CES1
entrez
1066
canonical
uniprot
P23141
canonical
ensembl
ENSG00000198848
resolver
ensembl
ENSG00000262243
resolver
ensp
ENSP00000353720
resolver
ensp
ENSP00000355193
resolver
ensp
ENSP00000390492
resolver
ensp
ENSP00000458586
resolver
ensp
ENSP00000460045
resolver
ensp
ENSP00000461208
resolver
ensp
ENSP00000575526
resolver
enst
ENST00000571922
resolver
enst
ENST00000574513
resolver
enst
ENST00000576783
resolver
genesymbol
CES1
resolver
genesymbol_syn
CES2
resolver
genesymbol_syn
SES1
resolver
hgnc
HGNC:1863
resolver
uniprot
A6NIM1
resolver
uniprot
A8K3K8
resolver
uniprot
A8K844
resolver
uniprot
E9PAU8
resolver
uniprot
P82127
resolver
uniprot
Q00015
resolver
uniprot
Q13657
resolver
uniprot
Q14062
resolver
uniprot
Q16737
resolver
uniprot
Q16788
resolver
uniprot
Q549X7
resolver
uniprot
Q549X8
resolver
uniprot
Q86UK2
resolver
uniprot
Q96EE8
resolver
uniprot
Q9UC52
resolver
uniprot
Q9UDG8
resolver
uniprot
Q9UK77
resolver
uniprot
Q9ULY2
resolver
uniprot_entry
EST1_HUMAN
resolver
uniprot_sec
A6NIM1
resolver
uniprot_sec
A8K3K8
resolver
uniprot_sec
A8K844
resolver
uniprot_sec
E9PAU8
resolver
uniprot_sec
P82127
resolver
uniprot_sec
Q00015
resolver
uniprot_sec
Q13657
resolver
uniprot_sec
Q14062
resolver
uniprot_sec
Q16737
resolver
uniprot_sec
Q16788
resolver
uniprot_sec
Q549X7
resolver
uniprot_sec
Q549X8
resolver
uniprot_sec
Q86UK2
resolver
uniprot_sec
Q96EE8
resolver
uniprot_sec
Q9UC52
resolver
uniprot_sec
Q9UDG8
resolver
uniprot_sec
Q9UK77
resolver
uniprot_sec
Q9ULY2
resolver
activity_regulation
ACTIVITY REGULATION: Activated by CHAPS (PubMed:9490062). Inhibited by chlorpyrifos oxon (IC(50)=0.21 nM), paraoxon (IC(50)=0.29 nM), or methyl paraoxon (IC(50)=49 nM) (PubMed:18762277). {ECO:0000269|PubMed:18762277, ECO:0000269|PubMed:9490062}.
uniprot
proteins
amino_acid_sequence
MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL
uniprot
proteins
ec_number
3.1.1.1
uniprot
proteins
ec_number
3.1.1.13
uniprot
proteins
ec_number
3.1.1.56
uniprot
proteins
function
FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs (PubMed:18762277, PubMed:7980644, PubMed:9169443, PubMed:9490062). Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester (PubMed:18762277, PubMed:7980644, PubMed:9169443, PubMed:9490062). Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine (PubMed:7980644). Catalyzes the transesterification of cocaine to form cocaethylene (PubMed:7980644). Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate (PubMed:7980644). Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (PubMed:21049984). Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process (PubMed:11015575, PubMed:16024911, PubMed:16971496, PubMed:18762277). First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile (PubMed:16971496, PubMed:18599737, PubMed:18762277). {ECO:0000269|PubMed:11015575, ECO:0000269|PubMed:16024911, ECO:0000269|PubMed:16971496, ECO:0000269|PubMed:18599737, ECO:0000269|PubMed:18762277, ECO:0000269|PubMed:21049984, ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443, ECO:0000269|PubMed:9490062}.
uniprot
proteins
mass_dalton
62521
uniprot
proteins
mutagenesis
MUTAGEN 79; /note="N->A: Abolishes glycosylation."; /evidence="ECO:0000269|PubMed:12022871"; MUTAGEN 221; /note="S->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12022871"; MUTAGEN 354; /note="E->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12022871"; MUTAGEN 468; /note="H->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12022871"; MUTAGEN 564..567; /note="Missing: Does not result in secretion."; /evidence="ECO:0000269|PubMed:12022871
uniprot
proteins
post_translational_modification
PTM: Contains sialic acid.; PTM: Cleavage of the signal sequence can occur at 2 positions, either between Trp-17 and Gly-18 or between Gly-18 and His-19.
uniprot
proteins
protein_family
Type-B carboxylesterase/lipase family
uniprot
proteins
pubmed
10518925
uniprot
proteins
pubmed
10562416
uniprot
proteins
pubmed
11015575
uniprot
proteins
pubmed
11812220
uniprot
proteins
pubmed
12022871
uniprot
proteins
pubmed
12679808
uniprot
proteins
pubmed
12725862
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16024911
uniprot
proteins
pubmed
16971496
uniprot
proteins
pubmed
1748313
uniprot
proteins
pubmed
18485328
uniprot
proteins
pubmed
18599737
uniprot
proteins
pubmed
18762277
uniprot
proteins
pubmed
1918003
uniprot
proteins
pubmed
1997784
uniprot
proteins
pubmed
2070086
uniprot
proteins
pubmed
21049984
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
39190717
uniprot
proteins
pubmed
7980644
uniprot
proteins
pubmed
8049197
uniprot
proteins
pubmed
8218228
uniprot
proteins
pubmed
8406473
uniprot
proteins
pubmed
8597091
uniprot
proteins
pubmed
9169443
uniprot
proteins
pubmed
9490062
uniprot
proteins
sequence_length
567
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:10562416}. Cytoplasm {ECO:0000269|PubMed:16024911}. Lipid droplet {ECO:0000269|PubMed:16024911}. Note=Moves from cytoplasm to lipid droplets upon lipid loading. Associates with lipid droplets independently of triglycerides (TG) content of the droplets and hydrolyzes cholesteryl esters more efficiently from mixed droplets. {ECO:0000269|PubMed:16024911}.
uniprot
proteins