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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)DescriptionActionsGraphical viewLength
    Binding sitei110TacrineCombined sources1
    Active sitei226Acyl-ester intermediatePROSITE-ProRule annotation1 Publication1
    Active sitei353Charge relay system1 Publication1
    Active sitei466Charge relay system1 Publication1
    Binding sitei466Tacrine; via carbonyl oxygenCombined sources1

    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
    • hydrolase activity, acting on ester bonds Source: Reactome

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    BioCyciZFISH:HS03747-MONOMER.
    BRENDAi3.1.1.8. 2681.
    ReactomeiR-HSA-112311. Neurotransmitter Clearance In The Synaptic Cleft.
    R-HSA-1483191. Synthesis of PC.
    R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RKP06276.

    Protein family/group databases

    ESTHERihuman-BCHE. BCHE.
    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
    Proteomesi
    • UP000005640 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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04001132Missing in BChE deficiency. 1 Publication1
    Natural variantiVAR_04001252T → M in BChE deficiency. 1 PublicationCorresponds to variant rs56309853dbSNPEnsembl.1
    Natural variantiVAR_04001356F → I in BChE deficiency. 1 PublicationCorresponds to variant rs531738678dbSNPEnsembl.1
    Natural variantiVAR_04001461Y → C in BChE deficiency; enzymatically inactive in the plasma. 1 PublicationCorresponds to variant rs116097205dbSNPEnsembl.1
    Natural variantiVAR_07273062A → 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 Publication1
    Natural variantiVAR_04001565P → S in BChE deficiency; seems to cause reduced expression of the protein. 1 PublicationCorresponds to variant rs148170012dbSNPEnsembl.1
    Natural variantiVAR_00236098D → 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 PublicationsCorresponds to variant rs1799807dbSNPEnsembl.1
    Natural variantiVAR_04001698D → H in BChE deficiency. 1 Publication1
    Natural variantiVAR_072095103G → R in BChE deficiency; reduced enzyme activity. 2 Publications1
    Natural variantiVAR_072096118E → D in BChE deficiency; the mutant undergoes rapid degradation. 2 Publications1
    Natural variantiVAR_040017124N → Y in BChE deficiency. 1 Publication1
    Natural variantiVAR_040018128P → S in BChE deficiency. 1 PublicationCorresponds to variant rs3732880dbSNPEnsembl.1
    Natural variantiVAR_040019143G → D in BChE deficiency. 1 PublicationCorresponds to variant rs201820739dbSNPEnsembl.1
    Natural variantiVAR_040020153L → F in BChE deficiency; seems to cause reduced expression of the protein. 1 PublicationCorresponds to variant rs747598704dbSNPEnsembl.1
    Natural variantiVAR_040021156Y → C in BChE deficiency. 1 PublicationCorresponds to variant rs121918558dbSNPEnsembl.1
    Natural variantiVAR_040022170V → M in BChE deficiency; allele H variant. 1 PublicationCorresponds to variant rs527843566dbSNPEnsembl.1
    Natural variantiVAR_040023198D → E in BChE deficiency; seems to cause reduced expression of the protein. 1 PublicationCorresponds to variant rs781368801dbSNPEnsembl.1
    Natural variantiVAR_040024226S → G in BChE deficiency; enzymatically inactive in the plasma. 1 PublicationCorresponds to variant rs370077923dbSNPEnsembl.1
    Natural variantiVAR_040025227A → V in BChE deficiency. 1 Publication1
    Natural variantiVAR_040026229A → T in BChE deficiency; enzymatically inactive in the plasma. 1 Publication1
    Natural variantiVAR_072098232V → D in BChE deficiency. 1 Publication1
    Natural variantiVAR_040027271T → M in BChE deficiency; allele fluoride-1. 2 PublicationsCorresponds to variant rs28933389dbSNPEnsembl.1
    Natural variantiVAR_040028278T → P in BChE deficiency. 2 Publications1
    Natural variantiVAR_040030295K → R in BChE deficiency. 1 PublicationCorresponds to variant rs115624085dbSNPEnsembl.1
    Natural variantiVAR_040031335L → P in BChE deficiency; expressed at very low level. 1 PublicationCorresponds to variant rs104893684dbSNPEnsembl.1
    Natural variantiVAR_040032356A → D in BChE deficiency. 1 PublicationCorresponds to variant rs770337031dbSNPEnsembl.1
    Natural variantiVAR_002362358L → I in BChE deficiency; BChE variant form; fluoride-resistant. 4 PublicationsCorresponds to variant rs121918557dbSNPEnsembl.1
    Natural variantiVAR_072100361G → C in BChE deficiency; results in 20% of activity compared to wild-type. 1 Publication1
    Natural variantiVAR_040033393G → R in BChE deficiency. 4 PublicationsCorresponds to variant rs115129687dbSNPEnsembl.1
    Natural variantiVAR_040034414R → C in BChE deficiency. 2 PublicationsCorresponds to variant rs745364489dbSNPEnsembl.1
    Natural variantiVAR_040035418G → V in BChE deficiency; allele fluoride-2. 1 PublicationCorresponds to variant rs28933390dbSNPEnsembl.1
    Natural variantiVAR_040036446F → S in BChE deficiency. 2 Publications1
    Natural variantiVAR_040037488E → K in BChE deficiency. 1 PublicationCorresponds to variant rs200998515dbSNPEnsembl.1
    Natural variantiVAR_040038499W → R in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication1
    Natural variantiVAR_040039502F → L in BChE deficiency. 1 PublicationCorresponds to variant rs769316835dbSNPEnsembl.1
    Natural variantiVAR_040040525E → V in BChE deficiency; allele J variant. 1 PublicationCorresponds to variant rs121918556dbSNPEnsembl.1
    Natural variantiVAR_040041543R → C in BChE deficiency. 3 PublicationsCorresponds to variant rs199660374dbSNPEnsembl.1
    Natural variantiVAR_040042546Q → L in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication1
    Natural variantiVAR_002364567A → T in BChE deficiency; allele K variant; with reduced enzyme activity. 4 PublicationsCorresponds to variant rs1803274dbSNPEnsembl.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi590.
    MalaCardsiBCHE.
    MIMi177400. gene+phenotype.
    OpenTargetsiENSG00000114200.
    Orphaneti132. Butyrylcholinesterase deficiency.
    413693. Curariform drugs toxicity.
    PharmGKBiPA25294.

