Acetylcholinesterase is a serine hydrolase that rapidly converts acetylcholine to choline and acetate, terminating cholinergic signaling at neuromuscular and neuronal synapses. Alternative C-terminal isoforms form soluble, GPI-anchored or anchoring-protein-associated assemblies. The synaptic T isoform forms tetramers associated with COLQ or PRIMA1, whereas the H isoform forms GPI-anchored dimers. Acetylcholinesterase also binds extracellular matrix proteins and amyloid-beta and has context-dependent non-synaptic roles. Nuclear accumulation occurs in apoptotic cells; it is not the usual location of synaptic acetylcholine hydrolysis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001507 acetylcholine catabolic process in synaptic cleft | NAS PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: AChE hydrolyses acetylcholine released into the synaptic cleft. Reason: Human catalytic-triad mutagenesis and curated reaction chemistry establish the enzymatic step terminating the synaptic signal. This is direct catabolic participation, distinct from receptor desensitization or acetylcholine transport. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0001540 amyloid-beta binding | TAS PMID:11283752 Acetylcholinesterase--new roles for an old actor. | KEEP AS NON CORE | Summary: AChE associates with amyloid-beta in aggregation experiments. Reason: The original review is supplemented by primary experiments: human recombinant AChE promotes amyloid formation, and crosslinking demonstrates AChE–amyloid-beta association. The latter brain-enzyme abstract does not specify the donor species. Retain the interaction as a non-core property without claiming that it establishes a causal human Alzheimer disease pathway. Supporting Evidence: PMID:8608006 bovine brain AChE, as well as the human and mouse recombinant enzyme, accelerates amyloid formation |
| GO:0002076 osteoblast development | IEP PMID:15454088 Characterization of acetylcholinesterase expression and secr... | UNDECIDED | Summary: The osteoblast study establishes expression and adhesion more clearly than osteoblast maturation. Reason: The accessible source reports differentiation-dependent expression/secretion and inhibitor-sensitive adhesion. Those observations do not by themselves distinguish a causal contribution to osteoblast development from a change accompanying differentiation. Full experimental detail needed to settle this more specific process was not recovered; the original IEP assertion is retained for reassessment, not declared false. Supporting Evidence: PMID:15454088 Further analyses revealed differentiation-dependent secretion by osteoblasts |
| GO:0003990 acetylcholinesterase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Human AChE catalyses acetylcholine hydrolysis. Reason: The substrate-specific serine hydrolase activity is established by human enzyme mutagenesis and substrate-pocket experiments. The different machine sources support the same core molecular claim. Original ancestral source: PANTHER:PTN000168471. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0003990 acetylcholinesterase activity | IDA PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: Human AChE catalyses acetylcholine hydrolysis. Reason: The substrate-specific serine hydrolase activity is established by human enzyme mutagenesis and substrate-pocket experiments. The different machine sources support the same core molecular claim. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0003990 acetylcholinesterase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Human AChE catalyses acetylcholine hydrolysis. Reason: The substrate-specific serine hydrolase activity is established by human enzyme mutagenesis and substrate-pocket experiments. The different machine sources support the same core molecular claim. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0003990 acetylcholinesterase activity | IMP PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: Human AChE catalyses acetylcholine hydrolysis. Reason: The substrate-specific serine hydrolase activity is established by human enzyme mutagenesis and substrate-pocket experiments. The different machine sources support the same core molecular claim. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0003990 acetylcholinesterase activity | TAS Reactome:R-HSA-372519 | ACCEPT | Summary: Human AChE catalyses acetylcholine hydrolysis. Reason: The substrate-specific serine hydrolase activity is established by human enzyme mutagenesis and substrate-pocket experiments. The different machine sources support the same core molecular claim. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0004104 cholinesterase activity | IDA PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | MODIFY | Summary: The broader hydrolase annotation can be made acetylcholine specific. Reason: Human target experiments identify acetylcholinesterase activity, an established specific descendant of the original catalytic class. Refine to that already-supported activity; the general term is true and is not being removed as incorrect. Proposed replacements: acetylcholinesterase activity Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0004104 cholinesterase activity | IEA GO_REF:0000120 | MODIFY | Summary: The broader hydrolase annotation can be made acetylcholine specific. Reason: Human target experiments identify acetylcholinesterase activity, an established specific descendant of the original catalytic class. Refine to that already-supported activity; the general term is true and is not being removed as incorrect. Proposed replacements: acetylcholinesterase activity Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0005515 protein binding | IPI PMID:10800960 Hydrophobic protein that copurifies with human brain acetylc... | REMOVE | Summary: The recorded interaction does not specify an informative binding function. Reason: The human caudate copurification remains evidence of an association with the recorded partner. Bare GO:0005515 is removed under the current project protein-binding policy, without denying that experimental association or inventing a more specific functional class. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15526038 The synaptic acetylcholinesterase tetramer assembles around ... | MODIFY | Summary: The COLQ interaction is collagen binding. Reason: The synaptic AChE C-terminal assembly region associates with the proline-rich attachment region of the collagenous anchor COLQ. Use the independently supported partner class, preserving the distinction between binding the anchor and being a collagen subunit. Proposed replacements: collagen binding Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0005515 protein binding | IPI PMID:18194455 Acetylcholinesterase-R increases germ cell apoptosis but enh... | MODIFY | Summary: The readthrough AChE isoform binds the enzyme enolase. Reason: The ENO1 interaction is more informative as enzyme binding. The primary study uses the human AChE-R C-terminal peptide and recombinant AChE-R; peptide-mediated enolase activation is not asserted as a universal activity of all native AChE isoforms. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18194455 Acetylcholinesterase-R increases germ cell apoptosis but enh... | REMOVE | Summary: The RACK1 association does not supply a specific binding activity term. Reason: Retain the primary interaction provenance, including its readthrough-isoform context. RACK1 is a scaffold rather than a protein kinase; its interaction does not justify kinase binding. The uninformative bare protein-binding annotation is removed under current policy. Supporting Evidence: |
| GO:0005518 collagen binding | IDA PMID:12524166 Human acetylcholinesterase binds to mouse laminin-1 and huma... | ACCEPT | Summary: Human AChE directly binds collagen. Reason: Human AChE binding to human collagen IV was measured as a specific saturable interaction; COLQ association independently establishes collagenous anchoring of synaptic forms. Preserve the broad collagen-binding property without conflating these two collagen partners. Supporting Evidence: PMID:12524166 specific saturable binding of biotinylated human AChE to mouse laminin and human collagen |
| GO:0005576 extracellular region | IDA PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: Secreted and extracellularly exposed AChE forms occupy the extracellular region. Reason: Soluble secretion and extracellular matrix/outer-membrane anchoring support the root extracellular claim. These isoform-specific distributions do not warrant replacing every extracellular annotation with the narrower synaptic cleft. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0005576 extracellular region | IEA GO_REF:0000120 | ACCEPT | Summary: Secreted and extracellularly exposed AChE forms occupy the extracellular region. Reason: Soluble secretion and extracellular matrix/outer-membrane anchoring support the root extracellular claim. These isoform-specific distributions do not warrant replacing every extracellular annotation with the narrower synaptic cleft. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0005576 extracellular region | TAS PMID:11283752 Acetylcholinesterase--new roles for an old actor. | ACCEPT | Summary: Secreted and extracellularly exposed AChE forms occupy the extracellular region. Reason: Soluble secretion and extracellular matrix/outer-membrane anchoring support the root extracellular claim. These isoform-specific distributions do not warrant replacing every extracellular annotation with the narrower synaptic cleft. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0005604 basement membrane | IEA GO_REF:0000107 | ACCEPT | Summary: Collagen-tailed synaptic AChE is anchored in the basal lamina. Reason: The COLQ-containing form is an extracellular basal-lamina assembly, unlike the GPI-anchored erythrocyte isoform. Human AChE/COLQ transplantation experiments support targeting, with the recipient frog muscle distinguished from the human recombinant material. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0005604 basement membrane | NAS PMID:16289501 Acetylcholinesterase and molecular interactions at the neuro... | ACCEPT | Summary: Collagen-tailed synaptic AChE is anchored in the basal lamina. Reason: The COLQ-containing form is an extracellular basal-lamina assembly, unlike the GPI-anchored erythrocyte isoform. Human AChE/COLQ transplantation experiments support targeting, with the recipient frog muscle distinguished from the human recombinant material. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: AChE can accumulate in apoptotic nuclei. Reason: PMID:11985878 reports nuclear accumulation in apoptotic human SK-N-SH cells, corroborated by the curated isoform-T localization. Retain this real but conditional, peripheral location rather than treating it as the principal compartment of synaptic acetylcholine hydrolysis. Supporting Evidence: PMID:11985878 in apoptotic SK-N-SH cells, AChE aggregated in the nucleus file:human/ACHE/ACHE-uniprot.txt [Isoform T]: Nucleus. Note=Only observed in CC apoptotic nuclei. |
| GO:0005794 Golgi apparatus | IDA PMID:15454088 Characterization of acetylcholinesterase expression and secr... | KEEP AS NON CORE | Summary: Osteoblastic AChE was observed in the Golgi apparatus. Reason: PMID:15454088 explicitly reports Golgi colocalization in osteoblastic cells together with secretion into conditioned medium. Retain the root Golgi term as a supported peripheral secretory-pathway pool; this does not make the Golgi the core site of synaptic acetylcholine hydrolysis or infer a finer subcompartment. Supporting Evidence: PMID:15454088 AChE colocalised with the Golgi apparatus in osteoblastic cells |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Anchored AChE forms occur at the cell surface and plasma membrane. Reason: GPI anchoring of the H isoform and association of T assemblies with membrane anchors support surface residence. Other soluble or nuclear forms do not negate this isoform-dependent membrane localization. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ file:human/ACHE/ACHE-uniprot.txt [Isoform H]: Cell membrane |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-372519 | ACCEPT | Summary: Anchored AChE forms occur at the cell surface and plasma membrane. Reason: GPI anchoring of the H isoform and association of T assemblies with membrane anchors support surface residence. Other soluble or nuclear forms do not negate this isoform-dependent membrane localization. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ file:human/ACHE/ACHE-uniprot.txt [Isoform H]: Cell membrane |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634834 | ACCEPT | Summary: Anchored AChE forms occur at the cell surface and plasma membrane. Reason: GPI anchoring of the H isoform and association of T assemblies with membrane anchors support surface residence. Other soluble or nuclear forms do not negate this isoform-dependent membrane localization. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ file:human/ACHE/ACHE-uniprot.txt [Isoform H]: Cell membrane |
| GO:0006581 acetylcholine catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: AChE performs the hydrolytic step of acetylcholine catabolism. Reason: The product itself catalyses cleavage to choline and acetate. Choline can then be reused for synthesis, but no physical complex with the choline transporter is required by this annotation. Original ancestral source: PANTHER:PTN000168471. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0006581 acetylcholine catabolic process | IDA PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: AChE performs the hydrolytic step of acetylcholine catabolism. Reason: The product itself catalyses cleavage to choline and acetate. Choline can then be reused for synthesis, but no physical complex with the choline transporter is required by this annotation. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0006581 acetylcholine catabolic process | TAS Reactome:R-HSA-372519 | ACCEPT | Summary: AChE performs the hydrolytic step of acetylcholine catabolism. Reason: The product itself catalyses cleavage to choline and acetate. Choline can then be reused for synthesis, but no physical complex with the choline transporter is required by this annotation. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0007155 cell adhesion | IDA PMID:15454088 Characterization of acetylcholinesterase expression and secr... | KEEP AS NON CORE | Summary: AChE contributes to osteoblastic cell–matrix adhesion in the reported assay. Reason: Blockade of proposed adhesive sites caused a concentration-dependent reduction in cell adhesion. This supports an ancillary adhesion role while keeping pharmacological perturbation and the osteoblastic context distinct from the core neurotransmitter-hydrolysis mechanism. Supporting Evidence: PMID:15454088 blockade of sites thought to be responsible for AChE adhesive properties caused a concentration-dependent decrease in osteoblastic cell adhesion |
| GO:0007399 nervous system development | TAS PMID:11283752 Acetylcholinesterase--new roles for an old actor. | UNDECIDED | Summary: The specific nervous system development contribution remains unresolved in the accessible source. Reason: The cited nonclassical-function review discusses multiple AChE activities, but its full text was not recovered through the normal source pipeline or publisher access. Enzyme catalysis, matrix binding and expression alone do not resolve the particular process assertion. Preserve the curated claim pending its actual experimental basis rather than infer that it is false. Supporting Evidence: |
| GO:0007416 synapse assembly | TAS PMID:11283752 Acetylcholinesterase--new roles for an old actor. | UNDECIDED | Summary: The specific synapse assembly contribution remains unresolved in the accessible source. Reason: The cited nonclassical-function review discusses multiple AChE activities, but its full text was not recovered through the normal source pipeline or publisher access. Enzyme catalysis, matrix binding and expression alone do not resolve the particular process assertion. Preserve the curated claim pending its actual experimental basis rather than infer that it is false. Supporting Evidence: |
| GO:0009986 cell surface | IEA GO_REF:0000107 | ACCEPT | Summary: Anchored AChE forms occur at the cell surface and plasma membrane. Reason: GPI anchoring of the H isoform and association of T assemblies with membrane anchors support surface residence. Other soluble or nuclear forms do not negate this isoform-dependent membrane localization. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ file:human/ACHE/ACHE-uniprot.txt [Isoform H]: Cell membrane |
| GO:0016020 membrane | IDA PMID:16262697 Biochemical characterization of human umbilical vein endothe... | MODIFY | Summary: The membrane-associated endothelial AChE claim can be specified to plasma membrane. Reason: The human endothelial membrane study is consistent with established surface-anchored AChE forms. Refine the general membrane component to the already-supported plasma-membrane location without excluding secreted or intracellular isoforms. Proposed replacements: plasma membrane Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0016787 hydrolase activity | IDA PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | MODIFY | Summary: The broader hydrolase annotation can be made acetylcholine specific. Reason: Human target experiments identify acetylcholinesterase activity, an established specific descendant of the original catalytic class. Refine to that already-supported activity; the general term is true and is not being removed as incorrect. Proposed replacements: acetylcholinesterase activity Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0017171 serine hydrolase activity | IDA PMID:3954986 Fractional diffusion-limited component of reactions catalyze... | MODIFY | Summary: The broader hydrolase annotation can be made acetylcholine specific. Reason: Human target experiments identify acetylcholinesterase activity, an established specific descendant of the original catalytic class. Refine to that already-supported activity; the general term is true and is not being removed as incorrect. Proposed replacements: acetylcholinesterase activity Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0031594 neuromuscular junction | IDA PMID:14702351 C-terminal and heparin-binding domains of collagenic tail su... | ACCEPT | Summary: AChE is localized at neuromuscular junctions. Reason: Synaptic AChE terminates transmission and is concentrated by extracellular anchoring. PMID:14702351 uses recombinant human AChE/COLQ at frog neuromuscular junctions; this is targeting evidence with a heterologous recipient, not an exclusively native-human localization assay. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0031594 neuromuscular junction | IEA GO_REF:0000107 | ACCEPT | Summary: AChE is localized at neuromuscular junctions. Reason: Synaptic AChE terminates transmission and is concentrated by extracellular anchoring. PMID:14702351 uses recombinant human AChE/COLQ at frog neuromuscular junctions; this is targeting evidence with a heterologous recipient, not an exclusively native-human localization assay. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0032223 negative regulation of synaptic transmission, cholinergic | IC PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: AChE limits cholinergic synaptic signaling by hydrolysing its transmitter. Reason: Removal of acetylcholine directly reduces its availability to receptors. This is the immediate chemical mechanism of negative regulation, rather than a claim that every chronic AChE deficiency simply increases all downstream responses. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0042166 acetylcholine binding | IDA PMID:8349597 Dissection of the human acetylcholinesterase active center d... | ACCEPT | Summary: Acetylcholine recognition is integral to AChE catalysis. Reason: Human substrate-pocket mutagenesis and established reaction chemistry support binding of the physiological substrate. This informative small-molecule binding property is integral to the enzyme and is not peripheral simply because catalysis is also annotated. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0042166 acetylcholine binding | NAS PMID:1517212 Mutagenesis of human acetylcholinesterase. Identification of... | ACCEPT | Summary: Acetylcholine recognition is integral to AChE catalysis. Reason: Human substrate-pocket mutagenesis and established reaction chemistry support binding of the physiological substrate. This informative small-molecule binding property is integral to the enzyme and is not peripheral simply because catalysis is also annotated. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: AChE subunits self-associate, including dimeric isoforms. Reason: Curated isoform-specific assembly establishes disulfide-linked H dimers and T dimers/tetramers. The self-association experiment in PMID:12524166 alone suggests pH-dependent nonspecific aggregation and should not be presented as proof of a uniquely physiological dimer; independent assembly evidence supports the claim holistically. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0042803 protein homodimerization activity | IPI PMID:12524166 Human acetylcholinesterase binds to mouse laminin-1 and huma... | ACCEPT | Summary: AChE subunits self-associate, including dimeric isoforms. Reason: Curated isoform-specific assembly establishes disulfide-linked H dimers and T dimers/tetramers. The self-association experiment in PMID:12524166 alone suggests pH-dependent nonspecific aggregation and should not be presented as proof of a uniquely physiological dimer; independent assembly evidence supports the claim holistically. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0042982 amyloid precursor protein metabolic process | TAS PMID:12769797 Role of acetylcholinesterase inhibitors in the metabolism of... | UNDECIDED | Summary: The precise contribution of AChE to APP metabolism is not resolved by the accessible review. Reason: The source discusses AChE-inhibitor effects on APP processing through muscarinic, kinase and secretase-related mechanisms. It does not establish from the accessible text which effect is due to AChE activity versus a drug-specific action. Full context is unavailable; retain uncertainty without requiring direct APP cleavage for all possible process participation. Supporting Evidence: |
| GO:0043083 synaptic cleft | IEA GO_REF:0000108 | ACCEPT | Summary: Synaptic AChE acts within the synaptic cleft. Reason: Extracellularly anchored enzyme hydrolyses acetylcholine between releasing and responding cells. This specific location is retained alongside broader extracellular and synaptic claims. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0043236 laminin binding | IDA PMID:12524166 Human acetylcholinesterase binds to mouse laminin-1 and huma... | KEEP AS NON CORE | Summary: Human AChE binds laminin in a direct biochemical assay. Reason: Biotinylated human enzyme binds mouse laminin saturably, with reported nanomolar affinity. Retain this precise extracellular-matrix binding property as ancillary to transmitter hydrolysis; the mixed species assay and electrostatic sensitivity do not negate measured binding. Supporting Evidence: PMID:12524166 binding of biotinylated human AChE to mouse laminin and human collagen, with K(d) values of 4.9482 nM |
