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Protein

Cholinesterase

Gene

BCHE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.2 Publications

Catalytic activityi

An acylcholine + H2O = choline + a carboxylate.2 Publications

Enzyme regulationi

Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging.3 Publications

Kineticsi

  1. KM=18.0 µM for butyrylthiocholine (at 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101TacrineCombined sources
    Active sitei226 – 2261Acyl-ester intermediatePROSITE-ProRule annotation1 Publication
    Active sitei353 – 3531Charge relay system1 Publication
    Active sitei466 – 4661Charge relay system1 Publication
    Binding sitei466 – 4661Tacrine; via carbonyl oxygenCombined sources

    GO - Molecular functioni

    • acetylcholinesterase activity Source: UniProtKB
    • beta-amyloid binding Source: UniProtKB
    • catalytic activity Source: UniProtKB
    • choline binding Source: Ensembl
    • cholinesterase activity Source: UniProtKB
    • enzyme binding Source: UniProtKB
    • identical protein binding Source: IntAct

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    BRENDAi3.1.1.8. 2681.
    ReactomeiREACT_121238. Synthesis of PC.
    REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RKP06276.

    Protein family/group databases

    MEROPSiS09.980.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cholinesterase (EC:3.1.1.8)
    Alternative name(s):
    Acylcholine acylhydrolase
    Butyrylcholine esterase
    Choline esterase II
    Pseudocholinesterase
    Gene namesi
    Name:BCHE
    Synonyms:CHE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:983. BCHE.

    Subcellular locationi

    GO - Cellular componenti

    • blood microparticle Source: UniProtKB
    • endoplasmic reticulum lumen Source: Ensembl
    • extracellular region Source: UniProtKB
    • membrane Source: Ensembl
    • nuclear envelope lumen Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Butyrylcholinesterase deficiency (BChE deficiency)24 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA metabolic disorder characterized by prolonged apnea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnea varies significantly depending on the extent of the enzyme deficiency.

    See also OMIM:177400
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321Missing in BChE deficiency. 1 Publication
    VAR_040011
    Natural varianti52 – 521T → M in BChE deficiency. 1 Publication
    Corresponds to variant rs56309853 [ dbSNP | Ensembl ].
    VAR_040012
    Natural varianti56 – 561F → I in BChE deficiency. 1 Publication
    VAR_040013
    Natural varianti61 – 611Y → C in BChE deficiency; enzymatically inactive in the plasma. 1 Publication
    VAR_040014
    Natural varianti62 – 621A → V in BChE deficiency; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of G-98; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of G-98. 1 Publication
    VAR_072730
    Natural varianti65 – 651P → S in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040015
    Natural varianti98 – 981D → G in BChE deficiency; atypical form; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of V-62; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of V-62 or at homozygosity. 6 Publications
    Corresponds to variant rs1799807 [ dbSNP | Ensembl ].
    VAR_002360
    Natural varianti98 – 981D → H in BChE deficiency. 1 Publication
    VAR_040016
    Natural varianti103 – 1031G → R in BChE deficiency; reduced enzyme activity. 2 Publications
    VAR_072095
    Natural varianti118 – 1181E → D in BChE deficiency; the mutant undergoes rapid degradation. 2 Publications
    VAR_072096
    Natural varianti124 – 1241N → Y in BChE deficiency. 1 Publication
    VAR_040017
    Natural varianti128 – 1281P → S in BChE deficiency. 1 Publication
    Corresponds to variant rs3732880 [ dbSNP | Ensembl ].
    VAR_040018
    Natural varianti143 – 1431G → D in BChE deficiency. 1 Publication
    VAR_040019
    Natural varianti153 – 1531L → F in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040020
    Natural varianti156 – 1561Y → C in BChE deficiency. 1 Publication
    VAR_040021
    Natural varianti170 – 1701V → M in BChE deficiency; allele H variant. 1 Publication
    VAR_040022
    Natural varianti198 – 1981D → E in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040023
    Natural varianti226 – 2261S → G in BChE deficiency; enzymatically inactive in the plasma. 1 Publication
    VAR_040024
    Natural varianti227 – 2271A → V in BChE deficiency. 1 Publication
    VAR_040025
    Natural varianti229 – 2291A → T in BChE deficiency; enzymatically inactive in the plasma. 1 Publication
    VAR_040026
    Natural varianti232 – 2321V → D in BChE deficiency. 1 Publication
    VAR_072098
    Natural varianti271 – 2711T → M in BChE deficiency; allele fluoride-1. 2 Publications
    Corresponds to variant rs28933389 [ dbSNP | Ensembl ].
    VAR_040027
    Natural varianti278 – 2781T → P in BChE deficiency. 2 Publications
    VAR_040028
    Natural varianti295 – 2951K → R in BChE deficiency. 1 Publication
    Corresponds to variant rs115624085 [ dbSNP | Ensembl ].
    VAR_040030
    Natural varianti335 – 3351L → P in BChE deficiency; expressed at very low level. 1 Publication
    VAR_040031
    Natural varianti356 – 3561A → D in BChE deficiency. 1 Publication
    VAR_040032
    Natural varianti358 – 3581L → I in BChE deficiency; BChE variant form; fluoride-resistant. 4 Publications
    Corresponds to variant rs121918557 [ dbSNP | Ensembl ].
    VAR_002362
    Natural varianti361 – 3611G → C in BChE deficiency; results in 20% of activity compared to wild-type. 1 Publication
    VAR_072100
    Natural varianti393 – 3931G → R in BChE deficiency. 4 Publications
    Corresponds to variant rs115129687 [ dbSNP | Ensembl ].
    VAR_040033
    Natural varianti414 – 4141R → C in BChE deficiency. 2 Publications
    VAR_040034
    Natural varianti418 – 4181G → V in BChE deficiency; allele fluoride-2. 1 Publication
    Corresponds to variant rs28933390 [ dbSNP | Ensembl ].
    VAR_040035
    Natural varianti446 – 4461F → S in BChE deficiency. 2 Publications
    VAR_040036
    Natural varianti488 – 4881E → K in BChE deficiency. 1 Publication
    VAR_040037
    Natural varianti499 – 4991W → R in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040038
    Natural varianti502 – 5021F → L in BChE deficiency. 1 Publication
    VAR_040039
    Natural varianti525 – 5251E → V in BChE deficiency; allele J variant. 1 Publication
    VAR_040040
    Natural varianti543 – 5431R → C in BChE deficiency. 3 Publications
    VAR_040041
    Natural varianti546 – 5461Q → L in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040042
    Natural varianti567 – 5671A → T in BChE deficiency; allele K variant; with reduced enzyme activity. 4 Publications
    Corresponds to variant rs1803274 [ dbSNP | Ensembl ].
    VAR_002364

