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P21836

- ACES_MOUSE

UniProt

P21836 - ACES_MOUSE

Protein

Acetylcholinesterase

Gene

Ache

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 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.

    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. acetylcholinesterase activity Source: MGI
    2. carboxylic ester hydrolase activity Source: RefGenome
    3. cholinesterase activity Source: RefGenome
    4. laminin binding Source: MGI
    5. protein self-association Source: MGI
    6. serine hydrolase activity Source: Ensembl

    GO - Biological processi

    1. acetylcholine catabolic process Source: MGI
    2. choline metabolic process Source: RefGenome
    3. neurotransmitter receptor biosynthetic process Source: MGI
    4. osteoblast development Source: Ensembl
    5. protein tetramerization Source: MGI
    6. receptor internalization Source: MGI
    7. regulation of axonogenesis Source: RefGenome
    8. regulation of dendrite morphogenesis Source: RefGenome
    9. regulation of receptor recycling Source: MGI
    10. retina development in camera-type eye Source: MGI
    11. synapse assembly Source: RefGenome
    12. synaptic transmission, cholinergic Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Neurotransmitter degradation

    Enzyme and pathway databases

    ReactomeiREACT_207335. Synthesis of PC.
    SABIO-RKP21836.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:87876. Ache.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. axon Source: RefGenome
    3. basal lamina Source: MGI
    4. cell junction Source: UniProtKB-KW
    5. cell surface Source: MGI
    6. dendrite Source: RefGenome
    7. endoplasmic reticulum lumen Source: RefGenome
    8. extracellular space Source: MGI
    9. Golgi apparatus Source: Ensembl
    10. neuromuscular junction Source: MGI
    11. perinuclear region of cytoplasm Source: Ensembl
    12. plasma membrane Source: MGI
    13. postsynaptic membrane Source: RefGenome
    14. presynaptic membrane Source: RefGenome
    15. synapse Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Secreted, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Add
    BLAST
    Chaini32 – 614583AcetylcholinesterasePRO_0000008588Add
    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...)
    Disulfide bondi440 ↔ 560
    Glycosylationi495 – 4951N-linked (GlcNAc...)
    Disulfide bondi611 – 611InterchainBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP21836.
    PRIDEiP21836.

    PTM databases

    PhosphoSiteiP21836.

    Expressioni

    Tissue specificityi

    Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.

    Gene expression databases

    ArrayExpressiP21836.
    BgeeiP21836.
    CleanExiMM_ACHE.
    GenevestigatoriP21836.

    Interactioni

    Subunit structurei

    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 By similarity. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi197921. 1 interaction.
    IntActiP21836. 2 interactions.
    MINTiMINT-1206315.

