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P06276

- CHLE_HUMAN

UniProt

P06276 - CHLE_HUMAN

Protein

Cholinesterase

Gene

BCHE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei226 – 2261Acyl-ester intermediate1 PublicationPROSITE-ProRule annotation
    Active sitei353 – 3531Charge relay system1 Publication
    Active sitei466 – 4661Charge relay system1 Publication

    GO - Molecular functioni

    1. acetylcholinesterase activity Source: UniProtKB
    2. beta-amyloid binding Source: UniProtKB
    3. catalytic activity Source: UniProtKB
    4. choline binding Source: Ensembl
    5. cholinesterase activity Source: UniProtKB
    6. enzyme binding Source: UniProtKB
    7. identical protein binding Source: IntAct

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. choline metabolic process Source: RefGenome
    3. cocaine metabolic process Source: UniProtKB
    4. learning Source: Ensembl
    5. negative regulation of cell proliferation Source: Ensembl
    6. negative regulation of synaptic transmission Source: Ensembl
    7. neuroblast differentiation Source: Ensembl
    8. response to alkaloid Source: Ensembl
    9. response to drug Source: Ensembl
    10. response to folic acid Source: Ensembl
    11. response to glucocorticoid Source: Ensembl
    12. synaptic transmission, cholinergic Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_121238. Synthesis of PC.
    REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-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: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:983. BCHE.

    Subcellular locationi

    Secreted 2 Publications

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. endoplasmic reticulum lumen Source: RefGenome
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: RefGenome
    5. membrane Source: Ensembl
    6. nuclear envelope lumen Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Butyrylcholinesterase deficiency (BChE deficiency) [MIM:177400]: A 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.19 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 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; BChE atypical form; dibucaine-resistant. 4 Publications
    Corresponds to variant rs1799807 [ dbSNP | Ensembl ].
    VAR_002360
    Natural varianti98 – 981D → H in BChE deficiency. 1 Publication
    VAR_040016
    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 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; Japanese type. 4 Publications
    Corresponds to variant rs121918557 [ dbSNP | Ensembl ].
    VAR_002362
    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.
    240861. Cisatracurium toxicity.
    240891. Mivacurium toxicity.
    240895. Pancuronium toxicity.
    240907. Rocuronium toxicity.
    240911. Satracurium toxicity.
    241023. Susceptibility to prolonged paralysis due to cisatracurium treatment.
    241025. Susceptibility to prolonged paralysis due to mivacurium treatment.
    241027. Susceptibility to prolonged paralysis due to pancuronium treatment.
    241029. Susceptibility to prolonged paralysis due to rocuronium treatment.
    241031. Susceptibility to prolonged paralysis due to satracurium treatment.
    241033. Susceptibility to prolonged paralysis due to vecuronium treatment.
    240917. Vecuronium toxicity.
    PharmGKBiPA25294.

    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)3 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)3 Publications
    Glycosylationi509 – 5091N-linked (GlcNAc...)4 Publications
    Glycosylationi513 – 5131N-linked (GlcNAc...)7 Publications
    Glycosylationi514 – 5141N-linked (GlcNAc...)4 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

    ArrayExpressiP06276.
    BgeeiP06276.
    CleanExiHS_BCHE.
    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. 2 interactions.
    DIPiDIP-46476N.
    STRINGi9606.ENSP00000264381.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    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

