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Protein

Liver carboxylesterase 1

Gene

CES1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.PROSITE-ProRule annotation
4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate.

Enzyme regulationi

Activated by CHAPS.1 Publication

Kineticsi

  1. KM=106.6 µM for p-nitrophenyl acetate4 Publications
  2. KM=775.7 µM for L-methylphenidate4 Publications
  3. KM=663.5 µM for D-methylphenidate4 Publications
  4. KM=116 µM for cocaine4 Publications
  5. KM=43 mM for ethanol4 Publications
  6. KM=0.8 mM for 4-methylumbelliferyl acetate4 Publications
  7. KM=6.3 mM for heroin4 Publications
  8. KM=8.3 mM for 6-monoacetylmorphine4 Publications

Vmax=493.9 nmol/min/mg enzyme with p-nitrophenyl acetate as substrate4 Publications

Vmax=1701.1 pmol/min/mg enzyme with L-methylphenidate as substrate4 Publications

Vmax=177.2 pmol/min/mg enzyme with D-methylphenidate as substrate4 Publications

pH dependencei

Optimum pH is 6.5.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211Acyl-ester intermediatePROSITE-ProRule annotation1 Publication
Active sitei354 – 3541Charge relay system1 Publication
Active sitei468 – 4681Charge relay system1 Publication

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: ProtInc
  2. methylumbelliferyl-acetate deacetylase activity Source: UniProtKB-EC

GO - Biological processi

  1. epithelial cell differentiation Source: UniProtKB
  2. metabolic process Source: ProtInc
  3. response to toxic substance Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:HS11616-MONOMER.
BRENDAi3.1.1.1. 2681.
SABIO-RKP23141.

Protein family/group databases

MEROPSiS09.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Liver carboxylesterase 1
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase
Short name:
ACAT
Brain carboxylesterase hBr1
Carboxylesterase 1 (EC:3.1.1.1)
Short name:
CE-1
Short name:
hCE-1
Cocaine carboxylesterase
Egasyn
HMSE
Methylumbelliferyl-acetate deacetylase 1 (EC:3.1.1.56)
Monocyte/macrophage serine esterase
Retinyl ester hydrolase
Short name:
REH
Serine esterase 1
Triacylglycerol hydrolase
Short name:
TGH
Gene namesi
Name:CES1
Synonyms:CES2, SES1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 16, Unplaced

Organism-specific databases

HGNCiHGNC:1863. CES1.

Subcellular locationi

  1. Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. extracellular space Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791N → A: Abolishes glycosylation. 1 Publication
Mutagenesisi221 – 2211S → A: Loss of activity. 1 Publication
Mutagenesisi354 – 3541E → A: Loss of activity. 1 Publication
Mutagenesisi468 – 4681H → A: Loss of activity. 1 Publication
Mutagenesisi564 – 5674Missing : Does not result in secretion. 1 Publication

Organism-specific databases

MIMi114835. gene+phenotype.
PharmGKBiPA107.

Chemistry

DrugBankiDB01086. Benzocaine.
DB01101. Capecitabine.
DB01410. Ciclesonide.
DB00758. Clopidogrel.
DB04838. Cyclandelate.
DB06695. Dabigatran etexilate.
DB00328. Indomethacin.
DB00762. Irinotecan.
DB00583. L-Carnitine.
DB00688. Mycophenolate mofetil.
DB00198. Oseltamivir.
DB01599. Probucol.
DB06201. Rufinamide.
DB00675. Tamoxifen.
DB00519. Trandolapril.

Polymorphism and mutation databases

BioMutaiCES1.
DMDMi119576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17172 PublicationsAdd
BLAST
Chaini18 – 567550Liver carboxylesterase 1PRO_0000391359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 116
Disulfide bondi274 ↔ 285
Modified residuei380 – 3801Phosphoserine1 Publication

Post-translational modificationi

Contains sialic acid.
Cleavage of the signal sequence can occur at 2 positions, either between Trp-17 and Gly-18 or between Gly-18 and His-19.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP23141.
PRIDEiP23141.

PTM databases

PhosphoSiteiP23141.