    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 – 555
    Beta strandi58 – 6710
    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 – 24511
    Helixi247 – 2504
    Beta strandi254 – 2607
    Beta strandi263 – 2686
    Helixi272 – 28514
    Turni286 – 2905
    Beta strandi291 – 2933
    Helixi297 – 3048
    Beta strandi305 – 3073
    Helixi309 – 3157
    Helixi316 – 3194
    Beta strandi321 – 3233
    Beta strandi336 – 3416
    Helixi343 – 3497
    Beta strandi356 – 3627
    Beta strandi364 – 3663
    Helixi367 – 3704
    Turni371 – 3733
    Beta strandi379 – 3813
    Helixi387 – 39711
    Helixi403 – 41311
    Beta strandi416 – 4183
    Helixi422 – 43716
    Helixi439 – 45113
    Beta strandi455 – 4617
    Helixi472 – 4743
    Turni478 – 4814
    Helixi482 – 4854
    Helixi488 – 4903
    Helixi492 – 4943
    Helixi498 – 51720
    Turni523 – 5253
    Beta strandi526 – 5283
    Turni536 – 5383
    Beta strandi540 – 5478
    Beta strandi550 – 5534
    Helixi557 – 57115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C2BX-ray4.50A35-574[»]
    1C2OX-ray4.20A/B/C/D36-574[»]
    1J06X-ray2.35A/B32-574[»]
    1J07X-ray2.35A/B32-574[»]
    1KU6X-ray2.50A32-580[»]
    1MAAX-ray2.90A/B/C/D32-578[»]
    1MAHX-ray3.20A32-574[»]
    1N5MX-ray2.20A/B32-572[»]
    1N5RX-ray2.25A/B32-574[»]
    1Q83X-ray2.65A/B1-580[»]
    1Q84X-ray2.45A/B1-580[»]
    2C0PX-ray2.50A/B32-574[»]
    2C0QX-ray2.50A/B32-574[»]
    2GYUX-ray2.20A/B32-574[»]
    2GYVX-ray2.50A/B32-574[»]
    2GYWX-ray2.40A/B32-574[»]
    2H9YX-ray2.40A/B32-574[»]
    2HA0X-ray2.20A/B32-574[»]
    2HA2X-ray2.05A/B32-574[»]
    2HA3X-ray2.25A/B32-574[»]
    2HA4X-ray2.56A/B32-574[»]
    2HA5X-ray2.15A/B32-574[»]
    2HA6X-ray2.25A/B32-574[»]
    2HA7X-ray2.66A/B32-574[»]
    2JEYX-ray2.70A/B32-574[»]
    2JEZX-ray2.60A/B32-574[»]
    2JF0X-ray2.50A/B32-574[»]
    2JGEX-ray2.60A/B32-574[»]
    2JGFX-ray2.50A/B32-574[»]
    2JGIX-ray2.90A/B32-574[»]
    2JGJX-ray2.50A/B32-574[»]
    2JGKX-ray2.90A/B32-574[»]
    2JGLX-ray2.60A/B32-574[»]
    2JGMX-ray2.90A/B32-574[»]
    2WHPX-ray2.20A/B32-573[»]
    2WHQX-ray2.15A/B32-574[»]
    2WHRX-ray2.54A/B32-574[»]
    2WLSX-ray2.60A/B32-574[»]
    2WU3X-ray2.70A/B32-574[»]
    2WU4X-ray2.40A/B32-574[»]
    2XUDX-ray2.65A/B32-574[»]
    2XUFX-ray2.55A/B32-575[»]
    2XUGX-ray2.60A/B32-575[»]
    2XUHX-ray2.65A/B32-574[»]
    2XUIX-ray2.60A/B32-574[»]
    2XUJX-ray2.65A/B32-574[»]
    2XUKX-ray2.75A/B32-574[»]
    2XUOX-ray2.80A/B32-574[»]
    2XUPX-ray2.70A/B32-574[»]
    2XUQX-ray2.70A/B32-574[»]
    2Y2UX-ray2.60A/B32-574[»]
    2Y2VX-ray2.45A/B32-574[»]
    3DL4X-ray2.50A/B32-574[»]
    3DL7X-ray2.50A/B32-574[»]
    3ZLTX-ray2.60A/B32-574[»]
    3ZLUX-ray2.60A/B32-574[»]
    3ZLVX-ray2.50A/B32-574[»]
    4A16X-ray2.65A/B/C/D35-574[»]
    4A23X-ray2.40A/B32-574[»]
    4ARAX-ray2.50A/B32-574[»]
    4ARBX-ray2.25A/B32-574[»]
    4B7ZX-ray2.30A/B32-574[»]
    4B80X-ray2.50A/B32-574[»]
    4B81X-ray2.80A/B32-574[»]
    4B82X-ray2.10A/B32-574[»]
    4B83X-ray2.40A/B32-574[»]
    4B84X-ray2.60A/B32-574[»]
    4B85X-ray2.10A/B32-574[»]
    4BC0X-ray3.35A/B/C/D32-574[»]
    4BC1X-ray2.95A/B/C/D32-574[»]
    4BTLX-ray2.50A/B32-574[»]
    ProteinModelPortaliP21836.
    SMRiP21836. Positions 35-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21836.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    HOGENOMiHOG000091866.
    HOVERGENiHBG008839.
    InParanoidiP21836.
    KOiK01049.
    OMAiRPPWCPL.
    OrthoDBiEOG789C9R.
    PhylomeDBiP21836.
    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 (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform T (identifier: P21836-1) [UniParc]FASTAAdd to Basket

    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

    MRPPWYPLHT PSLAFPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG    50
    IRLKAPGGPV SAFLGIPFAE PPVGSRRFMP PEPKRPWSGV LDATTFQNVC 100
    YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPA SPTPVLIWIY 150
    GGGFYSGAAS LDVYDGRFLA QVEGAVLVSM NYRVGTFGFL ALPGSREAPG 200
    NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV GMHILSLPSR 250
    SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL 300
    IACLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPEALINTG 350
    DFQDLQVLVG VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ 400
    ASDLAAEAVV LHYTDWLHPE DPTHLRDAMS AVVGDHNVVC PVAQLAGRLA 450
    AQGARVYAYI FEHRASTLTW PLWMGVPHGY EIEFIFGLPL DPSLNYTTEE 500
    RIFAQRLMKY WTNFARTGDP NDPRDSKSPQ WPPYTTAAQQ YVSLNLKPLE 550
    VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 600
    QFDHYSKQER CSDL 614
    Length:614
    Mass (Da):68,169
    Last modified:May 1, 1991 - v1
    Checksum:i66E2512463C21172
    GO
    Isoform H (identifier: P21836-2)

    Sequence is not available

    Note: No experimental confirmation available.