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi177400. gene+phenotype.
    Orphaneti132. Butyrylcholinesterase deficiency.
    413693. Curariform drugs toxicity.
    PharmGKBiPA25294.

    Chemistry

    DrugBankiDB08897. Aclidinium.
    DB01122. Ambenonium.
    DB01408. Bambuterol.
    DB01161. Chloroprocaine.
    DB00856. Chlorphenesin.
    DB00477. Chlorpromazine.
    DB00122. Choline.
    DB00527. Cinchocaine.
    DB00515. Cisplatin.
    DB04920. Clevidipine.
    DB00979. Cyclopentolate.
    DB01245. Decamethonium.
    DB00944. Demecarium.
    DB00711. Diethylcarbamazine.
    DB00449. Dipivefrin.
    DB01135. Doxacurium chloride.
    DB01395. Drospirenone.
    DB01057. Echothiophate.
    DB01010. Edrophonium.
    DB01364. Ephedrine.
    DB00392. Ethopropazine.
    DB00674. Galantamine.
    DB00941. Hexafluronium.
    DB00762. Irinotecan.
    DB00677. Isoflurophate.
    DB00772. Malathion.
    DB00358. Mefloquine.
    DB08893. Mirabegron.
    DB01226. Mivacurium.
    DB01400. Neostigmine.
    DB00585. Nizatidine.
    DB00892. Oxybuprocaine.
    DB01337. Pancuronium.
    DB00082. Pegvisomant.
    DB00183. Pentagastrin.
    DB00790. Perindopril.
    DB01338. Pipecuronium.
    DB00733. Pralidoxime.
    DB01035. Procainamide.
    DB00721. Procaine.
    DB00545. Pyridostigmine.
    DB00178. Ramipril.
    DB00989. Rivastigmine.
    DB00202. Succinylcholine.
    DB00391. Sulpiride.
    DB00871. Terbutaline.
    DB00620. Triamcinolone.
    DB00508. Triflupromazine.
    DB01116. Trimethaphan.

    Polymorphism and mutation databases

    BioMutaiBCHE.
    DMDMi116353.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28282 PublicationsAdd
    BLAST
    Chaini29 – 602574CholinesterasePRO_0000008613Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi85 – 851N-linked (GlcNAc...) (complex)9 Publications
    Disulfide bondi93 ↔ 120
    Glycosylationi134 – 1341N-linked (GlcNAc...) (complex)9 Publications
    Modified residuei226 – 2261Phosphoserine1 Publication
    Glycosylationi269 – 2691N-linked (GlcNAc...) (complex)6 Publications
    Disulfide bondi280 ↔ 291
    Glycosylationi284 – 2841N-linked (GlcNAc...) (complex)6 Publications
    Glycosylationi369 – 3691N-linked (GlcNAc...) (complex)9 Publications
    Disulfide bondi428 ↔ 547
    Glycosylationi483 – 4831N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi509 – 5091N-linked (GlcNAc...)3 Publications
    Glycosylationi513 – 5131N-linked (GlcNAc...)7 Publications
    Glycosylationi514 – 5141N-linked (GlcNAc...)3 Publications
    Disulfide bondi599 – 599Interchain

    Post-translational modificationi

    N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type.12 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP06276.
    PaxDbiP06276.
    PRIDEiP06276.

    PTM databases

    PhosphoSiteiP06276.

    Expressioni

    Tissue specificityi

    Detected in blood plasma (at protein level). Present in most cells except erythrocytes.2 Publications

    Gene expression databases

    BgeeiP06276.
    CleanExiHS_BCHE.
    ExpressionAtlasiP06276. baseline and differential.
    GenevestigatoriP06276.

    Organism-specific databases

    HPAiHPA001560.

    Interactioni

    Subunit structurei

    Homotetramer; disulfide-linked. Dimer of dimers.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-7936069,EBI-7936069

    Protein-protein interaction databases

    BioGridi107064. 26 interactions.
    DIPiDIP-46476N.
    STRINGi9606.ENSP00000264381.

    Structurei

    Secondary structure

    1
    602
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 364Combined sources
    Beta strandi39 – 424Combined sources
    Beta strandi44 – 485Combined sources
    Beta strandi51 – 6010Combined sources
    Helixi67 – 693Combined sources
    Beta strandi82 – 854Combined sources
    Helixi105 – 1084Combined sources
    Beta strandi116 – 1183Combined sources
    Beta strandi122 – 1309Combined sources
    Beta strandi133 – 1419Combined sources
    Turni145 – 1473Combined sources
    Helixi154 – 1563Combined sources
    Helixi159 – 1657Combined sources
    Beta strandi168 – 1725Combined sources
    Helixi177 – 1815Combined sources
    Beta strandi190 – 1923Combined sources
    Helixi194 – 20916Combined sources
    Helixi210 – 2134Combined sources
    Beta strandi215 – 22511Combined sources
    Helixi227 – 23711Combined sources
    Helixi239 – 2446Combined sources
    Beta strandi246 – 2527Combined sources
    Turni258 – 2603Combined sources
    Helixi264 – 27714Combined sources
    Helixi285 – 2928Combined sources
    Helixi297 – 3048Combined sources
    Helixi305 – 3073Combined sources
    Beta strandi308 – 3103Combined sources
    Beta strandi324 – 3263Combined sources
    Helixi331 – 3366Combined sources
    Beta strandi345 – 3506Combined sources
    Beta strandi352 – 3543Combined sources
    Helixi355 – 3584Combined sources
    Turni359 – 3613Combined sources
    Beta strandi367 – 3693Combined sources
    Helixi375 – 38511Combined sources
    Beta strandi387 – 3893Combined sources
    Helixi391 – 40111Combined sources
    Turni405 – 4084Combined sources
    Helixi412 – 42514Combined sources
    Helixi427 – 43812Combined sources
    Turni439 – 4413Combined sources
    Beta strandi444 – 4496Combined sources
    Helixi460 – 4623Combined sources
    Turni466 – 4694Combined sources
    Helixi470 – 4734Combined sources
    Helixi476 – 4783Combined sources
    Helixi480 – 4823Combined sources
    Helixi486 – 50520Combined sources
    Turni511 – 5144Combined sources
    Turni523 – 5253Combined sources
    Beta strandi527 – 5315Combined sources
    Beta strandi538 – 5414Combined sources
    Helixi544 – 5518Combined sources
    Turni552 – 5554Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EHOmodel-A30-560[»]
    1EHQmodel-A30-560[»]
    1KCJmodel-A30-560[»]
    1P0IX-ray2.00A29-557[»]
    1P0MX-ray2.38A29-557[»]
    1P0PX-ray2.30A29-557[»]
    1P0QX-ray2.43A29-557[»]
    1XLUX-ray2.20A29-557[»]
    1XLVX-ray2.25A29-557[»]
    1XLWX-ray2.10A29-557[»]
    2J4CX-ray2.75A29-557[»]
    2PM8X-ray2.80A/B29-602[»]
    2WIDX-ray2.30A29-557[»]
    2WIFX-ray2.25A29-557[»]
    2WIGX-ray2.15A29-557[»]
    2WIJX-ray2.10A29-557[»]
    2WIKX-ray2.10A29-557[»]
    2WILX-ray3.10A/B29-557[»]
    2WSLX-ray2.00A29-557[»]
    2XMBX-ray2.10A29-557[»]
    2XMCX-ray2.40A29-557[»]
    2XMDX-ray2.30A29-557[»]
    2XMGX-ray2.70A29-557[»]
    2XQFX-ray2.10A31-557[»]
    2XQGX-ray2.30A31-557[»]
    2XQIX-ray2.60A31-557[»]
    2XQJX-ray2.40A31-557[»]
    2XQKX-ray2.40A31-557[»]
    2Y1KX-ray2.50A29-557[»]
    3DJYX-ray2.10A29-557[»]
    3DKKX-ray2.31A29-557[»]
    3O9MX-ray2.98A/B29-602[»]
    4AQDX-ray2.50A/B29-557[»]
    4AXBX-ray2.40A31-557[»]
    4B0OX-ray2.35A29-557[»]
    4B0PX-ray2.50A29-557[»]
    4BBZX-ray2.70A29-557[»]
    4BDSX-ray2.10A29-557[»]
    4TPKX-ray2.70A/B1-602[»]
    ProteinModelPortaliP06276.
    SMRiP06276. Positions 31-557, 564-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06276.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 1452Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    GeneTreeiENSGT00760000118946.
    HOVERGENiHBG008839.
    InParanoidiP06276.
    KOiK01050.
    OMAiSFNAPWA.
    OrthoDBiEOG789C9R.
    PhylomeDBiP06276.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P06276-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MHSKVTIICI RFLFWFLLLC MLIGKSHTED DIIIATKNGK VRGMNLTVFG
    60 70 80 90 100
    GTVTAFLGIP YAQPPLGRLR FKKPQSLTKW SDIWNATKYA NSCCQNIDQS
    110 120 130 140 150
    FPGFHGSEMW NPNTDLSEDC LYLNVWIPAP KPKNATVLIW IYGGGFQTGT
    160 170 180 190 200
    SSLHVYDGKF LARVERVIVV SMNYRVGALG FLALPGNPEA PGNMGLFDQQ
    210 220 230 240 250
    LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPG SHSLFTRAIL
    260 270 280 290 300
    QSGSFNAPWA VTSLYEARNR TLNLAKLTGC SRENETEIIK CLRNKDPQEI
    310 320 330 340 350
    LLNEAFVVPY GTPLSVNFGP TVDGDFLTDM PDILLELGQF KKTQILVGVN
    360 370 380 390 400
    KDEGTAFLVY GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH
    410 420 430 440 450
    YTDWVDDQRP ENYREALGDV VGDYNFICPA LEFTKKFSEW GNNAFFYYFE
    460 470 480 490 500
    HRSSKLPWPE WMGVMHGYEI EFVFGLPLER RDNYTKAEEI LSRSIVKRWA
    510 520 530 540 550
    NFAKYGNPNE TQNNSTSWPV FKSTEQKYLT LNTESTRIMT KLRAQQCRFW
    560 570 580 590 600
    TSFFPKVLEM TGNIDEAEWE WKAGFHRWNN YMMDWKNQFN DYTSKKESCV

