Gene_Locus Report

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Gene_locus Report for: human-ACHE

Homo sapiens (Human) acetylcholinesterase

Comment
Acetylcholinesterase (ACHE; EC 3.1.1.7) controls synaptic and neurohumoral cholinergic activity by hydrolyzing the neurotransmitter acetylcholine. ACHE function relies on precise regulation of its expression and localization. In particular, alternative splicing of the 3-prime region of ACHE results in ACHE isoforms with distinct C-terminal peptides that determine posttranslational maturation and oligomeric assembly. Acetylcholinesterase is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. (H322N)


Relationship
Family|ACHE
Block| C
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
191 mutations: Table (e.g. : A127S, A141T, A278P ... more)
80 structures (e.g. : 1B41, 1F8U, 2X8B... more)
Kinetic: human-ACHE



Xenobiotic sensitivity: Hypersensitivity to acetylcholinesterase inhibitors -

3 substrates: 2,6-Dichlorophenolindophenyl-acetate, Acetylcholine, Acetylthiocholine
61 inhibitors (e.g. : 3,5-dihydroxybenzamido-huprine-hybrid-11, 3-butyl-6-benzyloxyphthalide-Mannich-base-7d, 4-aminopyridine-1,3,4-oxadiazole-9... more)
>3 Genbank links 14 more: AAA68151, NP000656, AK223443
>3 UniProt links 6 more: P22303, D6W5X8, D6W5X7
1 Ncbi-nid : 177974
>3 Structure links 77 more: 1B41, 1F8U, 8DT5
>3 UniProt links 5 more: P22303, D6W5X8, C9JZL6
>3 Interpro links 5 more: P22303, D6W5X8, C9JZL6
>3 Prodom links 5 more: P22303, D6W5X8, C9JZL6
>3 Pfam links 5 more: P22303, D6W5X8, C9JZL6
>3 PIRSF links 5 more: P22303, D6W5X8, C9JZL6
>3 SUPERFAM links 5 more: P22303, D6W5X8, C9JZL6
1 EntrezGene : 43
1 SNP : 43
1 UniGene : 154495
1 HUGO HGNC : 108
1 IUPHAR : 2465
2 OMIM : 100740, 112100
1 Ensembl : ENSG00000087085
Sequence
Graphical view for this peptide sequence: human-ACHE
Colored MSA for ACHE (raw)
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRG
IRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVC
YQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIY
GGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPG
NVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSR
GLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAG
DFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQ
VSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLA
AQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEE
KIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLE
VRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRG
IRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVC
YQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIY
GGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPG
NVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSR
GLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAG
DFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQ
VSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLA
AQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEE
KIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLE
VRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL


References
25 more
    Title: A New Class of Bi- and Trifunctional Sugar Oximes as Antidotes against Organophosphorus Poisoning
    Da Silva O, Probst N, Landry C, Hanak AS, Warnault P, Coisne C, Calas AG, Gosselet F, Courageux C and Dias J <7 more author(s)>
    Ref: Journal of Medicinal Chemistry, :, 2022 : PubMed

            

    Title: Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects
    Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radic Z
    Ref: Journal of Biological Chemistry, :101007, 2021 : PubMed

            

    Title: New evidence for dual binding site inhibitors of acetylcholinesterase as improved drugs for treatment of Alzheimer's disease
    Zueva IV, Dias J, Lushchekina SV, Semenov VE, Mukhamedyarov MA, Pashirova TN, Babaev VM, Nachon F, Petrova N and Petrov KA <4 more author(s)>
    Ref: Neuropharmacology, 155:131, 2019 : PubMed

            


Other Papers


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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