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Protein

Acetylcholinesterase

Gene

ACHE

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

Functioni

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.4 Publications

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171GalanthamineCombined sources
Binding sitei117 – 1171Huperzine ACombined sources
Binding sitei153 – 1531Huprine W; via amide nitrogenCombined sources
Binding sitei164 – 1641Huperzine ACombined sources
Active sitei234 – 2341Acyl-ester intermediate
Binding sitei234 – 2341Huprine WCombined sources
Active sitei365 – 3651Charge relay system
Binding sitei368 – 3681GalanthamineCombined sources
Binding sitei368 – 3681Huperzine ACombined sources
Binding sitei470 – 4701Huprine WCombined sources
Active sitei478 – 4781Charge relay system
Binding sitei478 – 4781Huprine W; via carbonyl oxygenCombined sources

GO - Molecular functioni

  1. acetylcholine binding Source: UniProtKB
  2. acetylcholinesterase activity Source: UniProtKB
  3. beta-amyloid binding Source: UniProtKB
  4. cholinesterase activity Source: HGNC
  5. collagen binding Source: HGNC
  6. hydrolase activity Source: HGNC
  7. laminin binding Source: BHF-UCL
  8. protein homodimerization activity Source: UniProtKB
  9. serine hydrolase activity Source: HGNC

GO - Biological processi

  1. acetylcholine catabolic process Source: HGNC
  2. acetylcholine catabolic process in synaptic cleft Source: UniProtKB
  3. amyloid precursor protein metabolic process Source: UniProtKB
  4. cell adhesion Source: UniProtKB
  5. cell proliferation Source: UniProtKB
  6. DNA replication Source: UniProtKB
  7. glycerophospholipid biosynthetic process Source: Reactome
  8. muscle organ development Source: UniProtKB
  9. negative regulation of synaptic transmission, cholinergic Source: HGNC
  10. nervous system development Source: UniProtKB
  11. neurotransmitter biosynthetic process Source: Reactome
  12. neurotransmitter receptor biosynthetic process Source: Ensembl
  13. osteoblast development Source: HGNC
  14. phosphatidylcholine biosynthetic process Source: Reactome
  15. phospholipid metabolic process Source: Reactome
  16. positive regulation of protein secretion Source: UniProtKB
  17. protein tetramerization Source: Ensembl
  18. receptor internalization Source: Ensembl
  19. regulation of receptor recycling Source: Ensembl
  20. response to wounding Source: UniProtKB
  21. retina development in camera-type eye Source: Ensembl
  22. small molecule metabolic process Source: Reactome
  23. synapse assembly Source: UniProtKB
  24. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen, Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

BRENDAi3.1.1.7. 2681.
ReactomeiREACT_121238. Synthesis of PC.
REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKP22303.

Protein family/group databases

MEROPSiS09.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ACHE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:108. ACHE.

Subcellular locationi

Cell junctionsynapse 2 Publications. Secreted By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity
Isoform T : Nucleus
Note: Only observed in apoptotic nuclei.
Isoform H : Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity; Extracellular side By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. basal lamina Source: HGNC
  3. cell junction Source: UniProtKB-KW
  4. cell surface Source: Ensembl
  5. extracellular region Source: UniProtKB
  6. extracellular space Source: GO_Central
  7. Golgi apparatus Source: HGNC
  8. membrane Source: HGNC
  9. neuromuscular junction Source: GO_Central
  10. nucleus Source: UniProtKB-SubCell
  11. perinuclear region of cytoplasm Source: HGNC
  12. plasma membrane Source: Reactome
  13. synapse Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Nucleus, Secreted, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2061D → N: Misfolding, absence of secretion. 1 Publication
Mutagenesisi234 – 2341S → A: Loss of activity. 1 Publication
Mutagenesisi365 – 3651E → A: Loss of activity. 1 Publication
Mutagenesisi435 – 4351D → N: Misfolding, absence of secretion. 1 Publication
Mutagenesisi478 – 4781H → A: Loss of activity. 1 Publication
Mutagenesisi611 – 6111C → A: Impairment of interchain disulfide bridge formation. 1 Publication

Organism-specific databases

MIMi100740. gene+phenotype.
112100. phenotype.
PharmGKBiPA20.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 614583AcetylcholinesterasePRO_0000008587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi100 ↔ 127
Disulfide bondi288 ↔ 303
Glycosylationi296 – 2961N-linked (GlcNAc...)Combined sources
Glycosylationi381 – 3811N-linked (GlcNAc...)Combined sources
Disulfide bondi440 ↔ 560
Glycosylationi495 – 4951N-linked (GlcNAc...)Combined sources
Disulfide bondi611 – 611Interchain

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP22303.
PRIDEiP22303.