    GL
    Length:602
    Mass (Da):68,418
    Last modified:August 1, 1988 - v1
    Checksum:iC9836409D9057F27
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321Missing in BChE deficiency. 1 Publication
    VAR_040011
    Natural varianti40 – 401K → R Rare polymorphism; does not affect enzymatic activity. 1 Publication
    Corresponds to variant rs116047990 [ dbSNP | Ensembl ].
    VAR_072094
    Natural varianti52 – 521T → M in BChE deficiency. 1 Publication
    Corresponds to variant rs56309853 [ dbSNP | Ensembl ].
    VAR_040012
    Natural varianti56 – 561F → I in BChE deficiency. 1 Publication
    VAR_040013
    Natural varianti61 – 611Y → C in BChE deficiency; enzymatically inactive in the plasma. 1 Publication
    VAR_040014
    Natural varianti62 – 621A → V in BChE deficiency; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of G-98; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of G-98. 1 Publication
    VAR_072730
    Natural varianti65 – 651P → S in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040015
    Natural varianti98 – 981D → G in BChE deficiency; atypical form; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of V-62; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of V-62 or at homozygosity. 6 Publications
    Corresponds to variant rs1799807 [ dbSNP | Ensembl ].
    VAR_002360
    Natural varianti98 – 981D → H in BChE deficiency. 1 Publication
    VAR_040016
    Natural varianti103 – 1031G → R in BChE deficiency; reduced enzyme activity. 2 Publications
    VAR_072095
    Natural varianti118 – 1181E → D in BChE deficiency; the mutant undergoes rapid degradation. 2 Publications
    VAR_072096
    Natural varianti124 – 1241N → Y in BChE deficiency. 1 Publication
    VAR_040017
    Natural varianti127 – 1271I → M Rare polymorphism; does not affect enzyme activity. 2 Publications
    VAR_072097
    Natural varianti128 – 1281P → S in BChE deficiency. 1 Publication
    Corresponds to variant rs3732880 [ dbSNP | Ensembl ].
    VAR_040018
    Natural varianti143 – 1431G → D in BChE deficiency. 1 Publication
    VAR_040019
    Natural varianti153 – 1531L → F in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040020
    Natural varianti156 – 1561Y → C in BChE deficiency. 1 Publication
    VAR_040021
    Natural varianti170 – 1701V → M in BChE deficiency; allele H variant. 1 Publication
    VAR_040022
    Natural varianti198 – 1981D → E in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040023
    Natural varianti226 – 2261S → G in BChE deficiency; enzymatically inactive in the plasma. 1 Publication
    VAR_040024
    Natural varianti227 – 2271A → V in BChE deficiency. 1 Publication
    VAR_040025
    Natural varianti229 – 2291A → T in BChE deficiency; enzymatically inactive in the plasma. 1 Publication
    VAR_040026
    Natural varianti232 – 2321V → D in BChE deficiency. 1 Publication
    VAR_072098
    Natural varianti271 – 2711T → M in BChE deficiency; allele fluoride-1. 2 Publications
    Corresponds to variant rs28933389 [ dbSNP | Ensembl ].
    VAR_040027
    Natural varianti278 – 2781T → P in BChE deficiency. 2 Publications
    VAR_040028
    Natural varianti283 – 2831E → D.
    Corresponds to variant rs16849700 [ dbSNP | Ensembl ].
    VAR_040029
    Natural varianti295 – 2951K → R in BChE deficiency. 1 Publication
    Corresponds to variant rs115624085 [ dbSNP | Ensembl ].
    VAR_040030
    Natural varianti322 – 3221V → M Rare polymorphism; does not affect enzymatic activity. 1 Publication
    VAR_072099
    Natural varianti335 – 3351L → P in BChE deficiency; expressed at very low level. 1 Publication
    VAR_040031
    Natural varianti356 – 3561A → D in BChE deficiency. 1 Publication
    VAR_040032
    Natural varianti358 – 3581L → I in BChE deficiency; BChE variant form; fluoride-resistant. 4 Publications
    Corresponds to variant rs121918557 [ dbSNP | Ensembl ].
    VAR_002362
    Natural varianti361 – 3611G → C in BChE deficiency; results in 20% of activity compared to wild-type. 1 Publication
    VAR_072100
    Natural varianti393 – 3931G → R in BChE deficiency. 4 Publications
    Corresponds to variant rs115129687 [ dbSNP | Ensembl ].
    VAR_040033
    Natural varianti414 – 4141R → C in BChE deficiency. 2 Publications
    VAR_040034
    Natural varianti418 – 4181G → V in BChE deficiency; allele fluoride-2. 1 Publication
    Corresponds to variant rs28933390 [ dbSNP | Ensembl ].
    VAR_040035
    Natural varianti446 – 4461F → S in BChE deficiency. 2 Publications
    VAR_040036
    Natural varianti488 – 4881E → K in BChE deficiency. 1 Publication
    VAR_040037
    Natural varianti498 – 4981R → W Rare polymorphism; does not affect enzymatic activity. 1 Publication
    Corresponds to variant rs115017300 [ dbSNP | Ensembl ].
    VAR_072101
    Natural varianti499 – 4991W → R in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040038
    Natural varianti502 – 5021F → L in BChE deficiency. 1 Publication
    VAR_040039
    Natural varianti525 – 5251E → V in BChE deficiency; allele J variant. 1 Publication
    VAR_040040
    Natural varianti543 – 5431R → C in BChE deficiency. 3 Publications
    VAR_040041
    Natural varianti546 – 5461Q → L in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication
    VAR_040042
    Natural varianti567 – 5671A → T in BChE deficiency; allele K variant; with reduced enzyme activity. 4 Publications
    Corresponds to variant rs1803274 [ dbSNP | Ensembl ].
    VAR_002364