    Chemistry databases

    ChEMBLiCHEMBL1914.
    DrugBankiDB08897. Aclidinium.
    DB01122. Ambenonium.
    DB01408. Bambuterol.
    DB06774. Capsaicin.
    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.
    DB06756. Glycine betaine.
    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.

    Polymorphism and mutation databases

    BioMutaiBCHE.
    DMDMi116353.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 282 PublicationsAdd BLAST28
    ChainiPRO_000000861329 – 602CholinesteraseAdd BLAST574

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi45N-linked (GlcNAc...) (complex)2 Publications1
    Glycosylationi85N-linked (GlcNAc...) (complex)9 Publications1
    Disulfide bondi93 ↔ 120
    Glycosylationi134N-linked (GlcNAc...) (complex)9 Publications1
    Modified residuei226Phosphoserine1 Publication1
    Glycosylationi269N-linked (GlcNAc...) (complex)6 Publications1
    Disulfide bondi280 ↔ 291
    Glycosylationi284N-linked (GlcNAc...) (complex)6 Publications1
    Glycosylationi369N-linked (GlcNAc...) (complex)9 Publications1
    Disulfide bondi428 ↔ 547
    Glycosylationi483N-linked (GlcNAc...) (complex)2 Publications1
    Glycosylationi509N-linked (GlcNAc...)3 Publications1
    Glycosylationi513N-linked (GlcNAc...)7 Publications1
    Glycosylationi514N-linked (GlcNAc...)3 Publications1
    Disulfide bondi599Interchain

    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

    EPDiP06276.
    MaxQBiP06276.
    PaxDbiP06276.
    PeptideAtlasiP06276.
    PRIDEiP06276.

    PTM databases

    iPTMnetiP06276.
    PhosphoSitePlusiP06276.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000114200.
    CleanExiHS_BCHE.
    ExpressionAtlasiP06276. baseline and differential.
    GenevisibleiP06276. HS.

