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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)DescriptionActionsGraphical viewLength
Binding sitei117GalanthamineCombined sources1
Binding sitei117Huperzine ACombined sources1
Binding sitei153Huprine W; via amide nitrogenCombined sources1
Binding sitei164Huperzine ACombined sources1
Active sitei234Acyl-ester intermediate1
Binding sitei234Huprine WCombined sources1
Active sitei365Charge relay system1
Binding sitei368GalanthamineCombined sources1
Binding sitei368Huperzine ACombined sources1
Binding sitei470Huprine WCombined sources1
Active sitei478Charge relay system1
Binding sitei478Huprine W; via carbonyl oxygenCombined sources1

GO - Molecular functioni

  • acetylcholine binding Source: UniProtKB
  • acetylcholinesterase activity Source: UniProtKB
  • beta-amyloid binding Source: UniProtKB
  • cholinesterase activity Source: HGNC
  • collagen binding Source: HGNC
  • hydrolase activity Source: HGNC
  • laminin binding Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB
  • serine hydrolase activity Source: HGNC

GO - Biological processi

  • acetylcholine catabolic process Source: HGNC
  • acetylcholine catabolic process in synaptic cleft Source: UniProtKB
  • amyloid precursor protein metabolic process Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • DNA replication Source: UniProtKB
  • muscle organ development Source: UniProtKB
  • negative regulation of synaptic transmission, cholinergic Source: HGNC
  • nervous system development Source: UniProtKB
  • neurotransmitter biosynthetic process Source: Reactome
  • neurotransmitter receptor biosynthetic process Source: Ensembl
  • osteoblast development Source: HGNC
  • phosphatidylcholine biosynthetic process Source: Reactome
  • positive regulation of protein secretion Source: UniProtKB
  • protein tetramerization Source: Ensembl
  • receptor internalization Source: Ensembl
  • regulation of receptor recycling Source: Ensembl
  • response to wounding Source: UniProtKB
  • retina development in camera-type eye Source: Ensembl
  • synapse assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen, Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

BioCyciZFISH:HS01552-MONOMER.
BRENDAi3.1.1.7. 2681.
ReactomeiR-HSA-112311. Neurotransmitter Clearance In The Synaptic Cleft.
R-HSA-1483191. Synthesis of PC.
R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKP22303.
SIGNORiP22303.

Protein family/group databases

ESTHERihuman-ACHE. AChE.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:108. ACHE.

Subcellular locationi

Isoform T :
  • Nucleus

  • Note: Only observed in apoptotic nuclei.
Isoform H :

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • basal lamina Source: HGNC
  • cell junction Source: UniProtKB-KW
  • cell surface Source: Ensembl
  • extracellular region Source: UniProtKB
  • extracellular space Source: GO_Central
  • Golgi apparatus Source: HGNC
  • membrane Source: HGNC
  • neuromuscular junction Source: GO_Central
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: HGNC
  • plasma membrane Source: Reactome
  • synapse Source: HGNC
  • synaptic cleft Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi206D → N: Misfolding, absence of secretion. 1 Publication1
Mutagenesisi234S → A: Loss of activity. 1 Publication1
Mutagenesisi365E → A: Loss of activity. 1 Publication1
Mutagenesisi435D → N: Misfolding, absence of secretion. 1 Publication1
Mutagenesisi478H → A: Loss of activity. 1 Publication1
Mutagenesisi611C → A: Impairment of interchain disulfide bridge formation. 1 Publication1

Organism-specific databases

DisGeNETi43.
MIMi100740. gene+phenotype.
112100. phenotype.
OpenTargetsiENSG00000087085.
PharmGKBiPA20.

Chemistry databases

ChEMBLiCHEMBL220.
DrugBankiDB03128. Acetylcholine.
DB01122. 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.

Polymorphism and mutation databases

BioMutaiACHE.
DMDMi113037.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000000858732 – 614AcetylcholinesteraseAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi100 ↔ 127
Disulfide bondi288 ↔ 303
Glycosylationi296N-linked (GlcNAc...)Combined sources1
Glycosylationi381N-linked (GlcNAc...)Combined sources1
Disulfide bondi440 ↔ 560
Glycosylationi495N-linked (GlcNAc...)Combined sources1
Disulfide bondi611Interchain

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiP22303.
PaxDbiP22303.
PeptideAtlasiP22303.
PRIDEiP22303.