    Length:
    Mass (Da):

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56518 mRNA. Translation: CAA39867.1.
    AF312033 Genomic DNA. Translation: AAK28816.1.
    BC046327 mRNA. Translation: AAH46327.1.
    CCDSiCCDS19763.1. [P21836-1]
    PIRiJH0314.
    RefSeqiNP_001276939.1. NM_001290010.1. [P21836-1]
    NP_033729.1. NM_009599.4. [P21836-1]
    UniGeneiMm.255464.
    Mm.489229.

    Genome annotation databases

    EnsembliENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328. [P21836-1]
    ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328. [P21836-1]
    GeneIDi11423.
    KEGGimmu:11423.
    UCSCiuc009abt.1. mouse. [P21836-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56518 mRNA. Translation: CAA39867.1 .
    AF312033 Genomic DNA. Translation: AAK28816.1 .
    BC046327 mRNA. Translation: AAH46327.1 .
    CCDSi CCDS19763.1. [P21836-1 ]
    PIRi JH0314.
    RefSeqi NP_001276939.1. NM_001290010.1. [P21836-1 ]
    NP_033729.1. NM_009599.4. [P21836-1 ]
    UniGenei Mm.255464.
    Mm.489229.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C2B X-ray 4.50 A 35-574 [» ]
    1C2O X-ray 4.20 A/B/C/D 36-574 [» ]
    1J06 X-ray 2.35 A/B 32-574 [» ]
    1J07 X-ray 2.35 A/B 32-574 [» ]
    1KU6 X-ray 2.50 A 32-580 [» ]
    1MAA X-ray 2.90 A/B/C/D 32-578 [» ]
    1MAH X-ray 3.20 A 32-574 [» ]
    1N5M X-ray 2.20 A/B 32-572 [» ]
    1N5R X-ray 2.25 A/B 32-574 [» ]
    1Q83 X-ray 2.65 A/B 1-580 [» ]
    1Q84 X-ray 2.45 A/B 1-580 [» ]
    2C0P X-ray 2.50 A/B 32-574 [» ]
    2C0Q X-ray 2.50 A/B 32-574 [» ]
    2GYU X-ray 2.20 A/B 32-574 [» ]
    2GYV X-ray 2.50 A/B 32-574 [» ]
    2GYW X-ray 2.40 A/B 32-574 [» ]
    2H9Y X-ray 2.40 A/B 32-574 [» ]
    2HA0 X-ray 2.20 A/B 32-574 [» ]
    2HA2 X-ray 2.05 A/B 32-574 [» ]
    2HA3 X-ray 2.25 A/B 32-574 [» ]
    2HA4 X-ray 2.56 A/B 32-574 [» ]
    2HA5 X-ray 2.15 A/B 32-574 [» ]
    2HA6 X-ray 2.25 A/B 32-574 [» ]
    2HA7 X-ray 2.66 A/B 32-574 [» ]
    2JEY X-ray 2.70 A/B 32-574 [» ]
    2JEZ X-ray 2.60 A/B 32-574 [» ]
    2JF0 X-ray 2.50 A/B 32-574 [» ]
    2JGE X-ray 2.60 A/B 32-574 [» ]
    2JGF X-ray 2.50 A/B 32-574 [» ]
    2JGI X-ray 2.90 A/B 32-574 [» ]
    2JGJ X-ray 2.50 A/B 32-574 [» ]
    2JGK X-ray 2.90 A/B 32-574 [» ]
    2JGL X-ray 2.60 A/B 32-574 [» ]
    2JGM X-ray 2.90 A/B 32-574 [» ]
    2WHP X-ray 2.20 A/B 32-573 [» ]
    2WHQ X-ray 2.15 A/B 32-574 [» ]
    2WHR X-ray 2.54 A/B 32-574 [» ]
    2WLS X-ray 2.60 A/B 32-574 [» ]
    2WU3 X-ray 2.70 A/B 32-574 [» ]
    2WU4 X-ray 2.40 A/B 32-574 [» ]
    2XUD X-ray 2.65 A/B 32-574 [» ]
    2XUF X-ray 2.55 A/B 32-575 [» ]
    2XUG X-ray 2.60 A/B 32-575 [» ]
    2XUH X-ray 2.65 A/B 32-574 [» ]
    2XUI X-ray 2.60 A/B 32-574 [» ]
    2XUJ X-ray 2.65 A/B 32-574 [» ]
    2XUK X-ray 2.75 A/B 32-574 [» ]
    2XUO X-ray 2.80 A/B 32-574 [» ]
    2XUP X-ray 2.70 A/B 32-574 [» ]
    2XUQ X-ray 2.70 A/B 32-574 [» ]
    2Y2U X-ray 2.60 A/B 32-574 [» ]
    2Y2V X-ray 2.45 A/B 32-574 [» ]
    3DL4 X-ray 2.50 A/B 32-574 [» ]
    3DL7 X-ray 2.50 A/B 32-574 [» ]
    3ZLT X-ray 2.60 A/B 32-574 [» ]
    3ZLU X-ray 2.60 A/B 32-574 [» ]
    3ZLV X-ray 2.50 A/B 32-574 [» ]
    4A16 X-ray 2.65 A/B/C/D 35-574 [» ]
    4A23 X-ray 2.40 A/B 32-574 [» ]
    4ARA X-ray 2.50 A/B 32-574 [» ]
    4ARB X-ray 2.25 A/B 32-574 [» ]
    4B7Z X-ray 2.30 A/B 32-574 [» ]
    4B80 X-ray 2.50 A/B 32-574 [» ]
    4B81 X-ray 2.80 A/B 32-574 [» ]
    4B82 X-ray 2.10 A/B 32-574 [» ]
    4B83 X-ray 2.40 A/B 32-574 [» ]
    4B84 X-ray 2.60 A/B 32-574 [» ]
    4B85 X-ray 2.10 A/B 32-574 [» ]
    4BC0 X-ray 3.35 A/B/C/D 32-574 [» ]
    4BC1 X-ray 2.95 A/B/C/D 32-574 [» ]
    4BTL X-ray 2.50 A/B 32-574 [» ]
    ProteinModelPortali P21836.
    SMRi P21836. Positions 35-608.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197921. 1 interaction.
    IntActi P21836. 2 interactions.
    MINTi MINT-1206315.