Expressioni

Tissue specificityi

Expressed predominantly in liver with lower levels in heart and lung.1 Publication

Gene expression databases

BgeeiP23141.
CleanExiHS_CES1.
HS_CES2.
ExpressionAtlasiP23141. baseline and differential.
GenevestigatoriP23141.

Organism-specific databases

HPAiHPA012023.
HPA046717.

Interactioni

Subunit structurei

Homotrimer and homohexamer. Binds to beta-glucuronidase.4 Publications

Protein-protein interaction databases

BioGridi107494. 2 interactions.
IntActiP23141. 1 interaction.
MINTiMINT-5004142.

Structurei

Secondary structure

1
567
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 284Combined sources
Beta strandi31 – 344Combined sources
Beta strandi36 – 383Combined sources
Beta strandi47 – 548Combined sources
Helixi61 – 633Combined sources
Beta strandi75 – 795Combined sources
Beta strandi86 – 883Combined sources
Helixi91 – 10111Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi118 – 1236Combined sources
Turni127 – 1304Combined sources
Beta strandi133 – 1397Combined sources
Turni143 – 1453Combined sources
Helixi149 – 1513Combined sources
Helixi155 – 1617Combined sources
Beta strandi164 – 1685Combined sources
Helixi173 – 1775Combined sources
Helixi183 – 1853Combined sources
Helixi189 – 20416Combined sources
Helixi205 – 2084Combined sources
Beta strandi210 – 22011Combined sources
Helixi222 – 23211Combined sources
Helixi234 – 2363Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2477Combined sources
Helixi253 – 2553Combined sources
Helixi262 – 27110Combined sources
Helixi279 – 28810Combined sources
Helixi291 – 30111Combined sources
Turni302 – 3043Combined sources
Beta strandi308 – 3103Combined sources
Helixi312 – 3143Combined sources
Beta strandi325 – 3273Combined sources
Helixi332 – 3354Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi346 – 3516Combined sources
Turni352 – 3554Combined sources
Helixi358 – 3614Combined sources
Turni363 – 3653Combined sources
Beta strandi369 – 3713Combined sources
Helixi375 – 38410Combined sources
Helixi386 – 3894Combined sources
Helixi393 – 3953Combined sources
Helixi396 – 4049Combined sources
Helixi410 – 42516Combined sources
Helixi427 – 43913Combined sources
Beta strandi444 – 4507Combined sources
Beta strandi458 – 4603Combined sources
Turni468 – 4714Combined sources
Helixi472 – 4754Combined sources
Helixi478 – 4803Combined sources
Helixi487 – 50620Combined sources
Beta strandi521 – 5233Combined sources
Beta strandi525 – 5328Combined sources
Beta strandi534 – 5374Combined sources
Helixi541 – 55212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MX1X-ray2.40A/B/C/D/E/F19-567[»]
1MX5X-ray2.80A/B/C/D/E/F19-567[»]
1MX9X-ray2.90A/B/C/D/E/F/G/H/I/J/K/L19-567[»]
1YA4X-ray3.20A/B/C21-552[»]
1YA8X-ray3.00A/B/C21-552[»]
1YAHX-ray3.00A/B/C21-552[»]
1YAJX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L21-552[»]
2DQYX-ray3.00A/B/C19-561[»]
2DQZX-ray2.80A/B/C19-561[»]
2DR0X-ray3.20A/B/C19-561[»]
2H7CX-ray2.00A/B/C/D/E/F19-561[»]
2HRQX-ray2.70A/B/C/D/E/F21-553[»]
2HRRX-ray2.70A/B/C21-553[»]
3K9BX-ray3.10A/B/C24-553[»]
4AB1X-ray2.20A21-553[»]
ProteinModelPortaliP23141.
SMRiP23141. Positions 21-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23141.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP23141.
KOiK01044.
OMAiRENITAF.
OrthoDBiEOG75XGKD.
PhylomeDBiP23141.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P23141-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWLRAFILAT LSASAAWGHP SSPPVVDTVH GKVLGKFVSL EGFAQPVAIF
60 70 80 90 100
LGIPFAKPPL GPLRFTPPQP AEPWSFVKNA TSYPPMCTQD PKAGQLLSEL
110 120 130 140 150
FTNRKENIPL KLSEDCLYLN IYTPADLTKK NRLPVMVWIH GGGLMVGAAS
160 170 180 190 200
TYDGLALAAH ENVVVVTIQY RLGIWGFFST GDEHSRGNWG HLDQVAALRW
210 220 230 240 250
VQDNIASFGG NPGSVTIFGE SAGGESVSVL VLSPLAKNLF HRAISESGVA
260 270 280 290 300
LTSVLVKKGD VKPLAEQIAI TAGCKTTTSA VMVHCLRQKT EEELLETTLK
310 320 330 340 350
MKFLSLDLQG DPRESQPLLG TVIDGMLLLK TPEELQAERN FHTVPYMVGI
360 370 380 390 400
NKQEFGWLIP MQLMSYPLSE GQLDQKTAMS LLWKSYPLVC IAKELIPEAT
410 420 430 440 450
EKYLGGTDDT VKKKDLFLDL IADVMFGVPS VIVARNHRDA GAPTYMYEFQ
460 470 480 490 500
YRPSFSSDMK PKTVIGDHGD ELFSVFGAPF LKEGASEEEI RLSKMVMKFW
510 520 530 540 550
ANFARNGNPN GEGLPHWPEY NQKEGYLQIG ANTQAAQKLK DKEVAFWTNL
560
FAKKAVEKPP QTEHIEL
Length:567
Mass (Da):62,521
Last modified:August 1, 1992 - v2
Checksum:iD3A00BDCDC7E5DFF
GO
Isoform 2 (identifier: P23141-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     17-17: W → WA

