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P06276

- CHLE_HUMAN

UniProt

P06276 - CHLE_HUMAN

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Protein

Cholinesterase

Gene
BCHE, CHE1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei226 – 2261Acyl-ester intermediate2 Publications
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
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: 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
Complete GO annotation...

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.
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)2 Publications
Glycosylationi85 – 851N-linked (GlcNAc...) (complex)8 Publications
Disulfide bondi93 ↔ 1205 Publications
Glycosylationi134 – 1341N-linked (GlcNAc...) (complex)8 Publications
Modified residuei226 – 2261Phosphoserine1 Publication
Glycosylationi269 – 2691N-linked (GlcNAc...) (complex)5 Publications
Disulfide bondi280 ↔ 2915 Publications
Glycosylationi284 – 2841N-linked (GlcNAc...) (complex)5 Publications
Glycosylationi369 – 3691N-linked (GlcNAc...) (complex)8 Publications
Disulfide bondi428 ↔ 5475 Publications
Glycosylationi483 – 4831N-linked (GlcNAc...) (complex)2 Publications
Glycosylationi509 – 5091N-linked (GlcNAc...)3 Publications
Glycosylationi513 – 5131N-linked (GlcNAc...)6 Publications
Glycosylationi514 – 5141N-linked (GlcNAc...)3 Publications
Disulfide bondi599 – 599Interchain5 Publications

Post-translational modificationi

N-glycosylated. No other PTM detected (1 Publication). 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.9 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.7 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.

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

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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

« 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. "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: September 3, 2014
This is version 160 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

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