    Chemistry

    BindingDBi P21836.
    ChEMBLi CHEMBL3198.

    Protein family/group databases

    MEROPSi S09.979.

    PTM databases

    PhosphoSitei P21836.

    Proteomic databases

    PaxDbi P21836.
    PRIDEi P21836.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024099 ; ENSMUSP00000024099 ; ENSMUSG00000023328 . [P21836-1 ]
    ENSMUST00000085934 ; ENSMUSP00000083097 ; ENSMUSG00000023328 . [P21836-1 ]
    GeneIDi 11423.
    KEGGi mmu:11423.
    UCSCi uc009abt.1. mouse. [P21836-1 ]

    Organism-specific databases

    CTDi 43.
    MGIi MGI:87876. Ache.

    Phylogenomic databases

    eggNOGi COG2272.
    HOGENOMi HOG000091866.
    HOVERGENi HBG008839.
    InParanoidi P21836.
    KOi K01049.
    OMAi RPPWCPL.
    OrthoDBi EOG789C9R.
    PhylomeDBi P21836.
    TreeFami TF315470.

    Enzyme and pathway databases

    Reactomei REACT_207335. Synthesis of PC.
    SABIO-RK P21836.

    Miscellaneous databases

    EvolutionaryTracei P21836.
    NextBioi 278674.
    PROi P21836.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21836.
    Bgeei P21836.
    CleanExi MM_ACHE.
    Genevestigatori P21836.

    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 ]
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    Publicationsi

    1. "Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species."
      Rachinsky T.L., Camp S., Li Y., Ekstroem T.J., Newton M., Taylor P.
      Neuron 5:317-327(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Strain: 129/Sv.
    3. "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].
      Tissue: Retina.
    4. "PRiMA: the membrane anchor of acetylcholinesterase in the brain."
      Perrier A.L., Massoulie J., Krejci E.
      Neuron 33:275-285(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRIMA1.
    5. "Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex."
      Bourne Y., Taylor P., Marchot P.
      Cell 83:503-512(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH FASCICULIN.
    6. "Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly."
      Bourne Y., Taylor P., Bougis P.E., Marchot P.
      J. Biol. Chem. 274:2963-2970(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    7. "Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site."
      Bourne Y., Taylor P., Radic Z., Marchot P.
      EMBO J. 22:1-12(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 34-573 IN COMPLEX WITH INHIBITOR.

    Entry informationi

    Entry nameiACES_MOUSE
    AccessioniPrimary (citable) accession number: P21836
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.
    This is the catalytic subunit of an asymmetric or soluble form of ACHE.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3