| GO:0043236 laminin binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Human AChE binds laminin in a direct biochemical assay. Reason: Biotinylated human enzyme binds mouse laminin saturably, with reported nanomolar affinity. Retain this precise extracellular-matrix binding property as ancillary to transmitter hydrolysis; the mixed species assay and electrostatic sensitivity do not negate measured binding. Supporting Evidence: PMID:12524166 binding of biotinylated human AChE to mouse laminin and human collagen, with K(d) values of 4.9482 nM |
| GO:0045202 synapse | IBA GO_REF:0000033 | ACCEPT | Summary: AChE is a synaptic enzyme. Reason: Synaptic cleft hydrolysis and anchoring establish the root synapse component, which remains valid alongside its narrower neuromuscular and extracellular locations. Original ancestral source: PANTHER:PTN000168471. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0045202 synapse | IDA PMID:8460160 Expression of a human acetylcholinesterase promoter-reporter... | ACCEPT | Summary: AChE is a synaptic enzyme. Reason: Synaptic cleft hydrolysis and anchoring establish the root synapse component, which remains valid alongside its narrower neuromuscular and extracellular locations. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0045202 synapse | IEA GO_REF:0000120 | ACCEPT | Summary: AChE is a synaptic enzyme. Reason: Synaptic cleft hydrolysis and anchoring establish the root synapse component, which remains valid alongside its narrower neuromuscular and extracellular locations. Supporting Evidence: file:human/ACHE/ACHE-uniprot.txt Reaction=acetylcholine + H2O = choline + acetate + H(+) file:human/ACHE/ACHE-uniprot.txt Isoform H generates GPI-anchored dimers; disulfide CC linked. file:human/ACHE/ACHE-uniprot.txt In the collagen-tailed CC forms, isoform T subunits are associated with a specific collagen, CC COLQ |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:14766237 Activation/deactivation of acetylcholinesterase by H2O2: mor... | UNDECIDED | Summary: The exact perinuclear distribution in the epidermal study remains unverified. Reason: The accessible primary abstract reports human epidermal AChE immunofluorescence and recombinant-enzyme oxidation kinetics, but does not describe the annotated perinuclear compartment. Its full images were not recovered; the specific location is left unresolved without treating secreted or surface AChE as counterevidence. Supporting Evidence: |
| GO:0050714 positive regulation of protein secretion | TAS PMID:11283752 Acetylcholinesterase--new roles for an old actor. | UNDECIDED | Summary: The specific positive regulation of protein secretion contribution remains unresolved in the accessible source. Reason: The cited nonclassical-function review discusses multiple AChE activities, but its full text was not recovered through the normal source pipeline or publisher access. Enzyme catalysis, matrix binding and expression alone do not resolve the particular process assertion. Preserve the curated claim pending its actual experimental basis rather than infer that it is false. Supporting Evidence: |
| GO:0120162 positive regulation of cold-induced thermogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: AChE supports cold-induced thermogenesis through peripheral cholinergic homeostasis. Reason: Full mouse Ache-knockout experiments compare 23 versus 29 degrees C, measure sympathetic-ganglion currents and rescue hypothermia pharmacologically. They support a conserved physiological contribution through control of transmitter exposure and receptor downregulation, not direct heat generation by AChE. The human annotation is a transfer from mouse P21836 and remains bounded by age and species. Supporting Evidence: PMID:17038428 When kept at 23°C in isolation from the mother, AChE-deficient mice were easily distinguishable from their wild-type littermates, not only by their small body size, but also by their severe shivering behaviour. |
| GO:0120162 positive regulation of cold-induced thermogenesis | ISS PMID:17038428 Reduced nicotinic receptor function in sympathetic ganglia i... | KEEP AS NON CORE | Summary: AChE supports cold-induced thermogenesis through peripheral cholinergic homeostasis. Reason: Full mouse Ache-knockout experiments compare 23 versus 29 degrees C, measure sympathetic-ganglion currents and rescue hypothermia pharmacologically. They support a conserved physiological contribution through control of transmitter exposure and receptor downregulation, not direct heat generation by AChE. The human annotation is a transfer from mouse P21836 and remains bounded by age and species. Supporting Evidence: PMID:17038428 When kept at 23°C in isolation from the mother, AChE-deficient mice were easily distinguishable from their wild-type littermates, not only by their small body size, but also by their severe shivering behaviour. |
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