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HUMAN:ACES

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) ACHE
Protein Name(s) Acetylcholinesterase

AChE

External Links
UniProt P22303
EMBL M55040
S71129
AF334270
AK291321
AK223443
AY750146
AC011895
AC011895
CH236956
CH236956
CH471091
CH471091
CH471091
BC036813
BC105060
BC105062
BC143469
AF312032
CCDS CCDS5709.1
CCDS5710.1
CCDS64736.1
PIR A39256
RefSeq NP_000656.1
NP_001269378.1
NP_056646.1
XP_006716058.1
UniGene Hs.154495
PDB 1B41
1F8U
1PUV
1PUW
1VZJ
2CLJ
2X8B
3LII
4BDT
4EY4
4EY5
4EY6
4EY7
4EY8
4M0E
4M0F
PDBsum 1B41
1F8U
1PUV
1PUW
1VZJ
2CLJ
2X8B
3LII
4BDT
4EY4
4EY5
4EY6
4EY7
4EY8
4M0E
4M0F
ProteinModelPortal P22303
SMR P22303
BioGrid 106561
DIP DIP-1119N
IntAct P22303
MINT MINT-149019
BindingDB P22303
ChEMBL CHEMBL2095233
DrugBank DB01122
DB00122
DB01245
DB00944
DB00449
DB00843
DB01010
DB01364
DB00674
DB00483
DB00677
DB00358
DB00805
DB01400
DB00981
DB00733
DB00545
DB00989
DB01199
GuidetoPHARMACOLOGY 2465
MEROPS S09.979
PhosphoSite P22303
DMDM 113037
SWISS-2DPAGE P22303
PaxDb P22303
PRIDE P22303
Ensembl ENST00000241069
ENST00000302913
ENST00000411582
ENST00000412389
ENST00000419336
ENST00000428317
GeneID 43
KEGG hsa:43
UCSC uc003uxd.3
uc003uxe.3
uc003uxh.3
CTD 43
GeneCards GC07M100487
HGNC HGNC:108
HPA HPA019704
MIM 100740
112100
neXtProt NX_P22303
PharmGKB PA20
eggNOG COG2272
GeneTree ENSGT00760000118946
HOVERGEN HBG008839
InParanoid P22303
KO K01049
OMA RPPWCPL
OrthoDB EOG789C9R
PhylomeDB P22303
TreeFam TF315470
Reactome REACT_121238
REACT_13583
REACT_19189
SABIO-RK P22303
ChiTaRS ACHE
EvolutionaryTrace P22303
GeneWiki Acetylcholinesterase
GenomeRNAi 43
NextBio 173
PRO PR:P22303
Proteomes UP000005640
Bgee P22303
ExpressionAtlas P22303
Genevestigator P22303
GO GO:0031225
GO:0030424
GO:0005605
GO:0030054
GO:0009986
GO:0030425
GO:0005788
GO:0005576
GO:0005615
GO:0005794
GO:0016020
GO:0031594
GO:0005634
GO:0048471
GO:0005886
GO:0045211
GO:0042734
GO:0045202
GO:0042166
GO:0003990
GO:0001540
GO:0004104
GO:0005518
GO:0016787
GO:0043236
GO:0042803
GO:0017171
GO:0006581
GO:0001507
GO:0042982
GO:0007155
GO:0008283
GO:0019695
GO:0006260
GO:0046474
GO:0007517
GO:0032223
GO:0007399
GO:0042136
GO:0045212
GO:0002076
GO:0006656
GO:0006644
GO:0050714
GO:0051262
GO:0031623
GO:0050770
GO:0048814
GO:0001919
GO:0009611
GO:0060041
GO:0044281
GO:0007416
GO:0007268
GO:0007271
Gene3D 3.40.50.1820
InterPro IPR029058
IPR014788
IPR002018
IPR019826
IPR019819
IPR000997
Pfam PF08674
PF00135
PRINTS PR00878
ProDom PD415333
SUPFAM SSF53474
PROSITE PS00122
PS00941

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0050435

beta-amyloid metabolic process

PMID:17140265[1]

ECO:0000314

P

THC is an inhibitor of AChE which leads to a decrease of beta-amyloid accumulation.

complete

involved_in

GO:0120162

positive regulation of cold-induced thermogenesis

PMID:17038428[2]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P21836

P

Seeded From UniProt

complete

enables

GO:0043236

laminin binding

PMID:12524166[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:14766237[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0045202

synapse

PMID:8460160[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:12524166[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P22303

F

Seeded From UniProt

complete

enables

GO:0042166

acetylcholine binding

PMID:8349597[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032223

negative regulation of synaptic transmission, cholinergic

PMID:1517212[7]

ECO:0000305

curator inference used in manual assertion

GO:0006581

P

Seeded From UniProt

complete

enables

GO:0017171

serine hydrolase activity

PMID:3954986[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

PMID:1517212[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16262697[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0007155

cell adhesion

PMID:15454088[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006581

acetylcholine catabolic process

PMID:1517212[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

PMID:15454088[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005604

basement membrane

PMID:16289501[11]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:1517212[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005518

collagen binding

PMID:12524166[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004104

cholinesterase activity

PMID:1517212[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003990

acetylcholinesterase activity

PMID:1517212[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0002076

osteoblast development

PMID:15454088[10]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:1517212[7]

ECO:0000303

author statement without traceable support used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042166

acetylcholine binding

PMID:1517212[7]