2D gel databases

SWISS-2DPAGEP22303.

PTM databases

PhosphoSiteiP22303.

Expressioni

Tissue specificityi

Isoform H is highly expressed in erythrocytes.1 Publication

Gene expression databases

BgeeiP22303.
ExpressionAtlasiP22303. baseline and differential.
GenevestigatoriP22303.

Organism-specific databases

HPAiHPA019704.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COLQQ9Y2152EBI-1637793,EBI-1637847
ENO1P067332EBI-1637793,EBI-353877
GNB2L1P632442EBI-1637793,EBI-296739

Protein-protein interaction databases

BioGridi106561. 2 interactions.
DIPiDIP-1119N.
IntActiP22303. 8 interactions.
MINTiMINT-149019.

Structurei

Secondary structure

1
614
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393Combined sources
Beta strandi40 – 434Combined sources
Beta strandi46 – 494Combined sources
Beta strandi51 – 533Combined sources
Beta strandi60 – 678Combined sources
Helixi74 – 763Combined sources
Beta strandi88 – 925Combined sources
Beta strandi99 – 1013Combined sources
Helixi112 – 1154Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi129 – 1379Combined sources
Beta strandi143 – 1497Combined sources
Turni153 – 1553Combined sources
Helixi162 – 1643Combined sources
Helixi167 – 1737Combined sources
Beta strandi176 – 1805Combined sources
Helixi185 – 1895Combined sources
Beta strandi196 – 1983Combined sources
Helixi202 – 21716Combined sources
Helixi218 – 2214Combined sources
Beta strandi223 – 23311Combined sources
Helixi235 – 24410Combined sources
Helixi247 – 2504Combined sources
Beta strandi254 – 2607Combined sources
Turni266 – 2683Combined sources
Helixi272 – 28514Combined sources
Helixi297 – 30610Combined sources
Helixi309 – 3157Combined sources
Helixi316 – 3194Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi333 – 3419Combined sources
Helixi343 – 3497Combined sources
Beta strandi356 – 3627Combined sources
Beta strandi364 – 3663Combined sources
Helixi367 – 3704Combined sources
Turni371 – 3733Combined sources
Beta strandi379 – 3813Combined sources
Helixi387 – 39711Combined sources
Helixi403 – 41311Combined sources
Helixi422 – 43716Combined sources
Helixi439 – 45113Combined sources
Beta strandi455 – 4617Combined sources
Helixi472 – 4743Combined sources
Turni478 – 4814Combined sources
Helixi482 – 4854Combined sources
Helixi488 – 4903Combined sources
Beta strandi492 – 4943Combined sources
Helixi498 – 51720Combined sources
Beta strandi526 – 5283Combined sources
Turni536 – 5383Combined sources
Beta strandi540 – 5478Combined sources
Beta strandi550 – 5534Combined sources
Helixi557 – 5648Combined sources
Helixi567 – 5726Combined sources
Helixi580 – 60122Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP22303.
SMRiP22303. Positions 35-573, 575-608.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22303.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni233 – 2342Galanthamine bindingCombined sources

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP22303.
KOiK01049.
OMAiRPPWCPL.
OrthoDBiEOG789C9R.
PhylomeDBiP22303.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform T (identifier: P22303-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG
60 70 80 90 100
IRLKTPGGPV SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC
110 120 130 140 150
YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPT SPTPVLVWIY
160 170 180 190 200
GGGFYSGASS LDVYDGRFLV QAERTVLVSM NYRVGAFGFL ALPGSREAPG
210 220 230 240 250
NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV GMHLLSPPSR
260 270 280 290 300
GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL
310 320 330 340 350
VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG
360 370 380 390 400
DFHGLQVLVG VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ
410 420 430 440 450
VSDLAAEAVV LHYTDWLHPE DPARLREALS DVVGDHNVVC PVAQLAGRLA
460 470 480 490 500
AQGARVYAYV FEHRASTLSW PLWMGVPHGY EIEFIFGIPL DPSRNYTAEE
510 520 530 540 550
KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ YVSLDLRPLE
560 570 580 590 600
VRRGLRAQAC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN
610
QFDHYSKQDR CSDL
Length:614
Mass (Da):67,796
Last modified:July 31, 1991 - v1
Checksum:iB9AA84C77831C302
GO
Isoform H (identifier: P22303-2) [UniParc]FASTAAdd to basket

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.Curated

Show »
Length:617
Mass (Da):67,376
Checksum:i7AC0B2536131A89D
GO
Isoform R (identifier: P22303-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:603
Mass (Da):65,560
Checksum:i3B65B9B3390C6AB1
GO
Isoform 4 (identifier: P22303-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     357-444: Missing.

