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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 intermediate1 PublicationPROSITE-ProRule annotation
Active sitei353 – 3531Charge relay system1 Publication
Active sitei466 – 4661Charge relay system1 Publication
Binding sitei466 – 4661Tacrine; via carbonyl oxygenCombined sources

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: Ensembl
  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
Complete GO annotation...

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: UniProtKB
  2. endoplasmic reticulum lumen Source: Ensembl
  3. extracellular region Source: UniProtKB
  4. membrane Source: Ensembl
  5. nuclear envelope lumen Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Butyrylcholinesterase deficiency23 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 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. 5 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; Japanese type. 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.
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)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. 3 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 that 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 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. 5 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 that 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 that 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; Japanese type. 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 that 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.

Polymorphism databases

DMDMi116353.

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. 3 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 databases

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.
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.
GenAtlasiSearch...

Phylogenomic databases

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

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.

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. "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.
  18. "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.
  19. "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.
  20. "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.
  21. 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.
  22. 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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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.
  46. "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.

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: February 4, 2015
This is version 165 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.