site2341Acyl-ester intermediate
Active site3651Charge relay system
Active site4781Charge relay system

Amino acid modifications

Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Ref.16
Glycosylation4951N-linked (GlcNAc...) Ref.16
Disulfide bond100 ↔ 127
Disulfide bond288 ↔ 303
Disulfide bond440 ↔ 560
Disulfide bond611Interchain

Natural variations

Alternative sequence357 – 44488Missing in isoform 4.
VSP_035568
Alternative sequence575 – 61440DTLDE…RCSDL → ASEAPSTCPGFTHGEAAPRP GLPLPLLLLHQLLLLFLSHL RRL in isoform H.
VSP_001457
Alternative sequence575 – 60329DTLDE…KNQFD → GMQGPAGSAGRRGVGARQCN PSLLPLASE in isoform R.
VSP_035569
Alternative sequence604 – 61411Missing in isoform R.
VSP_035570
Natural variant341R → Q. Ref.6
Corresponds to variant rs17881553 [ dbSNP | Ensembl ].
VAR_021325
Natural variant1351P → A. Ref.6
Corresponds to variant rs17885778 [ dbSNP | Ensembl ].
VAR_021326
Natural variant3331V → E.
Corresponds to variant rs8286 [ dbSNP | Ensembl ].
VAR_011934
Natural variant3531H → N in Yt(b) antigen. Ref.6 Ref.18
Corresponds to variant rs1799805 [ dbSNP | Ensembl ].
VAR_002359

Experimental info

Mutagenesis2061D → N: Misfolding, absence of secretion. Ref.13
Mutagenesis2341S → A: Loss of activity. Ref.13
Mutagenesis3651E → A: Loss of activity. Ref.13
Mutagenesis4351D → N: Misfolding, absence of secretion. Ref.13
Mutagenesis4781H → A: Loss of activity. Ref.13
Mutagenesis6111C → A: Impairment of interchain disulfide bridge formation. Ref.12
Sequence conflict2791A → T in BAD97163. Ref.5
Sequence conflict4151D → G in BAD97163. Ref.5
Sequence conflict4861F → L in AAI43470. Ref.9
Isoform H:
Sequence conflict5921P → R in AAI43470. Ref.9

Secondary structure

........................................................................................................ 614
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform T (ACHE-S) (synaptic) [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: B9AA84C77831C302

FASTA61467,796
        10         20         30         40         50         60 
MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV 

        70         80         90        100        110        120 
SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN 

       130        140        150        160        170        180 
RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM 

       190        200        210        220        230        240 
NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV 

       250        260        270        280        290        300 
GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 

       310        320        330        340        350        360 
VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQVLVG 

       370        380        390        400        410        420 
VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ VSDLAAEAVV LHYTDWLHPE 

       430        440        450        460        470        480 
DPARLREALS DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY 

       490        500        510        520        530        540 
EIEFIFGIPL DPSRNYTAEE KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ 

       550        560        570        580        590        600 
YVSLDLRPLE VRRGLRAQAC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 

       610 
QFDHYSKQDR CSDL 

« Hide

Isoform H (ACHE-E) (erythrocytic) (E4-E5) [UniParc].

Checksum: 7AC0B2536131A89D
Show »

FASTA61767,376
Isoform R (ACHE-R) (readthrough) [UniParc].

Checksum: 3B65B9B3390C6AB1
Show »

FASTA60365,560
Isoform 4 [UniParc].

Checksum: FB85F41EDFFF39DB
Show »

FASTA52658,352

References

« Hide 'large scale' references
[1]"Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure."
Soreq H., Ben-Aziz R., Prody C.A., Seidman S., Gnatt A., Neville L., Lieman-Hurwitz J., Lev-Lehman E., Ginzberg D., Lipidot-Lifson Y., Zakut H.
Proc. Natl. Acad. Sci. U.S.A. 87:9688-9692(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM T).
[2]"Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins."
Karpel R., Ben Aziz-Aloya R., Sternfeld M., Ehrlich G., Ginzberg D., Tarroni P., Clementi F., Zakut H., Soreq H.
Exp. Cell Res. 210:268-277(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H; R AND T).
[3]Yang L., Zhang X.J.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[4]"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 T).
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
Tissue: Brain.
[6]SeattleSNPs variation discovery resource
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-34; ALA-135 AND ASN-353.
[7]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-546 (ISOFORMS H/R/T).
Tissue: Cerebellum and Hippocampus.
[10]"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 521-614.
[11]"Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase."
Chhajlani V., Derr D., Earles B., Schmell E., August T.
FEBS Lett. 247:279-282(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 256-273; 306-326; 396-422; 465-480 AND 528-551, FUNCTION, TISSUE SPECIFICITY.
Tissue: Erythrocyte.
[12]"The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580-->Ala mutant."
Velan B., Grosfeld H., Kronman C., Leitner M., Gozes Y., Lazar A., Flashner Y., Marcus D., Cohen S., Shafferman A.
J. Biol. Chem. 266:23977-23984(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-611.
[13]"Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding."
Shafferman A., Kronman C., Flashner Y., Leitner M., Grosfeld H., Ordentlich A., Gozes Y., Cohen S., Ariel N., Barak D.
J. Biol. Chem. 267:17640-17648(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-206; SER-234; GLU-365; ASP-435 AND HIS-478.
[14]"Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells."
Yang L., He H.Y., Zhang X.J.
Neurosci. Res. 42:261-268(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"External and internal electrostatic potentials of cholinesterase models."
Felder C.E., Botti S.A., Lifson S., Silman I., Sussman J.L.
J. Mol. Graph. Model. 15:318-327(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 35-574.
[16]"Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II."
Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A., Silman I., Sussman J.L.
Acta Crystallogr. D 56:1385-1394(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-614 IN COMPLEX WITH FASCICULIN-2, GLYCOSYLATION AT ASN-381 AND ASN-495.
[17]"The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix."
Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I.
EMBO J. 23:4394-4405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 575-614 IN COMPLEX WITH COLQ.
[18]"Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism."
Bartels C.F., Zelinski T., Lockridge O.
Am. J. Hum. Genet. 52:928-936(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BLOOD GROUP YT(B) ASN-353.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