Note: No experimental confirmation available.

Show »
Length:526
Mass (Da):58,352
Checksum:iFB85F41EDFFF39DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791A → T in BAD97163 (Ref. 5) Curated
Sequence conflicti415 – 4151D → G in BAD97163 (Ref. 5) Curated
Sequence conflicti486 – 4861F → L in AAI43470 (PubMed:15489334).Curated
Isoform H (identifier: P22303-2)
Sequence conflicti592 – 5921P → R in AAI43470 (PubMed:15489334).Curated

Polymorphismi

ACHE is responsible for the Yt blood group system [MIMi: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).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341R → Q.1 Publication
Corresponds to variant rs17881553 [ dbSNP | Ensembl ].
VAR_021325
Natural varianti135 – 1351P → A.1 Publication
Corresponds to variant rs17885778 [ dbSNP | Ensembl ].
VAR_021326
Natural varianti333 – 3331V → E.
Corresponds to variant rs8286 [ dbSNP | Ensembl ].
VAR_011934
Natural varianti353 – 3531H → N in Yt(b) antigen. 2 Publications
Corresponds to variant rs1799805 [ dbSNP | Ensembl ].
VAR_002359

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei357 – 44488Missing in isoform 4. 1 PublicationVSP_035568Add
BLAST
Alternative sequencei575 – 61440DTLDE…RCSDL → ASEAPSTCPGFTHGEAAPRP GLPLPLLLLHQLLLLFLSHL RRL in isoform H. 2 PublicationsVSP_001457Add
BLAST
Alternative sequencei575 – 60329DTLDE…KNQFD → GMQGPAGSAGRRGVGARQCN PSLLPLASE in isoform R. 1 PublicationVSP_035569Add
BLAST
Alternative sequencei604 – 61411Missing in isoform R. 1 PublicationVSP_035570Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5709.1. [P22303-1]
CCDS5710.1. [P22303-2]
CCDS64736.1. [P22303-3]
PIRiA39256.
RefSeqiNP_000656.1. NM_000665.4. [P22303-1]
NP_001269378.1. NM_001282449.1. [P22303-3]
NP_001289550.1. NM_001302621.1. [P22303-2]
NP_001289551.1. NM_001302622.1. [P22303-1]
NP_056646.1. NM_015831.2. [P22303-2]
XP_006716058.1. XM_006715995.1. [P22303-2]
UniGeneiHs.154495.

Genome annotation databases

EnsembliENST00000241069; 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]
GeneIDi43.
KEGGihsa:43.
UCSCiuc003uxd.3. human. [P22303-1]
uc003uxe.3. human. [P22303-2]
uc003uxh.3. human. [P22303-3]

Polymorphism databases

DMDMi113037.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

dbRBC/BGMUT

Blood group antigen gene mutation database

Wikipedia

Acetylcholinesterase entry

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5709.1. [P22303-1]
CCDS5710.1. [P22303-2]
CCDS64736.1. [P22303-3]
PIRiA39256.
RefSeqiNP_000656.1. NM_000665.4. [P22303-1]
NP_001269378.1. NM_001282449.1. [P22303-3]
NP_001289550.1. NM_001302621.1. [P22303-2]
NP_001289551.1. NM_001302622.1. [P22303-1]
NP_056646.1. NM_015831.2. [P22303-2]
XP_006716058.1. XM_006715995.1. [P22303-2]
UniGeneiHs.154495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP22303.
SMRiP22303. Positions 35-573, 575-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106561. 2 interactions.
DIPiDIP-1119N.
IntActiP22303. 8 interactions.
MINTiMINT-149019.

Chemistry

BindingDBiP22303.
ChEMBLiCHEMBL2095233.
DrugBankiDB01122. Ambenonium.
DB00122. Choline.
DB01245. Decamethonium.
DB00944. Demecarium.
DB08996. Dimetacrine.
DB00449. Dipivefrin.
DB00843. Donepezil.
DB01010. Edrophonium.
DB01364. Ephedrine.
DB00674. Galantamine.
DB00483. Gallamine Triethiodide.
DB00677. Isoflurophate.
DB00358. Mefloquine.
DB00805. Minaprine.
DB01400. Neostigmine.
DB00981. Physostigmine.
DB00733. Pralidoxime.
DB00545. Pyridostigmine.
DB00989. Rivastigmine.
DB01199. Tubocurarine.
GuidetoPHARMACOLOGYi2465.

Protein family/group databases

MEROPSiS09.979.

PTM databases

PhosphoSiteiP22303.

Polymorphism databases

DMDMi113037.

2D gel databases

SWISS-2DPAGEP22303.

Proteomic databases

PaxDbiP22303.
PRIDEiP22303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241069; 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]
GeneIDi43.
KEGGihsa:43.
UCSCiuc003uxd.3. human. [P22303-1]
uc003uxe.3. human. [P22303-2]
uc003uxh.3. human. [P22303-3]

Organism-specific databases

CTDi43.
GeneCardsiGC07M100487.
HGNCiHGNC:108. ACHE.
HPAiHPA019704.
MIMi100740. gene+phenotype.
112100. phenotype.
neXtProtiNX_P22303.
PharmGKBiPA20.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP22303.
KOiK01049.
OMAiRPPWCPL.
OrthoDBiEOG789C9R.
PhylomeDBiP22303.
TreeFamiTF315470.

Enzyme and pathway databases

BRENDAi3.1.1.7. 2681.
ReactomeiREACT_121238. Synthesis of PC.
REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKP22303.

Miscellaneous databases

ChiTaRSiACHE. human.
EvolutionaryTraceiP22303.
GeneWikiiAcetylcholinesterase.
GenomeRNAii43.
NextBioi173.
PROiP22303.
SOURCEiSearch...

Gene expression databases

BgeeiP22303.
ExpressionAtlasiP22303. baseline and differential.
GenevestigatoriP22303.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1989) [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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H; R AND T).
  3. Yang L., Zhang X.J.
    Submitted (DEC-2000) 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.
    , 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(2003) [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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
    Tissue: Brain.
  6. SeattleSNPs variation discovery resource
    Submitted (AUG-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.
    , 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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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(2003) [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(2000) [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(1988) [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(1990) [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(1991) [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(2001) [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(1996) [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(1999) [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, DISULFIDE BOND.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 575-614 IN COMPLEX WITH COLQ.
  18. "Structural evidence that human acetylcholinesterase inhibited by tabun ages through O-dealkylation."
    Carletti E., Colletier J.P., Dupeux F., Trovaslet M., Masson P., Nachon F.
    J. Med. Chem. 53:4002-4008(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF COMPLEX WITH FASCICULIN-2, DISULFIDE BOND, GLYCOSYLATION AT ASN-381.
  19. "Structures of human acetylcholinesterase in complex with pharmacologically important ligands."
    Cheung J., Rudolph M.J., Burshteyn F., Cassidy M.S., Gary E.N., Love J., Franklin M.C., Height J.J.
    J. Med. Chem. 55:10282-10286(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 35-573 IN COMPLEX WITH FASCICULIN-2; HUPERZINE A; GALANTAMINE AND DONEPEZIL, GLYCOSYLATION AT ASN-381 AND ASN-495, DISULFIDE BOND.
  20. "Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase."
    Nachon F., Carletti E., Ronco C., Trovaslet M., Nicolet Y., Jean L., Renard P.Y.
    Biochem. J. 453:393-399(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 36-598 IN COMPLEX WITH FASCICULIN-2 AND HUPRINE W, DISULFIDE BOND, GLYCOSYLATION AT ASN-381.
  21. "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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BLOOD GROUP YT(B) ASN-353.

Entry informationi

Entry nameiACES_HUMAN
AccessioniPrimary (citable) accession number: P22303
Secondary accession number(s): A4D2E2
, B7ZKZ0, D6W5X7, Q16169, Q29S23, Q2M324, Q504V3, Q53F46, Q86TM9, Q86YX9, Q9BXP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: July 31, 1991
Last modified: March 31, 2015
This is version 169 of the entry and version 1 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. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.