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P22303

- ACES_HUMAN

UniProt

P22303 - ACES_HUMAN

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Protein

Acetylcholinesterase

Gene
ACHE
Organism
Homo sapiens (Human)
Status
Reviewed - 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
Active sitei234 – 2341Acyl-ester intermediate
Active sitei365 – 3651Charge relay system
Active sitei478 – 4781Charge relay system

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 binding Source: UniProtKB
  9. protein homodimerization activity Source: UniProtKB
  10. 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. choline metabolic process Source: RefGenome
  7. DNA replication Source: UniProtKB
  8. glycerophospholipid biosynthetic process Source: Reactome
  9. muscle organ development Source: UniProtKB
  10. negative regulation of synaptic transmission, cholinergic Source: HGNC
  11. nervous system development Source: UniProtKB
  12. neurotransmitter biosynthetic process Source: Reactome
  13. neurotransmitter receptor biosynthetic process Source: Ensembl
  14. osteoblast development Source: HGNC
  15. phosphatidylcholine biosynthetic process Source: Reactome
  16. phospholipid metabolic process Source: Reactome
  17. positive regulation of protein secretion Source: UniProtKB
  18. protein tetramerization Source: Ensembl
  19. receptor internalization Source: Ensembl
  20. regulation of axonogenesis Source: RefGenome
  21. regulation of dendrite morphogenesis Source: RefGenome
  22. regulation of receptor recycling Source: Ensembl
  23. response to wounding Source: UniProtKB
  24. retina development in camera-type eye Source: Ensembl
  25. small molecule metabolic process Source: Reactome
  26. synapse assembly Source: UniProtKB
  27. synaptic transmission Source: Reactome
  28. synaptic transmission, cholinergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen, Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

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: Chromosome 7

Organism-specific databases

HGNCiHGNC:108. ACHE.

Subcellular locationi

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

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. axon Source: RefGenome
  3. basal lamina Source: HGNC
  4. cell junction Source: UniProtKB-KW
  5. cell surface Source: RefGenome
  6. dendrite Source: RefGenome
  7. endoplasmic reticulum lumen Source: RefGenome
  8. extracellular region Source: UniProtKB
  9. extracellular space Source: RefGenome
  10. Golgi apparatus Source: HGNC
  11. membrane Source: HGNC
  12. neuromuscular junction Source: RefGenome
  13. nucleus Source: UniProtKB-SubCell
  14. perinuclear region of cytoplasm Source: HGNC
  15. plasma membrane Source: Reactome
  16. postsynaptic membrane Source: RefGenome
  17. presynaptic membrane Source: RefGenome
  18. 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 – 3131 Reviewed predictionAdd
BLAST
Chaini32 – 614583AcetylcholinesterasePRO_0000008587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi100 ↔ 127
Disulfide bondi288 ↔ 303
Glycosylationi296 – 2961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi381 – 3811N-linked (GlcNAc...)1 Publication
Disulfide bondi440 ↔ 560
Glycosylationi495 – 4951N-linked (GlcNAc...)1 Publication
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

ArrayExpressiP22303.
BgeeiP22303.
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.

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP22303.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
HOVERGENiHBG008839.
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. Align

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

MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG    50
IRLKTPGGPV SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC 100
YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPT SPTPVLVWIY 150
GGGFYSGASS LDVYDGRFLV QAERTVLVSM NYRVGAFGFL ALPGSREAPG 200
NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV GMHLLSPPSR 250
GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 300
VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG 350
DFHGLQVLVG VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ 400
VSDLAAEAVV LHYTDWLHPE DPARLREALS DVVGDHNVVC PVAQLAGRLA 450
AQGARVYAYV FEHRASTLSW PLWMGVPHGY EIEFIFGIPL DPSRNYTAEE 500
KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ YVSLDLRPLE 550
VRRGLRAQAC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 600
QFDHYSKQDR CSDL 614
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.

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

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. VSP_035568Add
BLAST
Alternative sequencei575 – 61440DTLDE…RCSDL → ASEAPSTCPGFTHGEAAPRP GLPLPLLLLHQLLLLFLSHL RRL in isoform H. VSP_001457Add
BLAST
Alternative sequencei575 – 60329DTLDE…KNQFD → GMQGPAGSAGRRGVGARQCN PSLLPLASE in isoform R. VSP_035569Add
BLAST
Alternative sequencei604 – 61411Missing in isoform R. VSP_035570Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791A → T in BAD97163. 1 Publication
Sequence conflicti415 – 4151D → G in BAD97163. 1 Publication
Sequence conflicti486 – 4861F → L in AAI43470. 1 Publication
Isoform H (identifier: P22303-2)
Sequence conflicti592 – 5921P → R in AAI43470. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_000665.3. [P22303-1]
NP_001269378.1. NM_001282449.1. [P22303-3]
NP_056646.1. NM_015831.2. [P22303-2]
XP_005250414.1. XM_005250357.1. [P22303-2]
XP_005250415.1. XM_005250358.1. [P22303-1]
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5709.1. [P22303-1 ]
CCDS5710.1. [P22303-2 ]
CCDS64736.1. [P22303-3 ]
PIRi A39256.
RefSeqi NP_000656.1. NM_000665.3. [P22303-1 ]
NP_001269378.1. NM_001282449.1. [P22303-3 ]
NP_056646.1. NM_015831.2. [P22303-2 ]
XP_005250414.1. XM_005250357.1. [P22303-2 ]
XP_005250415.1. XM_005250358.1. [P22303-1 ]
XP_006716058.1. XM_006715995.1. [P22303-2 ]
UniGenei Hs.154495.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B41 X-ray 2.76 A 36-574 [» ]
1F8U X-ray 2.90 A 32-614 [» ]
1PUV model - A 37-574 [» ]
1PUW model - A 37-574 [» ]
1VZJ X-ray 2.35 A/B/C/D/E/F/G/H 575-614 [» ]
2CLJ model - A 32-574 [» ]
2X8B X-ray 2.95 A 32-614 [» ]
3LII X-ray 3.20 A/B 35-574 [» ]
4BDT X-ray 3.10 A 32-614 [» ]
4EY4 X-ray 2.16 A/B 33-574 [» ]
4EY5 X-ray 2.30 A/B 33-574 [» ]
4EY6 X-ray 2.40 A/B 33-574 [» ]
4EY7 X-ray 2.35 A/B 33-574 [» ]
4EY8 X-ray 2.60 A 33-574 [» ]
4M0E X-ray 2.00 A/B 33-574 [» ]
4M0F X-ray 2.30 A/B 33-574 [» ]
ProteinModelPortali P22303.
SMRi P22303. Positions 35-573, 575-608.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106561. 2 interactions.
DIPi DIP-1119N.
IntActi P22303. 8 interactions.
MINTi MINT-149019.

Chemistry

BindingDBi P22303.
ChEMBLi CHEMBL2095233.
DrugBanki DB01122. 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.
GuidetoPHARMACOLOGYi 2465.

Protein family/group databases

MEROPSi S09.979.

PTM databases

PhosphoSitei P22303.

Polymorphism databases

DMDMi 113037.

2D gel databases

SWISS-2DPAGE P22303.

Proteomic databases

PaxDbi P22303.
PRIDEi P22303.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000241069 ; 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 ]
GeneIDi 43.
KEGGi hsa:43.
UCSCi uc003uxd.3. human. [P22303-1 ]
uc003uxe.3. human. [P22303-2 ]
uc003uxh.3. human. [P22303-3 ]

Organism-specific databases

CTDi 43.
GeneCardsi GC07M100487.
HGNCi HGNC:108. ACHE.
HPAi HPA019704.
MIMi 100740. gene+phenotype.
112100. phenotype.
neXtProti NX_P22303.
PharmGKBi PA20.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2272.
HOVERGENi HBG008839.
KOi K01049.
OMAi RPPWCPL.
OrthoDBi EOG789C9R.
PhylomeDBi P22303.
TreeFami TF315470.

Enzyme and pathway databases

Reactomei REACT_121238. Synthesis of PC.
REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RK P22303.

Miscellaneous databases

EvolutionaryTracei P22303.
GeneWikii Acetylcholinesterase.
GenomeRNAii 43.
NextBioi 173.
PROi P22303.
SOURCEi Search...

Gene expression databases

ArrayExpressi P22303.
Bgeei P22303.
Genevestigatori P22303.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00878. CHOLNESTRASE.
ProDomi PD415333. AChE_tetra. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.
    , 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. 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.

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: September 3, 2014
This is version 162 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

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