Show »
Length:568
Mass (Da):62,592
Checksum:iAEC3C3DB33D1DDAC
GO
Isoform 3 (identifier: P23141-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     362-362: Missing.

Show »
Length:566
Mass (Da):62,393
Checksum:iAE8F6F2B7004416D
GO

Sequence cautioni

The sequence AAA83932.1 differs from that shown. Reason: Frameshift at positions 301, 312, 318, 383 and 391. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21W → L in AAD53175 (PubMed:10562416).Curated
Sequence conflicti4 – 74RAFI → PALV in BAA04650 (PubMed:8406473).Curated
Sequence conflicti4 – 74RAFI → PALV in BAC87749 (Ref. 8) Curated
Sequence conflicti4 – 74RAFI → PALV in BAC87751 (Ref. 8) Curated
Sequence conflicti4 – 74RAFI → PALV in BAF83312 (PubMed:14702039).Curated
Sequence conflicti4 – 74RAFI → PALV in BAF84898 (PubMed:14702039).Curated
Sequence conflicti4 – 74RAFI → PALV in AAH12418 (PubMed:15489334).Curated
Sequence conflicti12 – 121S → A in BAA04650 (PubMed:8406473).Curated
Sequence conflicti12 – 121S → A in BAC87749 (Ref. 8) Curated
Sequence conflicti12 – 121S → A in BAC87751 (Ref. 8) Curated
Sequence conflicti12 – 121S → A in BAF83312 (PubMed:14702039).Curated
Sequence conflicti12 – 121S → A in BAF84898 (PubMed:14702039).Curated
Sequence conflicti12 – 121S → A in AAH12418 (PubMed:15489334).Curated
Sequence conflicti19 – 213HPS → GPP AA sequence (PubMed:8597091).Curated
Sequence conflicti19 – 191H → N AA sequence (PubMed:9490062).Curated
Sequence conflicti21 – 244SSPP → EAVV AA sequence (PubMed:9490062).Curated
Sequence conflicti27 – 282DT → AK AA sequence (PubMed:9490062).Curated
Sequence conflicti28 – 292TV → DT AA sequence (PubMed:8597091).Curated
Sequence conflicti56 – 561A → G in AAA16036 (PubMed:8218228).Curated
Sequence conflicti56 – 561A → G in AAA35711 (PubMed:8218228).Curated
Sequence conflicti64 – 641R → G in CAA37147 (PubMed:2070086).Curated
Sequence conflicti65 – 651F → S in AAP20868 (PubMed:11015575).Curated
Sequence conflicti75 – 751S → A AA sequence (PubMed:9490062).Curated
Sequence conflicti78 – 781K → I AA sequence (PubMed:9490062).Curated
Sequence conflicti89 – 891Q → R in AAP20868 (PubMed:11015575).Curated
Sequence conflicti98 – 981S → F AA sequence (PubMed:9490062).Curated
Sequence conflicti105 – 1073KEN → PAD AA sequence (PubMed:9490062).Curated
Sequence conflicti115 – 1151D → H in AAA83932 (PubMed:1748313).Curated
Sequence conflicti186 – 1861R → G in CAA37147 (PubMed:2070086).Curated
Sequence conflicti247 – 2471S → I AA sequence (PubMed:9490062).Curated
Sequence conflicti251 – 2511L → K AA sequence (PubMed:9490062).Curated
Sequence conflicti253 – 2531S → G AA sequence (PubMed:9490062).Curated
Sequence conflicti255 – 2551L → P in BAF83312 (PubMed:14702039).Curated
