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P22303

- ACES_HUMAN

UniProt

P22303 - ACES_HUMAN

Protein

Acetylcholinesterase

Gene

ACHE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    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

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

    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

    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 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 614583AcetylcholinesterasePRO_0000008587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi100 ↔ 127
    Disulfide bondi288 ↔ 303
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    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.By similarity2 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2791A → T in BAD97163. 1 PublicationCurated
    Sequence conflicti415 – 4151D → G in BAD97163. 1 PublicationCurated
    Sequence conflicti486 – 4861F → L in AAI43470. (PubMed:15489334)Curated
    Isoform H (identifier: P22303-2)
    Sequence conflicti592 – 5921P → R in AAI43470. (PubMed:15489334)Curated

    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. 1 PublicationVSP_035568Add
    BLAST
    Alternative sequencei575 – 61440DTLDE…RCSDL → ASEAPSTCPGFTHGEAAPRP GLPLPLLLLHQLLLLFLSHL RRL in isoform H. 2 PublicationsVSP_001457Add
    BLAST
    Alternative sequencei575 – 60329DTLDE…KNQFD → GMQGPAGSAGRRGVGARQCN PSLLPLASE in isoform R. 1 PublicationVSP_035569Add
    BLAST
    Alternative sequencei604 – 61411Missing in isoform R. 1 PublicationVSP_035570Add
    BLAST

    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

    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: October 1, 2014
    This is version 163 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