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32391, M32389, M32390 Genomic DNA. Translation: AAA99296.1.
    M16541 mRNA. Translation: AAA98113.1.
    M16474 mRNA. Translation: AAA52015.1.
    AK292063 mRNA. Translation: BAF84752.1.
    BC018141 mRNA. Translation: AAH18141.1.
    CCDSiCCDS3198.1.
    PIRiA33769. ACHU.
    RefSeqiNP_000046.1. NM_000055.2.
    UniGeneiHs.420483.

    Genome annotation databases

    EnsembliENST00000264381; ENSP00000264381; ENSG00000114200.
    GeneIDi590.
    KEGGihsa:590.
    UCSCiuc003fem.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32391, M32389, M32390 Genomic DNA. Translation: AAA99296.1.
    M16541 mRNA. Translation: AAA98113.1.
    M16474 mRNA. Translation: AAA52015.1.
    AK292063 mRNA. Translation: BAF84752.1.
    BC018141 mRNA. Translation: AAH18141.1.
    CCDSiCCDS3198.1.
    PIRiA33769. ACHU.
    RefSeqiNP_000046.1. NM_000055.2.
    UniGeneiHs.420483.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EHOmodel-A30-560[»]
    1EHQmodel-A30-560[»]
    1KCJmodel-A30-560[»]
    1P0IX-ray2.00A29-557[»]
    1P0MX-ray2.38A29-557[»]
    1P0PX-ray2.30A29-557[»]
    1P0QX-ray2.43A29-557[»]
    1XLUX-ray2.20A29-557[»]
    1XLVX-ray2.25A29-557[»]
    1XLWX-ray2.10A29-557[»]
    2J4CX-ray2.75A29-557[»]
    2PM8X-ray2.80A/B29-602[»]
    2WIDX-ray2.30A29-557[»]
    2WIFX-ray2.25A29-557[»]
    2WIGX-ray2.15A29-557[»]
    2WIJX-ray2.10A29-557[»]
    2WIKX-ray2.10A29-557[»]
    2WILX-ray3.10A/B29-557[»]
    2WSLX-ray2.00A29-557[»]
    2XMBX-ray2.10A29-557[»]
    2XMCX-ray2.40A29-557[»]
    2XMDX-ray2.30A29-557[»]
    2XMGX-ray2.70A29-557[»]
    2XQFX-ray2.10A31-557[»]
    2XQGX-ray2.30A31-557[»]
    2XQIX-ray2.60A31-557[»]
    2XQJX-ray2.40A31-557[»]
    2XQKX-ray2.40A31-557[»]
    2Y1KX-ray2.50A29-557[»]
    3DJYX-ray2.10A29-557[»]
    3DKKX-ray2.31A29-557[»]
    3O9MX-ray2.98A/B29-602[»]
    4AQDX-ray2.50A/B29-557[»]
    4AXBX-ray2.40A31-557[»]
    4B0OX-ray2.35A29-557[»]
    4B0PX-ray2.50A29-557[»]
    4BBZX-ray2.70A29-557[»]
    4BDSX-ray2.10A29-557[»]
    4TPKX-ray2.70A/B1-602[»]
    ProteinModelPortaliP06276.
    SMRiP06276. Positions 31-557, 564-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107064. 26 interactions.
    DIPiDIP-46476N.
    STRINGi9606.ENSP00000264381.

