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P06276 (CHLE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cholinesterase

EC=3.1.1.8
Alternative name(s):
Acylcholine acylhydrolase
Butyrylcholine esterase
Choline esterase II
Pseudocholinesterase
Gene names
Name:BCHE
Synonyms:CHE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. Ref.12 Ref.15

Catalytic activity

An acylcholine + H2O = choline + a carboxylate. Ref.15 Ref.22

Enzyme regulation

Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging. Ref.20 Ref.21 Ref.22

Subunit structure

Homotetramer; disulfide-linked. Dimer of dimers. Ref.7 Ref.8 Ref.12 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

Secreted Ref.12 Ref.22.

Tissue specificity

Detected in blood plasma (at protein level). Present in most cells except erythrocytes. Ref.12 Ref.22

Post-translational modification

N-glycosylated. No other PTM detected (Ref.7). 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. Ref.7 Ref.11 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Involvement in disease

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.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   LigandSialic acid
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

choline metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

cocaine metabolic process

Traceable author statement PubMed 8622553. Source: UniProtKB

learning

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

neuroblast differentiation

Inferred from electronic annotation. Source: Ensembl

response to alkaloid

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

endoplasmic reticulum lumen

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from electronic annotation. Source: Ensembl

nuclear envelope lumen

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionacetylcholinesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta-amyloid binding

Non-traceable author statement PubMed 11569538. Source: UniProtKB

catalytic activity

Non-traceable author statement PubMed 11569538. Source: UniProtKB

choline binding

Inferred from electronic annotation. Source: Ensembl

cholinesterase activity

Inferred from direct assay Ref.15. Source: UniProtKB

enzyme binding

Non-traceable author statement PubMed 11569538. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 20883446PubMed 22726956. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7936069,EBI-7936069

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.6 Ref.7
Chain29 – 602574Cholinesterase
PRO_0000008613

Regions

Region144 – 1452Substrate binding

Sites

Active site2261Acyl-ester intermediate Ref.6 Ref.17
Active site3531Charge relay system Ref.17
Active site4661Charge relay system Ref.17

Amino acid modifications

Modified residue2261Phosphoserine Ref.16
Glycosylation451N-linked (GlcNAc...) (complex) Ref.10 Ref.11
Glycosylation851N-linked (GlcNAc...) (complex) Ref.10 Ref.11 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Glycosylation1341N-linked (GlcNAc...) (complex) Ref.11 Ref.13 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Glycosylation2691N-linked (GlcNAc...) (complex) Ref.11 Ref.17 Ref.18 Ref.20 Ref.22
Glycosylation2841N-linked (GlcNAc...) (complex) Ref.11 Ref.13 Ref.14 Ref.21 Ref.22
Glycosylation3691N-linked (GlcNAc...) (complex) Ref.10 Ref.11 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Glycosylation4831N-linked (GlcNAc...) (complex) Ref.10 Ref.11
Glycosylation5091N-linked (GlcNAc...) Ref.6 Ref.9 Ref.10
Glycosylation5131N-linked (GlcNAc...) Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Glycosylation5141N-linked (GlcNAc...) Ref.6 Ref.9 Ref.10
Disulfide bond93 ↔ 120 Ref.8 Ref.17 Ref.18 Ref.19 Ref.20
Disulfide bond280 ↔ 291 Ref.8 Ref.17 Ref.18 Ref.19 Ref.20
Disulfide bond428 ↔ 547 Ref.8 Ref.17 Ref.18 Ref.19 Ref.20
Disulfide bond599Interchain Ref.8 Ref.17 Ref.18 Ref.19 Ref.20

Natural variations

Natural variant321Missing in BChE deficiency. Ref.33
VAR_040011
Natural variant521T → M in BChE deficiency. Ref.33
Corresponds to variant rs56309853 [ dbSNP | Ensembl ].
VAR_040012
Natural variant561F → I in BChE deficiency. Ref.38
VAR_040013
Natural variant611Y → C in BChE deficiency; enzymatically inactive in the plasma. Ref.30
VAR_040014
Natural variant651P → S in BChE deficiency; seems to cause reduced expression of the protein. Ref.30
VAR_040015
Natural variant981D → G in BChE deficiency; BChE atypical form; dibucaine-resistant. Ref.23 Ref.27 Ref.34 Ref.37
Corresponds to variant rs1799807 [ dbSNP | Ensembl ].
VAR_002360
Natural variant981D → H in BChE deficiency. Ref.37
VAR_040016
Natural variant1241N → Y in BChE deficiency. Ref.38
VAR_040017
Natural variant1281P → S in BChE deficiency. Ref.33
Corresponds to variant rs3732880 [ dbSNP | Ensembl ].
VAR_040018
Natural variant1431G → D in BChE deficiency. Ref.34
VAR_040019
Natural variant1531L → F in BChE deficiency; seems to cause reduced expression of the protein. Ref.30
VAR_040020
Natural variant1561Y → C in BChE deficiency. Ref.31
VAR_040021
Natural variant1701V → M in BChE deficiency; allele H variant. Ref.27
VAR_040022
Natural variant1981D → E in BChE deficiency; seems to cause reduced expression of the protein. Ref.30
VAR_040023
Natural variant2261S → G in BChE deficiency; enzymatically inactive in the plasma. Ref.30
VAR_040024
Natural variant2271A → V in BChE deficiency. Ref.35
VAR_040025
Natural variant2291A → T in BChE deficiency; enzymatically inactive in the plasma. Ref.30
VAR_040026
Natural variant2711T → M in BChE deficiency; allele fluoride-1. Ref.25 Ref.37
Corresponds to variant rs28933389 [ dbSNP | Ensembl ].
VAR_040027
Natural variant2781T → P in BChE deficiency. Ref.28 Ref.33
VAR_040028
Natural variant2831E → D.
Corresponds to variant rs16849700 [ dbSNP | Ensembl ].
VAR_040029
Natural variant2951K → R in BChE deficiency. Ref.33
Corresponds to variant rs115624085 [ dbSNP | Ensembl ].
VAR_040030
Natural variant3351L → P in BChE deficiency; expressed at very low level. Ref.40
VAR_040031
Natural variant3561A → D in BChE deficiency. Ref.41
VAR_040032
Natural variant3581L → I in BChE deficiency; BChE variant form; fluoride-resistant; Japanese type. Ref.29 Ref.32 Ref.33 Ref.36
Corresponds to variant rs121918557 [ dbSNP | Ensembl ].
VAR_002362
Natural variant3931G → R in BChE deficiency. Ref.26 Ref.28 Ref.33 Ref.36
Corresponds to variant rs115129687 [ dbSNP | Ensembl ].
VAR_040033
Natural variant4141R → C in BChE deficiency. Ref.38 Ref.39
VAR_040034
Natural variant4181G → V in BChE deficiency; allele fluoride-2. Ref.25
Corresponds to variant rs28933390 [ dbSNP | Ensembl ].
VAR_040035
Natural variant4461F → S in BChE deficiency. Ref.28 Ref.33
VAR_040036
Natural variant4881E → K in BChE deficiency. Ref.38
VAR_040037
Natural variant4991W → R in BChE deficiency; seems to cause reduced expression of the protein. Ref.30
VAR_040038
Natural variant5021F → L in BChE deficiency. Ref.39
VAR_040039
Natural variant5251E → V in BChE deficiency; allele J variant. Ref.24
VAR_040040
Natural variant5431R → C in BChE deficiency. Ref.28 Ref.33 Ref.36
VAR_040041
Natural variant5461Q → L in BChE deficiency; seems to cause reduced expression of the protein. Ref.30
VAR_040042
Natural variant5671A → T in BChE deficiency; allele K variant; with reduced enzyme activity. Ref.4 Ref.28 Ref.33 Ref.37
Corresponds to variant rs1803274 [ dbSNP | Ensembl ].
VAR_002364

Secondary structure

....................................................................................................... 602
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06276 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: C9836409D9057F27

FASTA60268,418
        10         20         30         40         50         60 
MHSKVTIICI RFLFWFLLLC MLIGKSHTED DIIIATKNGK VRGMNLTVFG GTVTAFLGIP 

        70         80         90        100        110        120 
YAQPPLGRLR FKKPQSLTKW SDIWNATKYA NSCCQNIDQS FPGFHGSEMW NPNTDLSEDC 

       130        140        150        160        170        180 
LYLNVWIPAP KPKNATVLIW IYGGGFQTGT SSLHVYDGKF LARVERVIVV SMNYRVGALG 

       190        200        210        220        230        240 
FLALPGNPEA PGNMGLFDQQ LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPG 

       250        260        270        280        290        300 
SHSLFTRAIL QSGSFNAPWA VTSLYEARNR TLNLAKLTGC SRENETEIIK CLRNKDPQEI 

       310        320        330        340        350        360 
LLNEAFVVPY GTPLSVNFGP TVDGDFLTDM PDILLELGQF KKTQILVGVN KDEGTAFLVY 

       370        380        390        400        410        420 
GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH YTDWVDDQRP ENYREALGDV 

       430        440        450        460        470        480 
VGDYNFICPA LEFTKKFSEW GNNAFFYYFE HRSSKLPWPE WMGVMHGYEI EFVFGLPLER 

       490        500        510        520        530        540 
RDNYTKAEEI LSRSIVKRWA NFAKYGNPNE TQNNSTSWPV FKSTEQKYLT LNTESTRIMT 

       550        560        570        580        590        600 
KLRAQQCRFW TSFFPKVLEM TGNIDEAEWE WKAGFHRWNN YMMDWKNQFN DYTSKKESCV 


GL 

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References

« Hide 'large scale' references
[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]"Brain cDNA clone for human cholinesterase."
McTiernan C., Adkins S., Chatonnet A., Vaughan T.A., Bartels C.F., Kott M., Rosenberry T.L., la Du B.N., Lockridge O.
Proc. Natl. Acad. Sci. U.S.A. 84:6682-6686(1987) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
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]"Mechanisms of cholinesterase inhibition by inorganic mercury."
Frasco M.F., Colletier J.-P., Weik M., Carvalho F., Guilhermino L., Stojan J., Fournier D.
FEBS J. 274:1849-1861(2007) [PubMed] [Europe PMC] [Abstract]
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]"Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation."
Carletti E., Li H., Li B., Ekstroem F., Nicolet Y., Loiodice M., Gillon E., Froment M.T., Lockridge O., Schopfer L.M., Masson P., Nachon F.
J. Am. Chem. Soc. 130:16011-16020(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRACHU. A33769.
RefSeqNP_000046.1. NM_000055.2.
UniGeneHs.420483.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP06276.
SMRP06276. Positions 31-557, 564-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107064. 2 interactions.
DIPDIP-46476N.
STRING9606.ENSP00000264381.

Chemistry

BindingDBP06276.
ChEMBLCHEMBL2095233.
DrugBankDB01122. 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.
GuidetoPHARMACOLOGY2471.

Protein family/group databases

MEROPSS09.980.

PTM databases

PhosphoSiteP06276.

Polymorphism databases

DMDM116353.

Proteomic databases

PaxDbP06276.
PRIDEP06276.

Protocols and materials databases

DNASU590.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264381; ENSP00000264381; ENSG00000114200.
GeneID590.
KEGGhsa:590.
UCSCuc003fem.4. human.

Organism-specific databases

CTD590.
GeneCardsGC03M165490.
HGNCHGNC:983. BCHE.
HPAHPA001560.
MIM177400. gene+phenotype.
neXtProtNX_P06276.
Orphanet132. 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.
PharmGKBPA25294.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2272.
HOVERGENHBG008839.
InParanoidP06276.
KOK01050.
OMASFNAPWA.
OrthoDBEOG789C9R.
PhylomeDBP06276.
TreeFamTF315470.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.
REACT_17015. Metabolism of proteins.
SABIO-RKP06276.

Gene expression databases

ArrayExpressP06276.
BgeeP06276.
CleanExHS_BCHE.
GenevestigatorP06276.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCHE. human.
EvolutionaryTraceP06276.
GeneWikiButyrylcholinesterase.
GenomeRNAi590.
NextBio2405.
PROP06276.
SOURCESearch...

Entry information

Entry nameCHLE_HUMAN
AccessionPrimary (citable) accession number: P06276
Secondary accession number(s): A8K7P8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM