Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cholinesterase  

UniProtKB / Swiss-Prot ID :  CHLE_HUMAN

Gene Name (Synonyms) : 
BCHE, CHE1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. 

Protein Sequence MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLR...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHHHHHHCCCCCCCCCEEECCCCEEEEEEEECCCCEEEEEECCCCCCCCCCCCC...
Protein Variant
LocationDescription
32Missing (in BChE deficiency). VAR_040011
52T -> M (in BChE deficiency;dbSNP:rs56309853).
56F -> I (in BChE deficiency). VAR_040013
61Y -> C (in BChE deficiency; enzymaticallyinactive in the plasma).
65P -> S (in BChE deficiency; seems tocause reduced expression of the protein).
98D -> G (in BChE deficiency; BChE atypicalform; dibucaine-resistant;
98D -> H (in BChE deficiency). VAR_040016
124N -> Y (in BChE deficiency). VAR_040017
128P -> S (in BChE deficiency;dbSNP:rs3732880).
143G -> D (in BChE deficiency). VAR_040019
153L -> F (in BChE deficiency; seems tocause reduced expression of the protein).
156Y -> C (in BChE deficiency). VAR_040021
170V -> M (in BChE deficiency; allele Hvariant).
198D -> E (in BChE deficiency; seems tocause reduced expression of the protein).
226S -> G (in BChE deficiency; enzymaticallyinactive in the plasma).
227A -> V (in BChE deficiency). VAR_040025
229A -> T (in BChE deficiency; enzymaticallyinactive in the plasma).
271T -> M (in BChE deficiency; allelefluoride-1; dbSNP:rs28933389).
278T -> P (in BChE deficiency). VAR_040028
283E -> D (in dbSNP:rs16849700). VAR_040029
295K -> R (in BChE deficiency). VAR_040030
335L -> P (in BChE deficiency; expressed atvery low level).
356A -> D (in BChE deficiency). VAR_040032
358L -> I (in BChE deficiency; BChE variantform; fluoride-resistant; Japanese type).
393G -> R (in BChE deficiency). VAR_040033
414R -> C (in BChE deficiency). VAR_040034
418G -> V (in BChE deficiency; allelefluoride-2; dbSNP:rs28933390).
446F -> S (in BChE deficiency). VAR_040036
488E -> K (in BChE deficiency). VAR_040037
499W -> R (in BChE deficiency; seems tocause reduced expression of the protein).
502F -> L (in BChE deficiency). VAR_040039
525E -> V (in BChE deficiency; allele Jvariant).
543R -> C (in BChE deficiency). VAR_040041
546Q -> L (in BChE deficiency; seems tocause reduced expression of the protein).
567A -> T (in BChE deficiency; allele Kvariant; with reduced enzyme activity;
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
45N-linked (Glc...)VRGMNLTVF
EEEEEEECC
35.07HPRD
Link
45N-linked (GlcNAc...).VRGMNLTVF
EEEEEEECC
35.07UniProtKB
Link
85N-linked (Glc...)SDIWNATKY
CCCCCCCCC
37.76HPRD
Link
85N-linked (GlcNAc...).SDIWNATKY
CCCCCCCCC
37.76UniProtKB
Link
134N-linked (Glc...)PKPKNATVL
CCCCCCCEE
49.74HPRD
Link
134N-linked (GlcNAc...).PKPKNATVL
CCCCCCCEE
49.74UniProtKB
Link
226PhosphoserineLFGESAGAA
EEEECHHHH
32.17Phosphositeplus
Link
269N-linked (Glc...)YEARNRTLN
CHHHHHHHH
48.62HPRD
Link
269N-linked (GlcNAc...).YEARNRTLN
CHHHHHHHH
48.62UniProtKB
Link
284N-linked (Glc...)CSRENETEI
CCCCCHHHH
61.45HPRD
Link
284N-linked (GlcNAc...).CSRENETEI
CCCCCHHHH
61.45UniProtKB
Link
369N-linked (Glc...)FSKDNNSII
CCCCCCCCC
48.13HPRD
Link
369N-linked (GlcNAc...).FSKDNNSII
CCCCCCCCC
48.13UniProtKB
Link
483N-linked (Glc...)ERRDNYTKA
CCCCCCCHH
44.56HPRD
Link
483N-linked (GlcNAc...).ERRDNYTKA
CCCCCCCHH
44.56UniProtKB
Link
509N-linked (Glc...)YGNPNETQN
CCCCCCCCC
69.79HPRD
Link
509N-linked (GlcNAc...).YGNPNETQN
CCCCCCCCC
69.79UniProtKB
Link
513N-linked (GlcNAc...).NETQNNSTS
CCCCCCCCC
52.41UniProtKB
Link
514N-linked (Glc...)ETQNNSTSW
CCCCCCCCC
36.53HPRD
Link
514N-linked (GlcNAc...).ETQNNSTSW
CCCCCCCCC
36.53UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CHLE_HUMANin vitroHPRD:01519HPRD12130740
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Disease Reference
Kegg disease
OMIM disease
177400Butyrylcholinesterase deficiency (BChE deficiency)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284, AND MASSSPECTROMETRY.
"Crystal structure of human butyrylcholinesterase and of its complexeswith substrate and products.";
Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., Nachon F.;
J. Biol. Chem. 278:41141-41147(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITHSUBSTRATE, SUBUNIT, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369AND ASN-513, DISULFIDE BONDS, AND ACTIVE SITE.
"Role of water in aging of human butyrylcholinesterase inhibited byechothiophate: the crystal structure suggests two alternativemechanisms of aging.";
Nachon F., Asojo O.A., Borgstahl G.E.O., Masson P., Lockridge O.;
Biochemistry 44:1154-1162(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITHECHOTHIOPHATE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-85; ASN-134;ASN-269; ASN-369 AND ASN-513.
"Crystallization and X-ray structure of full-length recombinant humanbutyrylcholinesterase.";
Ngamelue M.N., Homma K., Lockridge O., Asojo O.A.;
Acta Crystallogr. F 63:723-727(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATIONAT ASN-85; ASN-134; ASN-369 AND ASN-513, AND SUBUNIT.
"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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITHMERCURY IONS AND BUTANOIC ACID, DISULFIDE BONDS, GLYCOSYLATION ATASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, AND ENZYME REGULATION.
"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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITHTABUN, ENZYME REGULATION, MASS SPECTROMETRY, AND GLYCOSYLATION ATASN-85; ASN-134; ASN-284; ASN-369 AND ASN-513.
"Structure-activity analysis of aging and reactivation of humanbutyrylcholinesterase 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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUNANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 ANDASN-513, AND ENZYME REGULATION.
"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).
Cited for: PROTEIN SEQUENCE OF 29-602.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514, AND MASSSPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369;ASN-483; ASN-509 AND ASN-514, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures