EST2_HUMAN - dbPTM
EST2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EST2_HUMAN
UniProt AC O00748
Protein Name Cocaine esterase
Gene Name CES2
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Endoplasmic reticulum lumen.
Protein Description Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine..
Protein Sequence MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL
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
2Phosphorylation------MRLHRLRAR
------CCHHHHHHH
38.92-
5Phosphorylation---MRLHRLRARLSA
---CCHHHHHHHHHH
30.38-
7Phosphorylation-MRLHRLRARLSAVA
-CCHHHHHHHHHHHH
20.02-
27Pyrrolidone_carboxylic_acidLLVRGQGQDSASPIR
HHHHCCCCCCCCCCC
33.33-
27Pyrrolidone_carboxylic_acidLLVRGQGQDSASPIR
HHHHCCCCCCCCCCC
33.33-
38PhosphorylationSPIRTTHTGQVLGSL
CCCCCCCCCCEEEEE
27.50-
41PhosphorylationRTTHTGQVLGSLVHV
CCCCCCCEEEEEEEE
7.46-
44PhosphorylationHTGQVLGSLVHVKGA
CCCCEEEEEEEECCC
24.0623312004
58PhosphorylationANAGVQTFLGIPFAK
CCCCCEEECCCCCCC
3.08-
60PhosphorylationAGVQTFLGIPFAKPP
CCCEEECCCCCCCCC
22.72-
61PhosphorylationGVQTFLGIPFAKPPL
CCEEECCCCCCCCCC
2.49-
64PhosphorylationTFLGIPFAKPPLGPL
EECCCCCCCCCCCCC
20.35-
108PhosphorylationAVESEFLSQFNMTFP
HHHHHHHHHCCCCCC
37.74-
111N-linked_GlycosylationSEFLSQFNMTFPSDS
HHHHHHCCCCCCCCC
22.4319159218
116PhosphorylationQFNMTFPSDSMSEDC
HCCCCCCCCCCCCCE
37.8221601212
175N-linked_GlycosylationENVVVVIIQYRLGVL
HCEEEEEEEHHHCCC
1.6719159218
276N-linked_GlycosylationVISTVVANLSACDQV
HHHHHHHHHHHCCCC
23.95UniProtKB CARBOHYD
368PhosphorylationKEMDREASQAALQKM
HHHHHHHHHHHHHHH
18.66-
489AcetylationQLSRKMMKYWANFAR
HHHHHHHHHHHHHHH
33.867308067
539AcetylationAHRLQFWKKALPQKI
HHHHHHHHHHHHHHH
29.4727178108
609Ubiquitination---------------------------------------------------------
---------------------------------------------------------
-

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 EST2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EST2_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 EST2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EST2_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EST2_HUMAN

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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-111, AND MASSSPECTROMETRY.

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