    MHSKVTIICI RFLFWFLLLC MLIGKSHTED DIIIATKNGK VRGMNLTVFG    50
    GTVTAFLGIP YAQPPLGRLR FKKPQSLTKW SDIWNATKYA NSCCQNIDQS 100
    FPGFHGSEMW NPNTDLSEDC LYLNVWIPAP KPKNATVLIW IYGGGFQTGT 150
    SSLHVYDGKF LARVERVIVV SMNYRVGALG FLALPGNPEA PGNMGLFDQQ 200
    LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPG SHSLFTRAIL 250
    QSGSFNAPWA VTSLYEARNR TLNLAKLTGC SRENETEIIK CLRNKDPQEI 300
    LLNEAFVVPY GTPLSVNFGP TVDGDFLTDM PDILLELGQF KKTQILVGVN 350
    KDEGTAFLVY GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH 400
    YTDWVDDQRP ENYREALGDV VGDYNFICPA LEFTKKFSEW GNNAFFYYFE 450
    HRSSKLPWPE WMGVMHGYEI EFVFGLPLER RDNYTKAEEI LSRSIVKRWA 500
    NFAKYGNPNE TQNNSTSWPV FKSTEQKYLT LNTESTRIMT KLRAQQCRFW 550
    TSFFPKVLEM TGNIDEAEWE WKAGFHRWNN YMMDWKNQFN DYTSKKESCV 600
    GL 602
    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 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 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; BChE atypical form; dibucaine-resistant. 4 Publications
    Corresponds to variant rs1799807 [ dbSNP | Ensembl ].
    VAR_002360
    Natural varianti98 – 981D → H in BChE deficiency. 1 Publication
    VAR_040016
    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 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 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; Japanese type. 4 Publications
    Corresponds to variant rs121918557 [ dbSNP | Ensembl ].
    VAR_002362
    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi116353.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3198.1.
    PIRi A33769. ACHU.
    RefSeqi NP_000046.1. NM_000055.2.
    UniGenei Hs.420483.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EHO model - A 30-560 [» ]
    1EHQ model - A 30-560 [» ]
    1KCJ model - A 30-560 [» ]
    1P0I X-ray 2.00 A 29-557 [» ]
    1P0M X-ray 2.38 A 29-557 [» ]
    1P0P X-ray 2.30 A 29-557 [» ]
    1P0Q X-ray 2.43 A 29-557 [» ]
    1XLU X-ray 2.20 A 29-557 [» ]
    1XLV X-ray 2.25 A 29-557 [» ]
    1XLW X-ray 2.10 A 29-557 [» ]
    2J4C X-ray 2.75 A 29-557 [» ]
    2PM8 X-ray 2.80 A/B 29-602 [» ]
    2WID X-ray 2.30 A 29-557 [» ]
    2WIF X-ray 2.25 A 29-557 [» ]
    2WIG X-ray 2.15 A 29-557 [» ]
    2WIJ X-ray 2.10 A 29-557 [» ]
    2WIK X-ray 2.10 A 29-557 [» ]
    2WIL X-ray 3.10 A/B 29-557 [» ]
    2WSL X-ray 2.00 A 29-557 [» ]
    2XMB X-ray 2.10 A 29-557 [» ]
    2XMC X-ray 2.40 A 29-557 [» ]
    2XMD X-ray 2.30 A 29-557 [» ]
    2XMG X-ray 2.70 A 29-557 [» ]
    2XQF X-ray 2.10 A 31-557 [» ]
    2XQG X-ray 2.30 A 31-557 [» ]
    2XQI X-ray 2.60 A 31-557 [» ]
    2XQJ X-ray 2.40 A 31-557 [» ]
    2XQK X-ray 2.40 A 31-557 [» ]
    2Y1K X-ray 2.50 A 29-557 [» ]
    3DJY X-ray 2.10 A 29-557 [» ]
    3DKK X-ray 2.31 A 29-557 [» ]
    3O9M X-ray 2.98 A/B 29-602 [» ]
    4AQD X-ray 2.50 A/B 29-557 [» ]
    4AXB X-ray 2.40 A 31-557 [» ]
    4B0O X-ray 2.35 A 29-557 [» ]
    4B0P X-ray 2.50 A 29-557 [» ]
    4BBZ X-ray 2.70 A 29-557 [» ]
    4BDS X-ray 2.10 A 29-557 [» ]
    ProteinModelPortali P06276.
    SMRi P06276. Positions 31-557, 564-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107064. 2 interactions.
    DIPi DIP-46476N.
    STRINGi 9606.ENSP00000264381.