2D gel databases

SWISS-2DPAGEP22303.

PTM databases

iPTMnetiP22303.
PhosphoSitePlusiP22303.

Expressioni

Tissue specificityi

Isoform H is highly expressed in erythrocytes.1 Publication

Gene expression databases

BgeeiENSG00000087085.
ExpressionAtlasiP22303. baseline and differential.
GenevisibleiP22303. HS.

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
RACK1P632442EBI-1637793,EBI-296739

GO - Molecular functioni

  • collagen binding Source: HGNC
  • laminin binding Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi106561. 2 interactors.
DIPiDIP-1119N.
IntActiP22303. 8 interactors.
MINTiMINT-149019.
STRINGi9606.ENSP00000303211.

Chemistry databases

BindingDBiP22303.

Structurei

Secondary structure

1614
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 39Combined sources3
Beta strandi40 – 43Combined sources4
Beta strandi46 – 49Combined sources4
Beta strandi51 – 53Combined sources3
Beta strandi60 – 67Combined sources8
Helixi74 – 76Combined sources3
Beta strandi88 – 92Combined sources5
Beta strandi99 – 101Combined sources3
Helixi112 – 115Combined sources4
Beta strandi123 – 125Combined sources3
Beta strandi129 – 137Combined sources9
Beta strandi143 – 149Combined sources7
Turni153 – 155Combined sources3
Helixi162 – 164Combined sources3
Helixi167 – 173Combined sources7
Beta strandi176 – 180Combined sources5
Helixi185 – 189Combined sources5
Beta strandi196 – 198Combined sources3
Helixi202 – 217Combined sources16
Helixi218 – 221Combined sources4
Beta strandi223 – 233Combined sources11
Helixi235 – 244Combined sources10
Helixi247 – 250Combined sources4
Beta strandi254 – 260Combined sources7
Turni266 – 268Combined sources3
Helixi272 – 285Combined sources14
Beta strandi292 – 294Combined sources3
Helixi297 – 306Combined sources10
Helixi309 – 315Combined sources7
Helixi316 – 319Combined sources4
Beta strandi320 – 322Combined sources3
Beta strandi333 – 341Combined sources9
Helixi343 – 349Combined sources7
Beta strandi356 – 362Combined sources7
Turni363 – 366Combined sources4
Helixi367 – 370Combined sources4
Turni371 – 373Combined sources3
Beta strandi379 – 381Combined sources3
Helixi387 – 397Combined sources11
Helixi403 – 413Combined sources11
Helixi422 – 437Combined sources16
Helixi439 – 451Combined sources13
Beta strandi455 – 461Combined sources7
Helixi472 – 474Combined sources3
Turni478 – 481Combined sources4
Helixi482 – 485Combined sources4
Helixi488 – 490Combined sources3
Beta strandi492 – 494Combined sources3
Helixi498 – 517Combined sources20
Beta strandi526 – 528Combined sources3
Turni536 – 538Combined sources3
Beta strandi540 – 547Combined sources8
Beta strandi550 – 553Combined sources4
Helixi557 – 564Combined sources8
Helixi567 – 572Combined sources6
Helixi580 – 601Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PQEX-ray2.90A32-574[»]
5FOQX-ray2.30A/B32-576[»]
5FPQX-ray2.40A/B33-574[»]
5HF5X-ray2.15A/B33-574[»]
5HF6X-ray2.30A/B33-574[»]
5HF8X-ray2.80A/B33-574[»]
5HF9X-ray2.20A/B33-574[»]
5HFAX-ray2.20A/B33-574[»]
ProteinModelPortaliP22303.
SMRiP22303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22303.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 234Galanthamine bindingCombined sources2