    Organism-specific databases

    HPAiHPA001560.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

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

    GO - Molecular functioni

    • enzyme binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi107064. 30 interactors.
    DIPiDIP-46476N.
    IntActiP06276. 1 interactor.
    STRINGi9606.ENSP00000264381.

    Chemistry databases

    BindingDBiP06276.

    Structurei

    Secondary structure

    1602
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi33 – 36Combined sources4
    Beta strandi39 – 42Combined sources4
    Beta strandi44 – 48Combined sources5
    Beta strandi51 – 60Combined sources10
    Helixi67 – 69Combined sources3
    Beta strandi82 – 85Combined sources4
    Helixi105 – 108Combined sources4
    Beta strandi116 – 118Combined sources3
    Beta strandi122 – 130Combined sources9
    Beta strandi133 – 141Combined sources9
    Turni145 – 147Combined sources3
    Helixi154 – 156Combined sources3
    Helixi159 – 165Combined sources7
    Beta strandi168 – 172Combined sources5
    Helixi177 – 181Combined sources5
    Beta strandi190 – 192Combined sources3
    Helixi194 – 209Combined sources16
    Helixi210 – 213Combined sources4
    Beta strandi215 – 225Combined sources11
    Helixi227 – 237Combined sources11
    Helixi239 – 244Combined sources6
    Beta strandi246 – 252Combined sources7
    Turni258 – 260Combined sources3
    Helixi264 – 277Combined sources14
    Helixi285 – 292Combined sources8
    Helixi297 – 304Combined sources8
    Helixi305 – 307Combined sources3
    Beta strandi308 – 310Combined sources3
    Beta strandi324 – 326Combined sources3
    Helixi331 – 336Combined sources6
    Beta strandi345 – 350Combined sources6
    Beta strandi352 – 354Combined sources3
    Helixi355 – 358Combined sources4
    Turni359 – 361Combined sources3
    Beta strandi367 – 369Combined sources3
    Helixi375 – 385Combined sources11
    Beta strandi387 – 389Combined sources3
    Helixi391 – 401Combined sources11
    Turni405 – 408Combined sources4
    Helixi412 – 425Combined sources14
    Helixi427 – 438Combined sources12
    Turni439 – 441Combined sources3
    Beta strandi444 – 449Combined sources6
    Helixi460 – 462Combined sources3
    Turni466 – 469Combined sources4
    Helixi470 – 473Combined sources4
    Helixi476 – 478Combined sources3
    Helixi480 – 482Combined sources3
    Helixi486 – 505Combined sources20
    Turni511 – 514Combined sources4
    Turni523 – 525Combined sources3
    Beta strandi527 – 531Combined sources5
    Beta strandi538 – 541Combined sources4
    Helixi544 – 551Combined sources8
    Turni552 – 555Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4XIIX-ray2.70A/B29-572[»]
    5DYTX-ray2.55A/B28-557[»]
    5K5EX-ray2.80A/B29-557[»]
    ProteinModelPortaliP06276.
    SMRiP06276.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06276.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni144 – 145Substrate binding2