    Chemistry

    BindingDBiP06276.
    ChEMBLiCHEMBL2095233.
    DrugBankiDB08897. Aclidinium.
    DB01122. Ambenonium.
    DB01408. Bambuterol.
    DB01161. Chloroprocaine.
    DB00856. Chlorphenesin.
    DB00477. Chlorpromazine.
    DB00122. Choline.
    DB00527. Cinchocaine.
    DB00515. Cisplatin.
    DB04920. Clevidipine.
    DB00979. Cyclopentolate.
    DB01245. Decamethonium.
    DB00944. Demecarium.
    DB00711. Diethylcarbamazine.
    DB00449. Dipivefrin.
    DB01135. Doxacurium chloride.
    DB01395. Drospirenone.
    DB01057. Echothiophate.
    DB01010. Edrophonium.
    DB01364. Ephedrine.
    DB00392. Ethopropazine.
    DB00674. Galantamine.
    DB00941. Hexafluronium.
    DB00762. Irinotecan.
    DB00677. Isoflurophate.
    DB00772. Malathion.
    DB00358. Mefloquine.
    DB08893. Mirabegron.
    DB01226. Mivacurium.
    DB01400. Neostigmine.
    DB00585. Nizatidine.
    DB00892. Oxybuprocaine.
    DB01337. Pancuronium.
    DB00082. Pegvisomant.
    DB00183. Pentagastrin.
    DB00790. Perindopril.
    DB01338. Pipecuronium.
    DB00733. Pralidoxime.
    DB01035. Procainamide.
    DB00721. Procaine.
    DB00545. Pyridostigmine.
    DB00178. Ramipril.
    DB00989. Rivastigmine.
    DB00202. Succinylcholine.
    DB00391. Sulpiride.
    DB00871. Terbutaline.
    DB00620. Triamcinolone.
    DB00508. Triflupromazine.
    DB01116. Trimethaphan.
    GuidetoPHARMACOLOGYi2471.

    Protein family/group databases

    MEROPSiS09.980.

    PTM databases

    PhosphoSiteiP06276.

    Polymorphism and mutation databases

    BioMutaiBCHE.
    DMDMi116353.

    Proteomic databases

    MaxQBiP06276.
    PaxDbiP06276.
    PRIDEiP06276.

    Protocols and materials databases

    DNASUi590.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264381; ENSP00000264381; ENSG00000114200.
    GeneIDi590.
    KEGGihsa:590.
    UCSCiuc003fem.4. human.

    Organism-specific databases

    CTDi590.
    GeneCardsiGC03M165490.
    HGNCiHGNC:983. BCHE.
    HPAiHPA001560.
    MIMi177400. gene+phenotype.
    neXtProtiNX_P06276.
    Orphaneti132. Butyrylcholinesterase deficiency.
    413693. Curariform drugs toxicity.
    PharmGKBiPA25294.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2272.
    GeneTreeiENSGT00760000118946.
    HOVERGENiHBG008839.
    InParanoidiP06276.
    KOiK01050.
    OMAiSFNAPWA.
    OrthoDBiEOG789C9R.
    PhylomeDBiP06276.
    TreeFamiTF315470.

    Enzyme and pathway databases

    BRENDAi3.1.1.8. 2681.
    ReactomeiREACT_121238. Synthesis of PC.
    REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RKP06276.