Sequence conflicti258 – 2581K → Q AA sequence (PubMed:9490062).Curated
Sequence conflicti281 – 2811V → A in AAA83932 (PubMed:1748313).Curated
Sequence conflicti298 – 2981T → I AA sequence (PubMed:9490062).Curated
Sequence conflicti302 – 3021K → A AA sequence (PubMed:9490062).Curated
Sequence conflicti305 – 3051S → M AA sequence (PubMed:9490062).Curated
Sequence conflicti337 – 3371A → R in AAA83932 (PubMed:1748313).Curated
Sequence conflicti417 – 4171F → I in AAA83932 (PubMed:1748313).Curated
Sequence conflicti512 – 5121E → K in AAA83932 (PubMed:1748313).Curated
Sequence conflicti536 – 5361A → G in AAA16036 (PubMed:8218228).Curated
Sequence conflicti536 – 5361A → G in AAA35711 (PubMed:8218228).Curated
Sequence conflicti563 – 5631E → D in AAA83932 (PubMed:1748313).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181G → GA.
VAR_002357
Natural varianti75 – 751S → N.
Corresponds to variant rs2307240 [ dbSNP | Ensembl ].
VAR_014314
Natural varianti143 – 1431G → E 5.4-fold decrease in activity with p-nitrophenyl acetate as substrate; no change in affinity for p-nitrophenyl acetate; loss of activity with L- or D-methylphenidate as substrate. 1 Publication
Corresponds to variant rs71647871 [ dbSNP | Ensembl ].
VAR_046954
Natural varianti199 – 1991R → H.
Corresponds to variant rs2307243 [ dbSNP | Ensembl ].
VAR_014594
Natural varianti203 – 2031D → E.
Corresponds to variant rs2307227 [ dbSNP | Ensembl ].
VAR_014595

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei17 – 171W → WA in isoform 2. 2 PublicationsVSP_021026
Alternative sequencei362 – 3621Missing in isoform 3. 2 PublicationsVSP_047158

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73499 mRNA. Translation: AAA35649.1.
L07764 mRNA. Translation: AAA16036.1.
L07765 mRNA. Translation: AAA35711.1.
D21088 Genomic DNA. Translation: BAA04650.1.
S73751 mRNA. Translation: AAC60631.2.
AF177775 mRNA. Translation: AAD53175.1.
AY268104 mRNA. Translation: AAP20868.1.
AB119995 mRNA. Translation: BAC87748.1.
AB119996 mRNA. Translation: BAC87749.1.
AB119997 Genomic DNA. Translation: BAC87750.1.
AB119998 Genomic DNA. Translation: BAC87751.1.
AK290623 mRNA. Translation: BAF83312.1.
AK292209 mRNA. Translation: BAF84898.1.
AC147362 Genomic DNA. No translation available.
BC012418 mRNA. Translation: AAH12418.1.
BC110338 mRNA. Translation: AAI10339.1.
AB025026 mRNA. Translation: BAA84995.1.
M55509 mRNA. Translation: AAA35650.1.
X52973 mRNA. Translation: CAA37147.1.
M65261 mRNA. Translation: AAA83932.1. Frameshift.
CCDSiCCDS32450.1. [P23141-2]
CCDS45488.1. [P23141-1]
CCDS45489.1. [P23141-3]
PIRiA41010.
RefSeqiNP_001020365.1. NM_001025194.1. [P23141-1]
NP_001020366.1. NM_001025195.1. [P23141-2]
NP_001257.4. NM_001266.4. [P23141-3]
UniGeneiHs.558865.

