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P21836

- ACES_MOUSE

UniProt

P21836 - ACES_MOUSE

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Protein

Acetylcholinesterase

Gene

Ache

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

MaxQBiP21836.
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

BgeeiP21836.
CleanExiMM_ACHE.
ExpressionAtlasiP21836. baseline and differential.
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

        10         20         30         40         50
MRPPWYPLHT PSLAFPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG
60 70 80 90 100
IRLKAPGGPV SAFLGIPFAE PPVGSRRFMP PEPKRPWSGV LDATTFQNVC
110 120 130 140 150
YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPA SPTPVLIWIY
160 170 180 190 200
GGGFYSGAAS LDVYDGRFLA QVEGAVLVSM NYRVGTFGFL ALPGSREAPG
210 220 230 240 250
NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV GMHILSLPSR
260 270 280 290 300
SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL
310 320 330 340 350
IACLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPEALINTG
360 370 380 390 400
DFQDLQVLVG VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ
410 420 430 440 450
ASDLAAEAVV LHYTDWLHPE DPTHLRDAMS AVVGDHNVVC PVAQLAGRLA
460 470 480 490 500
AQGARVYAYI FEHRASTLTW PLWMGVPHGY EIEFIFGLPL DPSLNYTTEE
510 520 530 540 550
RIFAQRLMKY WTNFARTGDP NDPRDSKSPQ WPPYTTAAQQ YVSLNLKPLE
560 570 580 590 600
VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN
610
QFDHYSKQER CSDL
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

MaxQBi P21836.
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

Bgeei P21836.
CleanExi MM_ACHE.
ExpressionAtlasi P21836. baseline and differential.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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