    Miscellaneous databases

    ChiTaRSiBCHE. human.
    EvolutionaryTraceiP06276.
    GeneWikiiButyrylcholinesterase.
    GenomeRNAii590.
    NextBioi2405.
    PROiP06276.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP06276.
    CleanExiHS_BCHE.
    ExpressionAtlasiP06276. baseline and differential.
    GenevestigatoriP06276.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues."
      Prody C.A., Zevin-Sonkin D., Gnatt A., Goldberg O., Soreq H.
      Proc. Natl. Acad. Sci. U.S.A. 84:3555-3559(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetus.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Structure of the gene for human butyrylcholinesterase. Evidence for a single copy."
      Arpagaus M., Kott M., Vatsis K.P., Bartels C.F., la Du B.N., Lockridge O.
      Biochemistry 29:124-131(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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], VARIANT THR-567.
      Tissue: Stomach.
    5. "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: Skin.
    6. "Complete amino acid sequence of human serum cholinesterase."
      Lockridge O., Bartels C.F., Vaughan T.A., Wong C.K., Norton S.E., Johnson L.L.
      J. Biol. Chem. 262:549-557(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-602, SIGNAL SEQUENCE CLEAVAGE SITE.
      Tissue: Plasma.
    7. "Biochemical, molecular and preclinical characterization of a double-virus-reduced human butyrylcholinesterase preparation designed for clinical use."
      Weber A., Butterweck H., Mais-Paul U., Teschner W., Lei L., Muchitsch E.M., Kolarich D., Altmann F., Ehrlich H.J., Schwarz H.P.
      Vox Sang. 100:285-297(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-37; 43-68; 71-163; 167-290; 294-522; 528-543 AND 549-602, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, HOMOTETRAMERIZATION.
      Tissue: Plasma.
    8. "Location of disulfide bonds within the sequence of human serum cholinesterase."
      Lockridge O., Adkins S., la Du B.N.
      J. Biol. Chem. 262:12945-12952(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
    9. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514.
      Tissue: Plasma.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369; ASN-483; ASN-509 AND ASN-514.
      Tissue: Plasma.
    11. "Glycoproteomic characterization of butyrylcholinesterase from human plasma."
      Kolarich D., Weber A., Pabst M., Stadlmann J., Teschner W., Ehrlich H., Schwarz H.P., Altmann F.
      Proteomics 8:254-263(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-45; ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND ASN-483, CHARACTERIZATION OF GLYCOSYLATION.
    12. "Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents."
      Chilukuri N., Duysen E.G., Parikh K., diTargiani R., Doctor B.P., Lockridge O., Saxena A.
      Mol. Pharmacol. 76:612-617(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284.
      Tissue: Liver.
    14. Cited for: GLYCOSYLATION AT ASN-284.
    15. "The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger."
      Amitay M., Shurki A.
      Proteins 77:370-377(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    16. "Identification of phosphorylated butyrylcholinesterase in human plasma using immunoaffinity purification and mass spectrometry."
      Aryal U.K., Lin C.T., Kim J.S., Heibeck T.H., Wang J., Qian W.J., Lin Y.
      Anal. Chim. Acta 723:68-75(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-226.
    17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "Characterization of a novel BCHE 'silent' allele: point mutation (p.Val204Asp) causes loss of activity and prolonged apnea with suxamethonium."
      Delacour H., Lushchekina S., Mabboux I., Bousquet A., Ceppa F., Schopfer L.M., Lockridge O., Masson P.
      PLoS ONE 9:E101552-E101552(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, VARIANT BCHE DEFICIENCY ASP-232.
    19. "Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products."
      Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., Nachon F.
      J. Biol. Chem. 278:41141-41147(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH SUBSTRATE, SUBUNIT, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, DISULFIDE BONDS, ACTIVE SITE.
    20. "Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging."
      Nachon F., Asojo O.A., Borgstahl G.E.O., Masson P., Lockridge O.
      Biochemistry 44:1154-1162(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH ECHOTHIOPHATE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513.
    21. "Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase."
      Ngamelue M.N., Homma K., Lockridge O., Asojo O.A.
      Acta Crystallogr. F 63:723-727(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134; ASN-369 AND ASN-513, SUBUNIT.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITH MERCURY IONS AND BUTANOIC ACID, DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, ENZYME REGULATION.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-85; ASN-134; ASN-284; ASN-369 AND ASN-513.
    24. "Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun."
      Carletti E., Aurbek N., Gillon E., Loiodice M., Nicolet Y., Fontecilla-Camps J.C., Masson P., Thiermann H., Nachon F., Worek F.
      Biochem. J. 421:97-106(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN ANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND ASN-513, ENZYME REGULATION.
    25. "Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase."
      Nachon F., Carletti E., Ronco C., Trovaslet M., Nicolet Y., Jean L., Renard P.Y.
      Biochem. J. 453:393-399(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH TACRINE, DISULFIDE BOND, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND ASN-513.
    26. "Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase."
      McGuire M.C., Nogueira C.P., Bartels C.F., Lightstone H., Hajra A., van der Spek A.F.L., Lockridge O., la Du B.N.
      Proc. Natl. Acad. Sci. U.S.A. 86:953-957(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY GLY-98.
    27. "DNA mutations associated with the human butyrylcholinesterase J-variant."
      Bartels C.F., James K., La Du B.N.
      Am. J. Hum. Genet. 50:1104-1114(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY VAL-525.
    28. "Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase."
      Nogueira C.P., Bartels C.F., McGuire M.C., Adkins S., Lubrano T., Rubinstein H.M., Lightstone H., Van Der Spek A.F.L., Lockridge O., La Du B.N.
      Am. J. Hum. Genet. 51:821-828(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY MET-271 AND VAL-418.
    29. "A variant serum cholinesterase and a confirmed point mutation at Gly-365 to Arg found in a patient with liver cirrhosis."