Genome annotation databases

EnsembliENST00000360526; ENSP00000353720; ENSG00000198848. [P23141-2]
ENST00000361503; ENSP00000355193; ENSG00000198848. [P23141-1]
ENST00000422046; ENSP00000390492; ENSG00000198848. [P23141-3]
ENST00000571922; ENSP00000460045; ENSG00000262243.
ENST00000574513; ENSP00000461208; ENSG00000262243.
ENST00000576783; ENSP00000458586; ENSG00000262243.
GeneIDi1066.
KEGGihsa:1066.
UCSCiuc002eil.3. human. [P23141-2]
uc002eim.3. human. [P23141-1]

Polymorphism and mutation databases

BioMutaiCES1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73499 mRNA. Translation: AAA35649.1.
L07764 mRNA. Translation: AAA16036.1.
L07765 mRNA. Translation: AAA35711.1.
D21088 Genomic DNA. Translation: BAA04650.1.
S73751 mRNA. Translation: AAC60631.2.
AF177775 mRNA. Translation: AAD53175.1.
AY268104 mRNA. Translation: AAP20868.1.
AB119995 mRNA. Translation: BAC87748.1.
AB119996 mRNA. Translation: BAC87749.1.
AB119997 Genomic DNA. Translation: BAC87750.1.
AB119998 Genomic DNA. Translation: BAC87751.1.
AK290623 mRNA. Translation: BAF83312.1.
AK292209 mRNA. Translation: BAF84898.1.
AC147362 Genomic DNA. No translation available.
BC012418 mRNA. Translation: AAH12418.1.
BC110338 mRNA. Translation: AAI10339.1.
AB025026 mRNA. Translation: BAA84995.1.
M55509 mRNA. Translation: AAA35650.1.
X52973 mRNA. Translation: CAA37147.1.
M65261 mRNA. Translation: AAA83932.1. Frameshift.
CCDSiCCDS32450.1. [P23141-2]
CCDS45488.1. [P23141-1]
CCDS45489.1. [P23141-3]
PIRiA41010.
RefSeqiNP_001020365.1. NM_001025194.1. [P23141-1]
NP_001020366.1. NM_001025195.1. [P23141-2]
NP_001257.4. NM_001266.4. [P23141-3]
UniGeneiHs.558865.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MX1X-ray2.40A/B/C/D/E/F19-567[»]
1MX5X-ray2.80A/B/C/D/E/F19-567[»]
1MX9X-ray2.90A/B/C/D/E/F/G/H/I/J/K/L19-567[»]
1YA4X-ray3.20A/B/C21-552[»]
1YA8X-ray3.00A/B/C21-552[»]
1YAHX-ray3.00A/B/C21-552[»]
1YAJX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L21-552[»]
2DQYX-ray3.00A/B/C19-561[»]
2DQZX-ray2.80A/B/C19-561[»]
2DR0X-ray3.20A/B/C19-561[»]
2H7CX-ray2.00A/B/C/D/E/F19-561[»]
2HRQX-ray2.70A/B/C/D/E/F21-553[»]
2HRRX-ray2.70A/B/C21-553[»]
3K9BX-ray3.10A/B/C24-553[»]
4AB1X-ray2.20A21-553[»]
ProteinModelPortaliP23141.
SMRiP23141. Positions 21-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107494. 2 interactions.
IntActiP23141. 1 interaction.
MINTiMINT-5004142.