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG4389. Eukaryota.
    COG2272. LUCA.
    GeneTreeiENSGT00760000118946.
    HOVERGENiHBG008839.
    InParanoidiP06276.
    KOiK01050.
    OMAiFLGSEMW.
    OrthoDBiEOG091G0I4G.
    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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04001132Missing in BChE deficiency. 1 Publication1
    Natural variantiVAR_07209440K → R Rare polymorphism; does not affect enzymatic activity. 1 PublicationCorresponds to variant rs116047990dbSNPEnsembl.1
    Natural variantiVAR_04001252T → M in BChE deficiency. 1 PublicationCorresponds to variant rs56309853dbSNPEnsembl.1
    Natural variantiVAR_04001356F → I in BChE deficiency. 1 PublicationCorresponds to variant rs531738678dbSNPEnsembl.1
    Natural variantiVAR_04001461Y → C in BChE deficiency; enzymatically inactive in the plasma. 1 PublicationCorresponds to variant rs116097205dbSNPEnsembl.1
    Natural variantiVAR_07273062A → 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 Publication1
    Natural variantiVAR_04001565P → S in BChE deficiency; seems to cause reduced expression of the protein. 1 PublicationCorresponds to variant rs148170012dbSNPEnsembl.1
    Natural variantiVAR_00236098D → 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 PublicationsCorresponds to variant rs1799807dbSNPEnsembl.1
    Natural variantiVAR_04001698D → H in BChE deficiency. 1 Publication1
    Natural variantiVAR_072095103G → R in BChE deficiency; reduced enzyme activity. 2 Publications1
    Natural variantiVAR_072096118E → D in BChE deficiency; the mutant undergoes rapid degradation. 2 Publications1
    Natural variantiVAR_040017124N → Y in BChE deficiency. 1 Publication1
    Natural variantiVAR_072097127I → M Rare polymorphism; does not affect enzyme activity. 2 PublicationsCorresponds to variant rs755600722dbSNPEnsembl.1
    Natural variantiVAR_040018128P → S in BChE deficiency. 1 PublicationCorresponds to variant rs3732880dbSNPEnsembl.1
    Natural variantiVAR_040019143G → D in BChE deficiency. 1 PublicationCorresponds to variant rs201820739dbSNPEnsembl.1
    Natural variantiVAR_040020153L → F in BChE deficiency; seems to cause reduced expression of the protein. 1 PublicationCorresponds to variant rs747598704dbSNPEnsembl.1
    Natural variantiVAR_040021156Y → C in BChE deficiency. 1 PublicationCorresponds to variant rs121918558dbSNPEnsembl.1
    Natural variantiVAR_040022170V → M in BChE deficiency; allele H variant. 1 PublicationCorresponds to variant rs527843566dbSNPEnsembl.1
    Natural variantiVAR_040023198D → E in BChE deficiency; seems to cause reduced expression of the protein. 1 PublicationCorresponds to variant rs781368801dbSNPEnsembl.1
    Natural variantiVAR_040024226S → G in BChE deficiency; enzymatically inactive in the plasma. 1 PublicationCorresponds to variant rs370077923dbSNPEnsembl.1
    Natural variantiVAR_040025227A → V in BChE deficiency. 1 Publication1
    Natural variantiVAR_040026229A → T in BChE deficiency; enzymatically inactive in the plasma. 1 Publication1
    Natural variantiVAR_072098232V → D in BChE deficiency. 1 Publication1
    Natural variantiVAR_040027271T → M in BChE deficiency; allele fluoride-1. 2 PublicationsCorresponds to variant rs28933389dbSNPEnsembl.1
    Natural variantiVAR_040028278T → P in BChE deficiency. 2 Publications1
    Natural variantiVAR_040029283E → D.Corresponds to variant rs16849700dbSNPEnsembl.1
    Natural variantiVAR_040030295K → R in BChE deficiency. 1 PublicationCorresponds to variant rs115624085dbSNPEnsembl.1
    Natural variantiVAR_072099322V → M Rare polymorphism; does not affect enzymatic activity. 1 PublicationCorresponds to variant rs754644618dbSNPEnsembl.1
    Natural variantiVAR_040031335L → P in BChE deficiency; expressed at very low level. 1 PublicationCorresponds to variant rs104893684dbSNPEnsembl.1
    Natural variantiVAR_040032356A → D in BChE deficiency. 1 PublicationCorresponds to variant rs770337031dbSNPEnsembl.1
    Natural variantiVAR_002362358L → I in BChE deficiency; BChE variant form; fluoride-resistant. 4 PublicationsCorresponds to variant rs121918557dbSNPEnsembl.1
    Natural variantiVAR_072100361G → C in BChE deficiency; results in 20% of activity compared to wild-type. 1 Publication1
    Natural variantiVAR_040033393G → R in BChE deficiency. 4 PublicationsCorresponds to variant rs115129687dbSNPEnsembl.1
    Natural variantiVAR_040034414R → C in BChE deficiency. 2 PublicationsCorresponds to variant rs745364489dbSNPEnsembl.1
    Natural variantiVAR_040035418G → V in BChE deficiency; allele fluoride-2. 1 PublicationCorresponds to variant rs28933390dbSNPEnsembl.1
    Natural variantiVAR_040036446F → S in BChE deficiency. 2 Publications1
    Natural variantiVAR_040037488E → K in BChE deficiency. 1 PublicationCorresponds to variant rs200998515dbSNPEnsembl.1
    Natural variantiVAR_072101498R → W Rare polymorphism; does not affect enzymatic activity. 1 PublicationCorresponds to variant rs115017300dbSNPEnsembl.1
    Natural variantiVAR_040038499W → R in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication1
    Natural variantiVAR_040039502F → L in BChE deficiency. 1 PublicationCorresponds to variant rs769316835dbSNPEnsembl.1
    Natural variantiVAR_040040525E → V in BChE deficiency; allele J variant. 1 PublicationCorresponds to variant rs121918556dbSNPEnsembl.1
    Natural variantiVAR_040041543R → C in BChE deficiency. 3 PublicationsCorresponds to variant rs199660374dbSNPEnsembl.1
    Natural variantiVAR_040042546Q → L in BChE deficiency; seems to cause reduced expression of the protein. 1 Publication1
    Natural variantiVAR_002364567A → T in BChE deficiency; allele K variant; with reduced enzyme activity. 4 PublicationsCorresponds to variant rs1803274dbSNPEnsembl.1