      Hada T., Muratani K., Ohue T., Imanishi H., Moriwaki Y., Itoh M., Amuro Y., Higashino K.
      Intern. Med. 31:357-362(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY ARG-393.
    30. "Structural basis of the butyrylcholinesterase H-variant segregating in two Danish families."
      Jensen F.S., Bartels C.F., La Du B.N.
      Pharmacogenetics 2:234-240(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY GLY-98 AND MET-170.
    31. "Genetic basis of the silent phenotype of serum butyrylcholinesterase in three compound heterozygotes."
      Maekawa M., Sudo K., Kanno T., Kotani K., Dey D.C., Ishikawa J., Izumi M., Etoh K.
      Clin. Chim. Acta 235:41-57(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY PRO-278; ARG-393; SER-446; CYS-543 AND THR-567.
    32. "Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia."
      Iida S., Kinoshita M., Fujii H., Moriyama Y., Nakamura Y., Yura N., Moriwaki K.
      Hum. Mutat. 6:349-351(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY ILE-358.
    33. "Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene."
      Primo-Parmo S.L., Bartels C.F., Wiersema B., van der Spek A.F.L., Innis J.W., La Du B.N.
      Am. J. Hum. Genet. 58:52-64(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY CYS-61; SER-65; PHE-153; GLU-198; GLY-226; THR-229; ARG-499 AND LEU-546, CHARACTERIZATION OF VARIANTS BCHE DEFICIENCY SER-65; PHE-153; GLU-198; ARG-499 AND LEU-546.
    34. "Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency."
      Hidaka K., Iuchi I., Tomita M., Watanabe Y., Minatogawa Y., Iwasaki K., Gotoh K., Shimizu C.
      Ann. Hum. Genet. 61:491-496(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY CYS-156.
    35. "Human butyrylcholinesterase L330I mutation belongs to a fluoride-resistant gene, by expression in human fetal kidney cells."
      Sudo K., Maekawa M., Akizuki S., Magara T., Ogasawara H., Tanaka T.
      Biochem. Biophys. Res. Commun. 240:372-375(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BUTYRYLCHOLINESTERASE DEFICIENCY ILE-358.
    36. "Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan."
      Maekawa M., Sudo K., Dey D.C., Ishikawa J., Izumi M., Kotani K., Kanno T.
      Clin. Chem. 43:924-929(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY ILE-32 DEL; MET-52; SER-128; PRO-278; ARG-295; ILE-358; ARG-393; SER-446; CYS-543 AND THR-567.
    37. "Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase."
      Primo-Parmo S.L., Lightstone H., La Du B.N.
      Pharmacogenetics 7:27-34(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY GLY-98 AND ASP-143.
    38. "Identification of a point mutation associated with a silent phenotype of human serum butyrylcholinesterase - a case of familial cholinesterasemia."
      Sakamoto N., Hidaka K., Fujisawa T., Maeda M., Iuchi I.
      Clin. Chim. Acta 274:159-166(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY VAL-227.
    39. "Three point mutations of human butyrylcholinesterase in a Japanese family and the alterations of three-dimensional structure."
      Asanuma K., Yagihashi A., Uehara N., Kida T., Watanabe N.
      Clin. Chim. Acta 283:33-42(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY ILE-358; ARG-393 AND CYS-543.
    40. "Naturally occurring mutation, Asp70His, in human butyrylcholinesterase."
      Boeck A.T., Fry D.L., Sastre A., Lockridge O.
      Ann. Clin. Biochem. 39:154-156(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY GLY-98; HIS-98; MET-271 AND THR-567.
    41. "Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population."
      Yen T., Nightingale B.N., Burns J.C., Sullivan D.R., Stewart P.M.
      Clin. Chem. 49:1297-1308(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY ILE-56; TYR-124; CYS-414 AND LYS-488.
    42. "Novel mutations in the BCHE gene in patients with no butyrylcholinesterase activity."
      On-Kei Chan A., Lam C.-W., Tong S.-F., Man Tung C., Yung K., Chan Y.-W., Au K.-M., Yuen Y.-P., Hung C.-T., Ng K.-P., Shek C.-C.
      Clin. Chim. Acta 351:155-159(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY CYS-414 AND LEU-502.
    43. "Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample."
      Souza R.L., Mikami L.R., Maegawa R.O., Chautard-Freire-Maia E.A.
      Mol. Genet. Metab. 84:349-353(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MET-127, VARIANTS BCHE DEFICIENCY GLY-98; ARG-103 AND ASP-118.
    44. "Naturally occurring mutation Leu307Pro of human butyrylcholinesterase in the Vysya community of India."
      Manoharan I., Wieseler S., Layer P.G., Lockridge O., Boopathy R.
      Pharmacogenet. Genomics 16:461-468(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY PRO-335, CHARACTERIZATION OF VARIANT BCHE DEFICIENCY PRO-335.
    45. "Expression of three naturally occurring genetic variants (G75R, E90D, I99M) of the BCHE gene of human butyrylcholinesterase."
      Mikami L.R., Wieseler S., Souza R.L., Schopfer L.M., Lockridge O., Chautard-Freire-Maia E.A.
      Pharmacogenet. Genomics 17:681-685(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT MET-127, CHARACTERIZATION OF VARIANTS BCHE DEFICIENCY ARG-103 AND ASP-118.
    46. "Two novel mutations in the BCHE gene in patients with prolonged duration of action of mivacurium or succinylcholine during anaesthesia."
      Gaetke M.R., Bundgaard J.R., Viby-Mogensen J.
      Pharmacogenet. Genomics 17:995-999(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY ASP-356.
    47. "Five new naturally occurring mutations of the BCHE gene and frequencies of 12 butyrylcholinesterase alleles in a Brazilian population."
      Mikami L.R., Wieseler S., Souza R.L., Schopfer L.M., Nachon F., Lockridge O., Chautard-Freire-Maia E.A.
      Pharmacogenet. Genomics 18:213-218(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BCHE DEFICIENCY CYS-361, VARIANTS ARG-40; MET-322 AND TRP-498, CHARACTERIZATION OF VARIANT BCHE DEFICIENCY CYS-361, CHARACTERIZATION OF VARIANTS ARG-40; MET-322 AND TRP-498.
    48. "Characterization of a novel butyrylcholinesterase point mutation (p.Ala34Val), 'silent' with mivacurium."
      Delacour H., Lushchekina S., Mabboux I., Ceppa F., Masson P., Schopfer L.M., Lockridge O.
      Biochem. Pharmacol. 92:476-483(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BCHE DEFICIENCY VAL-62 AND GLY-98, CHARACTERIZATION OF VARIANTS BCHE DEFICIENCY VAL-62 AND GLY-98.

    Entry informationi

    Entry nameiCHLE_HUMAN
    AccessioniPrimary (citable) accession number: P06276
    Secondary accession number(s): A8K7P8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: August 1, 1988
    Last modified: April 29, 2015
    This is version 168 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. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.