Wikipedia

Acetylcholinesterase entry

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55040 mRNA. Translation: AAA68151.1.
S71129 Genomic DNA. Translation: AAC60618.1. Sequence problems.
AF334270 mRNA. Translation: AAO32948.1.
AK291321 mRNA. Translation: BAF84010.1.
AK223443 mRNA. Translation: BAD97163.1.
AY750146 Genomic DNA. Translation: AAU43801.1.
AC011895 Genomic DNA. Translation: AAP22364.1.
AC011895 Genomic DNA. Translation: AAP22365.1.
CH236956 Genomic DNA. Translation: EAL23812.1.
CH236956 Genomic DNA. Translation: EAL23813.1.
CH471091 Genomic DNA. Translation: EAW76461.1.
CH471091 Genomic DNA. Translation: EAW76463.1.
CH471091 Genomic DNA. Translation: EAW76462.1.
BC036813 mRNA. Translation: AAH36813.1.
BC105060 mRNA. Translation: AAI05061.1.
BC105062 mRNA. Translation: AAI05063.1.
BC143469 mRNA. Translation: AAI43470.1.
AF312032 Genomic DNA. Translation: AAK21003.1.
PIRA39256.
RefSeqNP_000656.1. NM_000665.3.
NP_001269378.1. NM_001282449.1.
NP_056646.1. NM_015831.2.
XP_005250414.1. XM_005250357.1.
XP_005250415.1. XM_005250358.1.
UniGeneHs.154495.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B41X-ray2.76A36-574[»]
1F8UX-ray2.90A32-614[»]
1PUVmodel-A37-574[»]
1PUWmodel-A37-574[»]
1VZJX-ray2.35A/B/C/D/E/F/G/H575-614[»]
2CLJmodel-A32-574[»]
2X8BX-ray2.95A32-614[»]
3LIIX-ray3.20A/B35-574[»]
4BDTX-ray3.10A32-614[»]
4EY4X-ray2.16A/B33-574[»]
4EY5X-ray2.30A/B33-574[»]
4EY6X-ray2.40A/B33-574[»]
4EY7X-ray2.35A/B33-574[»]
4EY8X-ray2.60A33-574[»]
4M0EX-ray2.00A/B33-574[»]
4M0FX-ray2.30A/B33-574[»]
ProteinModelPortalP22303.
SMRP22303. Positions 35-573, 575-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106561. 2 interactions.
DIPDIP-1119N.
IntActP22303. 8 interactions.
MINTMINT-149019.

Chemistry

BindingDBP22303.
ChEMBLCHEMBL2095233.
DrugBankDB01122. Ambenonium.
DB00572. Atropine.
DB00122. Choline.
DB01245. Decamethonium.
DB00944. Demecarium bromide.
DB00843. Donepezil.
DB01010. Edrophonium.
DB01364. Ephedrine.
DB00674. Galantamine.
DB00483. Gallamine Triethiodide.
DB00677. Isoflurophate.
DB01400. Neostigmine.
DB00981. Physostigmine.
DB00545. Pyridostigmine.
DB00989. Rivastigmine.
DB00382. Tacrine.
DB01199. Tubocurarine.
GuidetoPHARMACOLOGY2465.

Protein family/group databases

MEROPSS09.979.

PTM databases

PhosphoSiteP22303.

Polymorphism databases

DMDM113037.

2D gel databases

SWISS-2DPAGEP22303.

Proteomic databases

PaxDbP22303.
PRIDEP22303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241069; ENSP00000241069; ENSG00000087085. [P22303-1]
ENST00000302913; ENSP00000303211; ENSG00000087085. [P22303-2]
ENST00000411582; ENSP00000404865; ENSG00000087085. [P22303-2]
ENST00000412389; ENSP00000394976; ENSG00000087085. [P22303-1]
ENST00000419336; ENSP00000403474; ENSG00000087085. [P22303-3]
ENST00000428317; ENSP00000414858; ENSG00000087085. [P22303-1]
GeneID43.
KEGGhsa:43.
UCSCuc003uxd.3. human. [P22303-1]
uc003uxe.3. human. [P22303-2]
uc003uxh.3. human. [P22303-3]

Organism-specific databases

CTD43.
GeneCardsGC07M100487.
HGNCHGNC:108. ACHE.
HPAHPA019704.
MIM100740. gene+phenotype.
112100. phenotype.
neXtProtNX_P22303.
PharmGKBPA20.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2272.
HOVERGENHBG008839.
KOK01049.
OMARPPWCPL.
OrthoDBEOG789C9R.
PhylomeDBP22303.
TreeFamTF315470.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.
REACT_17015. Metabolism of proteins.
SABIO-RKP22303.

Gene expression databases

ArrayExpressP22303.
BgeeP22303.
GenevestigatorP22303.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22303.
GeneWikiAcetylcholinesterase.
GenomeRNAi43.
NextBio173.
PROP22303.
SOURCESearch...

Entry information

Entry nameACES_HUMAN
AccessionPrimary (citable) accession number: P22303
Secondary accession number(s): A4D2E2 expand/collapse secondary AC list , B7ZKZ0, D6W5X7, Q16169, Q29S23, Q2M324, Q504V3, Q53F46, Q86TM9, Q86YX9, Q9BXP7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries