CHLE_HUMAN - dbPTM
CHLE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHLE_HUMAN
UniProt AC P06276
Protein Name Cholinesterase
Gene Name BCHE
Organism Homo sapiens (Human).
Sequence Length 602
Subcellular Localization Secreted .
Protein Description Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters..
Protein Sequence MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MHSKVTIICI
-----CCCHHHHHHH		27.7626503514
6Phosphorylation--MHSKVTIICIRFL
--CCCHHHHHHHHHH		14.36-
45N-linked_GlycosylationNGKVRGMNLTVFGGT
CCEEECEEEEEECCE		35.0718203274
45N-linked_GlycosylationNGKVRGMNLTVFGGT
CCEEECEEEEEECCE		35.0718203274
85N-linked_GlycosylationTKWSDIWNATKYANS
CCHHHHHHHHHHHHH		37.7617355286
85N-linked_GlycosylationTKWSDIWNATKYANS
CCHHHHHHHHHHHHH		37.7617355286
88AcetylationSDIWNATKYANSCCQ
HHHHHHHHHHHHHHC		39.707666003
134N-linked_GlycosylationIPAPKPKNATVLIWI
EECCCCCCCEEEEEE		49.7417355286
134N-linked_GlycosylationIPAPKPKNATVLIWI
EECCCCCCCEEEEEE		49.7417355286
171PhosphorylationVERVIVVSMNYRVGA
EEEEEEEECCCCCCE		7.1624719451
174PhosphorylationVIVVSMNYRVGALGF
EEEEECCCCCCEEEE		9.6825072903
221PhosphorylationGGNPKSVTLFGESAG
CCCCCEEEEEECCCC		24.38-
226PhosphorylationSVTLFGESAGAASVS
EEEEEECCCCCCEEE		32.1722444575
252PhosphorylationFTRAILQSGSFNAPW
HHHHHHHHCCCCCCH		32.7227762562
254PhosphorylationRAILQSGSFNAPWAV
HHHHHHCCCCCCHHH		22.1527762562
269N-linked_GlycosylationTSLYEARNRTLNLAK
HHHHHHHHHHCCHHH		48.6217355286
269N-linked_GlycosylationTSLYEARNRTLNLAK
HHHHHHHHHHCCHHH		48.6217355286
284N-linked_GlycosylationLTGCSRENETEIIKC
HHCCCCCCHHHHHHH		61.4518203274
284N-linked_GlycosylationLTGCSRENETEIIKC
HHCCCCCCHHHHHHH		61.4518203274
369N-linked_GlycosylationAPGFSKDNNSIITRK
CCCCCCCCCCCCCHH		48.1317355286
369N-linked_GlycosylationAPGFSKDNNSIITRK
CCCCCCCCCCCCCHH		48.1317355286
371PhosphorylationGFSKDNNSIITRKEF
CCCCCCCCCCCHHHH		22.9424719451
436MethylationPALEFTKKFSEWGNN
HHHHHHHHHHHCCCC		51.5723644510
455MethylationYFEHRSSKLPWPEWM
EEECCCCCCCCCHHH		60.8723644510
483N-linked_GlycosylationLPLERRDNYTKAEEI
CCCHHCCCCCCHHHH		44.5618203274
483N-linked_GlycosylationLPLERRDNYTKAEEI
CCCHHCCCCCCHHHH		44.5618203274
492PhosphorylationTKAEEILSRSIVKRW
CCHHHHHHHHHHHHH		29.6424719451
505PhosphorylationRWANFAKYGNPNETQ
HHHHHHHHCCCCCCC		20.78-
509N-linked_GlycosylationFAKYGNPNETQNNST
HHHHCCCCCCCCCCC		69.7916335952
509N-linked_GlycosylationFAKYGNPNETQNNST
HHHHCCCCCCCCCCC		69.793542989
513N-linked_GlycosylationGNPNETQNNSTSWPV
CCCCCCCCCCCCCCC		52.4117355286
514N-linked_GlycosylationNPNETQNNSTSWPVF
CCCCCCCCCCCCCCC		36.5316335952
514N-linked_GlycosylationNPNETQNNSTSWPVF
CCCCCCCCCCCCCCC		36.533542989
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CHLE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHLE_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CHLE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHLE_HUMANBCHEphysical
10529218
COLQ_HUMANCOLQphysical
10529218
LOXL1_HUMANLOXL1physical
28514442
ENTP5_HUMANENTPD5physical
28514442
LTBP1_HUMANLTBP1physical
28514442
NAF1_HUMANNAF1physical
28514442
ACTN3_HUMANACTN3physical
28514442
PALLD_HUMANPALLDphysical
28514442
SHOT1_HUMANKIAA1598physical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
DKC1_HUMANDKC1physical
28514442
MANEL_HUMANMANEALphysical
28514442
DIAP3_HUMANDIAPH3physical
28514442
FBX2_HUMANFBXO2physical
28514442
NOP10_HUMANNOP10physical
28514442
CTGE5_HUMANCTAGE5physical
28514442
F120A_HUMANFAM120Aphysical
28514442
SF01_HUMANSF1physical
28514442
ASPH_HUMANASPHphysical
28514442
WASL_HUMANWASLphysical
28514442
CPSF7_HUMANCPSF7physical
28514442
NHP2_HUMANNHP2physical
28514442
ENAH_HUMANENAHphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
177400Butyrylcholinesterase deficiency (BChE deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHLE_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.

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