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4389. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP22303.
KOiK01049.
OMAiHYSKQDR.
OrthoDBiEOG091G0I4G.
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:August 1, 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)DescriptionActionsGraphical viewLength
Sequence conflicti279A → T in BAD97163 (Ref. 5) Curated1
Sequence conflicti415D → G in BAD97163 (Ref. 5) Curated1
Sequence conflicti486F → L in AAI43470 (PubMed:15489334).Curated1
Isoform H (identifier: P22303-2)
Sequence conflicti592P → R in AAI43470 (PubMed:15489334).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_02132534R → Q.1 PublicationCorresponds to variant rs17881553dbSNPEnsembl.1
Natural variantiVAR_021326135P → A.1 PublicationCorresponds to variant rs17885778dbSNPEnsembl.1
Natural variantiVAR_011934333V → E.Corresponds to variant rs8286dbSNPEnsembl.1
Natural variantiVAR_002359353H → N in Yt(b) antigen. 2 PublicationsCorresponds to variant rs1799805dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_035568357 – 444Missing in isoform 4. 1 PublicationAdd BLAST88
Alternative sequenceiVSP_001457575 – 614DTLDE…RCSDL → ASEAPSTCPGFTHGEAAPRP GLPLPLLLLHQLLLLFLSHL RRL in isoform H. 2 PublicationsAdd BLAST40
Alternative sequenceiVSP_035569575 – 603DTLDE…KNQFD → GMQGPAGSAGRRGVGARQCN PSLLPLASE in isoform R. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_035570604 – 614Missing in isoform R. 1 PublicationAdd BLAST11

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_006715995.2. [P22303-2]
XP_011514530.1. XM_011516228.2. [P22303-2]
XP_011514531.1. XM_011516229.2. [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.4. human. [P22303-1]

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_006715995.2. [P22303-2]
XP_011514530.1. XM_011516228.2. [P22303-2]
XP_011514531.1. XM_011516229.2. [P22303-2]
UniGeneiHs.154495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PQEX-ray2.90A32-574[»]
5FOQX-ray2.30A/B32-576[»]
5FPQX-ray2.40A/B33-574[»]
5HF5X-ray2.15A/B33-574[»]
5HF6X-ray2.30A/B33-574[»]
5HF8X-ray2.80A/B33-574[»]
5HF9X-ray2.20A/B33-574[»]
5HFAX-ray2.20A/B33-574[»]
ProteinModelPortaliP22303.
SMRiP22303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106561. 2 interactors.
DIPiDIP-1119N.
IntActiP22303. 8 interactors.
MINTiMINT-149019.
STRINGi9606.ENSP00000303211.

Chemistry databases

BindingDBiP22303.
ChEMBLiCHEMBL220.
DrugBankiDB03128. Acetylcholine.
DB01122. 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

ESTHERihuman-ACHE. AChE.
MEROPSiS09.979.

PTM databases

iPTMnetiP22303.
PhosphoSitePlusiP22303.

Polymorphism and mutation databases

BioMutaiACHE.
DMDMi113037.

2D gel databases

SWISS-2DPAGEP22303.

Proteomic databases

EPDiP22303.
PaxDbiP22303.
PeptideAtlasiP22303.
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.4. human. [P22303-1]

Organism-specific databases

CTDi43.
DisGeNETi43.
GeneCardsiACHE.
HGNCiHGNC:108. ACHE.
MIMi100740. gene+phenotype.
112100. phenotype.
neXtProtiNX_P22303.
OpenTargetsiENSG00000087085.
PharmGKBiPA20.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4389. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP22303.
KOiK01049.
OMAiHYSKQDR.
OrthoDBiEOG091G0I4G.
PhylomeDBiP22303.
TreeFamiTF315470.

Enzyme and pathway databases

BioCyciZFISH:HS01552-MONOMER.
BRENDAi3.1.1.7. 2681.
ReactomeiR-HSA-112311. Neurotransmitter Clearance In The Synaptic Cleft.
R-HSA-1483191. Synthesis of PC.
R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKP22303.
SIGNORiP22303.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000087085.
ExpressionAtlasiP22303. baseline and differential.
GenevisibleiP22303. HS.

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...

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: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 2, 2016
This is version 185 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

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 one 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.