    Chemistry

    BindingDBi P06276.
    ChEMBLi CHEMBL1914.
    DrugBanki DB01122. Ambenonium.
    DB00572. Atropine.
    DB01408. Bambuterol.
    DB00477. Chlorpromazine.
    DB00122. Choline.
    DB00568. Cinnarizine.
    DB00944. Demecarium bromide.
    DB00527. Dibucaine.
    DB00843. Donepezil.
    DB01057. Echothiophate Iodide.
    DB01010. Edrophonium.
    DB00392. Ethopropazine.
    DB00292. Etomidate.
    DB00674. Galantamine.
    DB00941. Hexafluronium bromide.
    DB00677. Isoflurophate.
    DB00358. Mefloquine.
    DB01226. Mivacurium.
    DB01400. Neostigmine.
    DB01337. Pancuronium.
    DB00733. Pralidoxime.
    DB01035. Procainamide.
    DB00545. Pyridostigmine.
    DB00989. Rivastigmine.
    DB00202. Succinylcholine.
    DB00871. Terbutaline.
    DB01116. Trimethaphan.
    GuidetoPHARMACOLOGYi 2471.

    Protein family/group databases

    MEROPSi S09.980.

    PTM databases

    PhosphoSitei P06276.

    Polymorphism databases

    DMDMi 116353.

    Proteomic databases

    MaxQBi P06276.
    PaxDbi P06276.
    PRIDEi P06276.

    Protocols and materials databases

    DNASUi 590.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264381 ; ENSP00000264381 ; ENSG00000114200 .
    GeneIDi 590.
    KEGGi hsa:590.
    UCSCi uc003fem.4. human.

    Organism-specific databases

    CTDi 590.
    GeneCardsi GC03M165490.
    HGNCi HGNC:983. BCHE.
    HPAi HPA001560.
    MIMi 177400. gene+phenotype.
    neXtProti NX_P06276.
    Orphaneti 132. Butyrylcholinesterase deficiency.
    240861. Cisatracurium toxicity.
    240891. Mivacurium toxicity.
    240895. Pancuronium toxicity.
    240907. Rocuronium toxicity.
    240911. Satracurium toxicity.
    241023. Susceptibility to prolonged paralysis due to cisatracurium treatment.
    241025. Susceptibility to prolonged paralysis due to mivacurium treatment.
    241027. Susceptibility to prolonged paralysis due to pancuronium treatment.
    241029. Susceptibility to prolonged paralysis due to rocuronium treatment.
    241031. Susceptibility to prolonged paralysis due to satracurium treatment.
    241033. Susceptibility to prolonged paralysis due to vecuronium treatment.
    240917. Vecuronium toxicity.
    PharmGKBi PA25294.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2272.
    HOVERGENi HBG008839.
    InParanoidi P06276.
    KOi K01050.
    OMAi SFNAPWA.
    OrthoDBi EOG789C9R.
    PhylomeDBi P06276.
    TreeFami TF315470.

    Enzyme and pathway databases

    Reactomei REACT_121238. Synthesis of PC.
    REACT_13583. Neurotransmitter Clearance In The Synaptic Cleft.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RK P06276.

    Miscellaneous databases

    ChiTaRSi BCHE. human.
    EvolutionaryTracei P06276.
    GeneWikii Butyrylcholinesterase.
    GenomeRNAii 590.
    NextBioi 2405.
    PROi P06276.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06276.
    Bgeei P06276.
    CleanExi HS_BCHE.
    Genevestigatori P06276.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR014788. AChE_tetra.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view ]
    Pfami PF08674. AChE_tetra. 1 hit.
    PF00135. COesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR00878. CHOLNESTRASE.
    ProDomi PD415333. AChE_tetra. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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. "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.
    18. "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.
    19. "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.
    20. 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.
    21. 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.
    22. "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.
    23. "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.
    24. "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.
    25. "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.
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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.
    31. "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.
    32. "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.
    33. "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.
    34. "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.
    35. "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.
    36. "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.
    37. "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.
    38. "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.
    39. "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.
    40. "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.
    41. "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.

    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: October 1, 2014
    This is version 161 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