Chemistry

BindingDBiP23141.
ChEMBLiCHEMBL2265.
DrugBankiDB01086. Benzocaine.
DB01101. Capecitabine.
DB01410. Ciclesonide.
DB00758. Clopidogrel.
DB04838. Cyclandelate.
DB06695. Dabigatran etexilate.
DB00328. Indomethacin.
DB00762. Irinotecan.
DB00583. L-Carnitine.
DB00688. Mycophenolate mofetil.
DB00198. Oseltamivir.
DB01599. Probucol.
DB06201. Rufinamide.
DB00675. Tamoxifen.
DB00519. Trandolapril.
GuidetoPHARMACOLOGYi2592.

Protein family/group databases

MEROPSiS09.982.

PTM databases

PhosphoSiteiP23141.

Polymorphism and mutation databases

BioMutaiCES1.
DMDMi119576.

Proteomic databases

MaxQBiP23141.
PRIDEiP23141.

Protocols and materials databases

DNASUi1066.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360526; ENSP00000353720; ENSG00000198848. [P23141-2]
ENST00000361503; ENSP00000355193; ENSG00000198848. [P23141-1]
ENST00000422046; ENSP00000390492; ENSG00000198848. [P23141-3]
ENST00000571922; ENSP00000460045; ENSG00000262243.
ENST00000574513; ENSP00000461208; ENSG00000262243.
ENST00000576783; ENSP00000458586; ENSG00000262243.
GeneIDi1066.
KEGGihsa:1066.
UCSCiuc002eil.3. human. [P23141-2]
uc002eim.3. human. [P23141-1]

Organism-specific databases

CTDi1066.
GeneCardsiGC16M055836.
HGNCiHGNC:1863. CES1.
HPAiHPA012023.
HPA046717.
MIMi114835. gene+phenotype.
neXtProtiNX_P23141.
PharmGKBiPA107.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP23141.
KOiK01044.
OMAiRENITAF.
OrthoDBiEOG75XGKD.
PhylomeDBiP23141.
TreeFamiTF315470.

Enzyme and pathway databases

BioCyciMetaCyc:HS11616-MONOMER.
BRENDAi3.1.1.1. 2681.
SABIO-RKP23141.

Miscellaneous databases

ChiTaRSiCES1. human.
EvolutionaryTraceiP23141.
GeneWikiiCarboxylesterase_1.
GenomeRNAii1066.
NextBioi4450.
PROiP23141.
SOURCEiSearch...

Gene expression databases

BgeeiP23141.
CleanExiHS_CES1.
HS_CES2.
ExpressionAtlasiP23141. baseline and differential.
GenevestigatoriP23141.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases."
    Munger J.S., Shi G.P., Mark E.A., Chin D.T., Gerard C., Chapman H.A.
    J. Biol. Chem. 266:18832-18838(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms."
    Kroetz D.L., McBride O.W., Gonzalez F.J.
    Biochemistry 32:11606-11617(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Liver.
  3. "Molecular cloning and characterization of a human carboxylesterase gene."
    Shibata F., Takagi Y., Kitajima M., Kuroda T., Omura T.
    Genomics 17:76-82(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Peripheral blood and Placenta.
  4. "Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase."
    Becker A., Bottcher A., Lackner K.J., Fehringer P., Notka F., Aslanidis C., Schmitz G.
    Arterioscler. Thromb. 14:1346-1355(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C-terminus of beta-glucuronidase is involved in their interaction."
    Islam M.R., Waheed A., Shah G.N., Tomatsu S., Sly W.S.
    Arch. Biochem. Biophys. 372:53-61(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH BETA-GLUCURONIDASE.
    Tissue: Liver.
  6. "Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA."
    Ghosh S.
    Physiol. Genomics 2:1-8(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Macrophage.
  7. "Heterologous expression, purification, and characterization of human triacylglycerol hydrolase."
    Alam M., Ho S., Vance D.E., Lehner R.
    Protein Expr. Purif. 24:33-42(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 19-28.
    Tissue: Liver.
  8. "Inverted duplication of human carboxylesterase 1(CES1) genes, which are difference in regulation at the transcriptional level."
    Hosokawa M., Yaginuma Y., Watanabe N., Yamamoto N., Tsukada E., Ohhata Y., Satoh T., Chiba K.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Liver.
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Esophagus and Heart.
  10. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Blood and Lung.
  12. "cDNA cloning, characterization and stable expression of novel human brain carboxylesterase."
    Mori M., Hosokawa M., Ogasawara Y., Tsukada E., Chiba K.
    FEBS Lett. 458:17-22(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-429 (ISOFORM 1).
    Tissue: Brain.
  13. "Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine."
    Brzezinski M.R., Abraham T.L., Stone C.L., Dean R.A., Bosron W.F.
    Biochem. Pharmacol. 48:1747-1755(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-27; 37-52; 65-75; 187-198; 258-273; 288-298; 314-319; 340-352; 377-382; 439-461; 463-473; 499-504; 506-514 AND 539-557, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Tissue: Liver.
  14. "Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family."
    Schindler R., Mentlein R., Feldheim W.
    Eur. J. Biochem. 251:863-873(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-28; 65-78; 93-107; 243-255; 258-266; 297-313 AND 341-346, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Liver.
  15. "Molecular aspects of carboxylesterase isoforms in comparison with other esterases."
    Satoh T., Hosokawa M.
    Toxicol. Lett. 82:439-445(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-34, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121; 138-149; 216-224; 351-357 AND 466-471, SUBUNIT.
    Tissue: Liver.
  16. "Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site."
    Alam M., Vance D.E., Lehner R.
    Biochemistry 41:6679-6687(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-28, ACTIVE SITES, GLYCOSYLATION AT ASN-79, MUTAGENESIS OF ASN-79; SER-221; GLU-354; HIS-468 AND 564-HIS--LEU-567.
  17. "Cloning and sequencing of a human liver carboxylesterase isoenzyme."
    Long R.M., Calabrese M.R., Martin B.M., Pohl L.R.
    Life Sci. 48:PL43-PL49(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-567.
    Tissue: Liver.
  18. "cDNA cloning and characterization of human monocyte/macrophage serine esterase-1."
    Zschunke F., Salmassi A., Kreipe H., Buck F., Parwaresch M.R., Radzun H.J.
    Blood 78:506-512(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-567, PARTIAL PROTEIN SEQUENCE.
  19. "Cloning and analysis of a cDNA encoding a human liver carboxylesterase."
    Riddles P.W., Richards L.J., Bowles M.R., Pond S.M.
    Gene 108:289-292(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-567.
    Tissue: Liver.
  20. "Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin."
    Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J., Dean R.A., Bosron W.F.
    J. Biol. Chem. 272:14769-14775(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS METHYLUMBELLIFERYL-ACETATE DEACETYLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  21. "Two CES1 gene mutations lead to dysfunctional carboxylesterase 1 activity in man: clinical significance and molecular basis."
    Zhu H.-J., Patrick K.S., Yuan H.-J., Wang J.-S., Donovan J.L., DeVane C.L., Malcolm R., Johnson J.A., Youngblood G.L., Sweet D.H., Langaee T.Y., Markowitz J.S.
    Am. J. Hum. Genet. 82:1241-1248(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, VARIANT GLU-143, CHARACTERIZATION OF VARIANT GLU-143.
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine. From binding promiscuity to selective inhibition."
    Bencharit S., Morton C.L., Hyatt J.L., Kuhn P., Danks M.K., Potter P.M., Redinbo M.R.
    Chem. Biol. 10:341-349(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
  24. "Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme."
    Bencharit S., Morton C.L., Xue Y., Potter P.M., Redinbo M.R.
    Nat. Struct. Biol. 10:349-356(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.

Entry informationi

Entry nameiEST1_HUMAN
AccessioniPrimary (citable) accession number: P23141
Secondary accession number(s): A6NIM1
, A8K3K8, A8K844, E9PAU8, P82127, Q00015, Q13657, Q14062, Q16737, Q16788, Q549X7, Q549X8, Q86UK2, Q96EE8, Q9UC52, Q9UDG8, Q9UK77, Q9ULY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 1, 1992
Last modified: April 29, 2015
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.