ECO:0000303

author statement without traceable support used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003990

acetylcholinesterase activity

PMID:1517212[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0001507

acetylcholine catabolic process in synaptic cleft

PMID:1517212[7]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0052689

carboxylic ester hydrolase activity

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0000592
FB:FBgn0000594
FB:FBgn0010052
MGI:MGI:2142491
MGI:MGI:2148202
MGI:MGI:2443170
MGI:MGI:95420
MGI:MGI:95432
PANTHER:PTN000168392
RGD:2571
RGD:70896
UniProtKB:O00748
WB:WBGene00001578

F

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:95420
PANTHER:PTN000168732

C

Seeded From UniProt

complete

part_of

GO:0043083

synaptic cleft

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001507

C

Seeded From UniProt

complete

involved_in

GO:0120162

positive regulation of cold-induced thermogenesis

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

involved_in

GO:0060041

retina development in camera-type eye

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

involved_in

GO:0051262

protein tetramerization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

involved_in

GO:0045212

neurotransmitter receptor biosynthetic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

part_of

GO:0045202

synapse

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

C

Seeded From UniProt

complete

enables

GO:0043621

protein self-association

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

F

Seeded From UniProt

complete

enables

GO:0043236

laminin binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

F

Seeded From UniProt

complete

involved_in

GO:0031623

receptor internalization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

part_of

GO:0031594

neuromuscular junction

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

C

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

C

Seeded From UniProt

complete

involved_in

GO:0006581

acetylcholine catabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

C

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

C

Seeded From UniProt

complete

part_of

GO:0005604

basement membrane

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

C

Seeded From UniProt

complete

enables

GO:0003990

acetylcholinesterase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

F

Seeded From UniProt

complete

involved_in

GO:0001919

regulation of receptor recycling

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P21836
ensembl:ENSMUSP00000024099

P

Seeded From UniProt

complete

enables

GO:0004104

cholinesterase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000997

F

Seeded From UniProt

complete

enables

GO:0003990

acetylcholinesterase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.7

F

Seeded From UniProt

complete

involved_in

GO:0050714

positive regulation of protein secretion

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042982

amyloid precursor protein metabolic process

PMID:12769797[14]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009611

response to wounding

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008283

cell population proliferation

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007517

muscle organ development

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007416

synapse assembly

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007399

nervous system development

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007155

cell adhesion

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0001540

amyloid-beta binding

PMID:11283752[13]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0042136

neurotransmitter biosynthetic process

Reactome:R-HSA-112311

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006656

phosphatidylcholine biosynthetic process

Reactome:R-HSA-1483191

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

Reactome:R-HSA-372519

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0045202

synapse

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0770
UniProtKB-SubCell:SL-0258

C

Seeded From UniProt

complete

part_of

GO:0031225

anchored component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0336

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

involved_in

GO:0042135

neurotransmitter catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0531

P

Seeded From UniProt

complete

part_of

GO:0030054

cell junction

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0965

C

Seeded From UniProt

complete

enables

GO:0052689

carboxylic ester hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0719

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Eubanks, LM et al. () A molecular link between the active component of marijuana and Alzheimer's disease pathology. Mol. Pharm. 3 773-7 PubMed GONUTS page
  2. Sun, M et al. (2007) Reduced nicotinic receptor function in sympathetic ganglia is responsible for the hypothermia in the acetylcholinesterase knockout mouse. J. Physiol. (Lond.) 578 751-64 PubMed GONUTS page
  3. 3.0 3.1 3.2 Johnson, G & Moore, SW (2003) Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site. Neurosci. Lett. 337 37-40 PubMed GONUTS page
  4. Schallreuter, KU et al. (2004) Activation/deactivation of acetylcholinesterase by H2O2: more evidence for oxidative stress in vitiligo. Biochem. Biophys. Res. Commun. 315 502-8 PubMed GONUTS page
  5. Ben Aziz-Aloya, R et al. (1993) Expression of a human acetylcholinesterase promoter-reporter construct in developing neuromuscular junctions of Xenopus embryos. Proc. Natl. Acad. Sci. U.S.A. 90 2471-5 PubMed GONUTS page
  6. Ordentlich, A et al. (1993) Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket. J. Biol. Chem. 268 17083-95 PubMed GONUTS page
  7. 7.0 7.1 7.2 7.3 7.4 7.5 7.6 7.7 7.8 7.9 Shafferman, A et al. (1992) Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J. Biol. Chem. 267 17640-8 PubMed GONUTS page
  8. Bazelyansky, M et al. (1986) Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry 25 125-30 PubMed GONUTS page
  9. Carvalho, FA et al. (2005) Biochemical characterization of human umbilical vein endothelial cell membrane bound acetylcholinesterase. FEBS J. 272 5584-94 PubMed GONUTS page
  10. 10.0 10.1 10.2 Inkson, CA et al. (2004) Characterization of acetylcholinesterase expression and secretion during osteoblast differentiation. Bone 35 819-27 PubMed GONUTS page
  11. Guerra, M et al. (2005) Acetylcholinesterase and molecular interactions at the neuromuscular junction. Chem. Biol. Interact. 157-158 57-61 PubMed GONUTS page
  12. 12.0 12.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  13. 13.0 13.1 13.2 13.3 13.4 13.5 13.6 13.7 13.8 13.9 Soreq, H & Seidman, S (2001) Acetylcholinesterase--new roles for an old actor. Nat. Rev. Neurosci. 2 294-302 PubMed GONUTS page
  14. Pakaski, M & Kasa, P (2003) Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein. Curr Drug Targets CNS Neurol Disord 2 163-71 PubMed GONUTS page