    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_000055.3.
    UniGeneiHs.420483.

    Genome annotation databases

    EnsembliENST00000264381; ENSP00000264381; ENSG00000114200.
    GeneIDi590.
    KEGGihsa:590.
    UCSCiuc003fem.5. 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_000055.3.
    UniGeneiHs.420483.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4XIIX-ray2.70A/B29-572[»]
    5DYTX-ray2.55A/B28-557[»]
    5K5EX-ray2.80A/B29-557[»]
    ProteinModelPortaliP06276.
    SMRiP06276.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107064. 30 interactors.
    DIPiDIP-46476N.
    IntActiP06276. 1 interactor.
    STRINGi9606.ENSP00000264381.

    Chemistry databases

    BindingDBiP06276.
    ChEMBLiCHEMBL1914.
    DrugBankiDB08897. Aclidinium.
    DB01122. Ambenonium.
    DB01408. Bambuterol.
    DB06774. Capsaicin.
    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.
    DB06756. Glycine betaine.
    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

    ESTHERihuman-BCHE. BCHE.
    MEROPSiS09.980.

    PTM databases

    iPTMnetiP06276.
    PhosphoSitePlusiP06276.

    Polymorphism and mutation databases

    BioMutaiBCHE.
    DMDMi116353.

    Proteomic databases

    EPDiP06276.
    MaxQBiP06276.
    PaxDbiP06276.
    PeptideAtlasiP06276.
    PRIDEiP06276.

    Protocols and materials databases

    DNASUi590.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264381; ENSP00000264381; ENSG00000114200.
    GeneIDi590.
    KEGGihsa:590.
    UCSCiuc003fem.5. human.

    Organism-specific databases

    CTDi590.
    DisGeNETi590.
    GeneCardsiBCHE.
    HGNCiHGNC:983. BCHE.
    HPAiHPA001560.
    MalaCardsiBCHE.
    MIMi177400. gene+phenotype.
    neXtProtiNX_P06276.
    OpenTargetsiENSG00000114200.
    Orphaneti132. Butyrylcholinesterase deficiency.
    413693. Curariform drugs toxicity.
    PharmGKBiPA25294.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG4389. Eukaryota.
    COG2272. LUCA.
    GeneTreeiENSGT00760000118946.
    HOVERGENiHBG008839.
    InParanoidiP06276.
    KOiK01050.
    OMAiFLGSEMW.
    OrthoDBiEOG091G0I4G.
    PhylomeDBiP06276.
    TreeFamiTF315470.

    Enzyme and pathway databases

    BioCyciZFISH:HS03747-MONOMER.
    BRENDAi3.1.1.8. 2681.
    ReactomeiR-HSA-112311. Neurotransmitter Clearance In The Synaptic Cleft.
    R-HSA-1483191. Synthesis of PC.
    R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RKP06276.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000114200.
    CleanExiHS_BCHE.
    ExpressionAtlasiP06276. baseline and differential.
    GenevisibleiP06276. HS.

    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...

    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: November 30, 2016
    This is version 184 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

    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 one 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.