Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Liver carboxylesterase 1  

UniProtKB / Swiss-Prot ID :  EST1_HUMAN

Gene Name (Synonyms) : 
CES1, CES2, SES1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Endoplasmic reticulum lumen. 

Protein Function :  Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. 

Protein Sequence MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQP...
Predicted Secondary Structure CHHHHHHHHHHHHHHCCCCCCCCCEEECCCCEEEEEEEECCCCCCCEEEEECCCCCCCCCCHHHCCCCCC...
Protein Variant
LocationDescription
18G -> GA. VAR_002357
75S -> N (in dbSNP:rs2307240). VAR_014314
143G -> E (5.4-fold decrease in activitywith p-nitrophenyl acetate as substrate;
199R -> H (in dbSNP:rs2307243). VAR_014594
203D -> E (in dbSNP:rs2307227). VAR_014595
362Missing. VAR_002358
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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
79N-linked (GlcNAc...).SFVKNATSY
CCCCCCCCC
43.05UniProtKB
Link
402N6-acetyllysineEATEKYLGG
HHHHHHCCC
41.23Phosphositeplus
Link
558N6-acetyllysineKAVEKPPQT
HHHCCCCCC
56.23Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
EST1_HUMANin vitroHPRD:00268HPRD12679808
12725862
BGLR_HUMANENSP00000353720STRING
BGLR_HUMANENSP00000353720STRING
BGLR_HUMANENSP00000353720STRING
BGLR_HUMANENSP00000353720STRING
BGLR_HUMANENSP00000353720STRING
BGLR_HUMANENSP00000353720STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure-function analysis of human triacylglycerol hydrolase bysite-directed mutagenesis: identification of the catalytic triad and aglycosylation site.";
Alam M., Vance D.E., Lehner R.;
Biochemistry 41:6679-6687(2002).
Cited for: PROTEIN SEQUENCE OF 19-28, ACTIVE SITES, GLYCOSYLATION AT ASN-79, ANDMUTAGENESIS OF ASN-79; SER-221; GLU-354; HIS-468 AND 564-HIS--LEU-567.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures