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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 annotation3 Publications
4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate.1 Publication

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
  1. Vmax=493.9 nmol/min/mg enzyme with p-nitrophenyl acetate as substrate4 Publications
  2. Vmax=1701.1 pmol/min/mg enzyme with L-methylphenidate as substrate4 Publications
  3. 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)DescriptionActionsGraphical viewLength
Active sitei221Acyl-ester intermediatePROSITE-ProRule annotation1 Publication1
Active sitei354Charge relay system1 Publication1
Active sitei468Charge relay system1 Publication1

GO - Molecular functioni

GO - Biological processi

  • cholesterol biosynthetic process Source: BHF-UCL
  • cholesterol ester hydrolysis involved in cholesterol transport Source: BHF-UCL
  • epithelial cell differentiation Source: UniProtKB
  • medium-chain fatty acid metabolic process Source: BHF-UCL
  • metabolic process Source: ProtInc
  • response to toxic substance Source: ProtInc
  • xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:HS11616-MONOMER.
ZFISH:HS02417-MONOMER.
ZFISH:HS11616-MONOMER.
BRENDAi3.1.1.1. 2681.
ReactomeiR-HSA-211945. Phase 1 - Functionalization of compounds.
SABIO-RKP23141.

Protein family/group databases

ESTHERihuman-CES1. Carb_B_Chordata.
MEROPSiS09.982.

Chemistry databases

SwissLipidsiSLP:000001265.

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:3.1.1.13 Publications)
Short name:
CE-1
Short name:
hCE-1
Cocaine carboxylesterase
Egasyn
HMSE
Methylumbelliferyl-acetate deacetylase 1 (EC:3.1.1.561 Publication)
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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1863. CES1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi79N → A: Abolishes glycosylation. 1 Publication1
Mutagenesisi221S → A: Loss of activity. 1 Publication1
Mutagenesisi354E → A: Loss of activity. 1 Publication1
Mutagenesisi468H → A: Loss of activity. 1 Publication1
Mutagenesisi564 – 567Missing : Does not result in secretion. 1 Publication4

Organism-specific databases

DisGeNETi1066.
MIMi114835. gene+phenotype.
OpenTargetsiENSG00000198848.
PharmGKBiPA107.

Chemistry databases

ChEMBLiCHEMBL2265.
DrugBankiDB01086. Benzocaine.
DB01101. Capecitabine.
DB02659. Cholic Acid.
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.
DB11362. Selexipag.
DB00675. Tamoxifen.
DB00519. Trandolapril.
GuidetoPHARMACOLOGYi2592.

Polymorphism and mutation databases

BioMutaiCES1.
DMDMi119576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 172 PublicationsAdd BLAST17
ChainiPRO_000039135918 – 567Liver carboxylesterase 1Add BLAST550

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)1 Publication1
Disulfide bondi87 ↔ 116
Disulfide bondi274 ↔ 285
Modified residuei380PhosphoserineCombined sources1

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.
PaxDbiP23141.
PeptideAtlasiP23141.
PRIDEiP23141.

PTM databases

iPTMnetiP23141.
PhosphoSitePlusiP23141.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000198848.
CleanExiHS_CES1.
HS_CES2.
ExpressionAtlasiP23141. baseline and differential.
GenevisibleiP23141. HS.

Organism-specific databases

HPAiHPA012023.
HPA046717.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107494. 3 interactors.
IntActiP23141. 5 interactors.
MINTiMINT-5004142.
STRINGi9606.ENSP00000353720.

Chemistry databases

BindingDBiP23141.

Structurei

Secondary structure

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 28Combined sources4
Beta strandi31 – 34Combined sources4
Beta strandi36 – 38Combined sources3
Beta strandi47 – 54Combined sources8
Helixi61 – 63Combined sources3
Beta strandi75 – 79Combined sources5
Beta strandi86 – 88Combined sources3
Helixi91 – 101Combined sources11
Beta strandi104 – 106Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi118 – 123Combined sources6
Turni127 – 130Combined sources4
Beta strandi133 – 139Combined sources7
Turni143 – 145Combined sources3
Helixi149 – 151Combined sources3
Helixi155 – 161Combined sources7
Beta strandi164 – 168Combined sources5
Helixi173 – 177Combined sources5
Helixi183 – 185Combined sources3
Helixi189 – 204Combined sources16
Helixi205 – 208Combined sources4
Beta strandi210 – 220Combined sources11
Helixi222 – 231Combined sources10
Helixi234 – 236Combined sources3
Turni237 – 239Combined sources3
Beta strandi241 – 247Combined sources7
Helixi253 – 255Combined sources3
Helixi262 – 272Combined sources11
Helixi279 – 288Combined sources10
Helixi291 – 301Combined sources11
Turni302 – 304Combined sources3
Beta strandi308 – 310Combined sources3
Helixi312 – 314Combined sources3
Beta strandi325 – 327Combined sources3
Helixi332 – 338Combined sources7
Beta strandi339 – 341Combined sources3
Beta strandi346 – 351Combined sources6
Turni352 – 355Combined sources4
Helixi358 – 361Combined sources4
Turni363 – 365Combined sources3
Beta strandi369 – 371Combined sources3
Helixi375 – 384Combined sources10
Helixi386 – 389Combined sources4
Helixi393 – 395Combined sources3
Helixi396 – 404Combined sources9
Helixi410 – 425Combined sources16
Helixi427 – 439Combined sources13
Beta strandi444 – 450Combined sources7
Beta strandi458 – 460Combined sources3
Turni468 – 471Combined sources4
Helixi472 – 475Combined sources4
Helixi478 – 480Combined sources3
Helixi487 – 506Combined sources20
Beta strandi521 – 523Combined sources3
Beta strandi525 – 532Combined sources8
Beta strandi534 – 537Combined sources4
Helixi541 – 551Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A7FX-ray1.86A21-553[»]
5A7GX-ray1.48A21-553[»]
5A7HX-ray2.01A22-553[»]
ProteinModelPortaliP23141.
SMRiP23141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23141.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP23141.
KOiK01044.
OMAiEYGPACA.
OrthoDBiEOG091G03ZC.
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 differs from that shown. Reason: Frameshift at positions 301, 312, 318, 383 and 391.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2W → L in AAD53175 (PubMed:10562416).Curated1
Sequence conflicti4 – 7RAFI → PALV in BAA04650 (PubMed:8406473).Curated4
Sequence conflicti4 – 7RAFI → PALV in BAC87749 (Ref. 8) Curated4
Sequence conflicti4 – 7RAFI → PALV in BAC87751 (Ref. 8) Curated4
Sequence conflicti4 – 7RAFI → PALV in BAF83312 (PubMed:14702039).Curated4
Sequence conflicti4 – 7RAFI → PALV in BAF84898 (PubMed:14702039).Curated4
Sequence conflicti4 – 7RAFI → PALV in AAH12418 (PubMed:15489334).Curated4
Sequence conflicti12S → A in BAA04650 (PubMed:8406473).Curated1
Sequence conflicti12S → A in BAC87749 (Ref. 8) Curated1
Sequence conflicti12S → A in BAC87751 (Ref. 8) Curated1
Sequence conflicti12S → A in BAF83312 (PubMed:14702039).Curated1
Sequence conflicti12S → A in BAF84898 (PubMed:14702039).Curated1
Sequence conflicti12S → A in AAH12418 (PubMed:15489334).Curated1
Sequence conflicti19 – 21HPS → GPP AA sequence (PubMed:8597091).Curated3
Sequence conflicti19H → N AA sequence (PubMed:9490062).Curated1
Sequence conflicti21 – 24SSPP → EAVV AA sequence (PubMed:9490062).Curated4
Sequence conflicti27 – 28DT → AK AA sequence (PubMed:9490062).Curated2
Sequence conflicti28 – 29TV → DT AA sequence (PubMed:8597091).Curated2
Sequence conflicti56A → G in AAA16036 (PubMed:8218228).Curated1
Sequence conflicti56A → G in AAA35711 (PubMed:8218228).Curated1
Sequence conflicti64R → G in CAA37147 (PubMed:2070086).Curated1
Sequence conflicti65F → S in AAP20868 (PubMed:11015575).Curated1
Sequence conflicti75S → A AA sequence (PubMed:9490062).Curated1
Sequence conflicti78K → I AA sequence (PubMed:9490062).Curated1
Sequence conflicti89Q → R in AAP20868 (PubMed:11015575).Curated1
Sequence conflicti98S → F AA sequence (PubMed:9490062).Curated1
Sequence conflicti105 – 107KEN → PAD AA sequence (PubMed:9490062).Curated3
Sequence conflicti115D → H in AAA83932 (PubMed:1748313).Curated1
Sequence conflicti186R → G in CAA37147 (PubMed:2070086).Curated1
Sequence conflicti247S → I AA sequence (PubMed:9490062).Curated1
Sequence conflicti251L → K AA sequence (PubMed:9490062).Curated1
Sequence conflicti253S → G AA sequence (PubMed:9490062).Curated1
Sequence conflicti255L → P in BAF83312 (PubMed:14702039).Curated1
Sequence conflicti258K → Q AA sequence (PubMed:9490062).Curated1
Sequence conflicti281V → A in AAA83932 (PubMed:1748313).Curated1
Sequence conflicti298T → I AA sequence (PubMed:9490062).Curated1
Sequence conflicti302K → A AA sequence (PubMed:9490062).Curated1
Sequence conflicti305S → M AA sequence (PubMed:9490062).Curated1
Sequence conflicti337A → R in AAA83932 (PubMed:1748313).Curated1
Sequence conflicti417F → I in AAA83932 (PubMed:1748313).Curated1
Sequence conflicti512E → K in AAA83932 (PubMed:1748313).Curated1
Sequence conflicti536A → G in AAA16036 (PubMed:8218228).Curated1
Sequence conflicti536A → G in AAA35711 (PubMed:8218228).Curated1
Sequence conflicti563E → D in AAA83932 (PubMed:1748313).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00235718G → GA.1
Natural variantiVAR_01431475S → N.Corresponds to variant rs2307240dbSNPEnsembl.1
Natural variantiVAR_046954143G → 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 PublicationCorresponds to variant rs71647871dbSNPEnsembl.1
Natural variantiVAR_014594199R → H.Corresponds to variant rs2307243dbSNPEnsembl.1
Natural variantiVAR_014595203D → E.Corresponds to variant rs2307227dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02102617W → WA in isoform 2. 2 Publications1
Alternative sequenceiVSP_047158362Missing in isoform 3. 2 Publications1

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.4. human. [P23141-1]

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
PDB 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[»]
5A7FX-ray1.86A21-553[»]
5A7GX-ray1.48A21-553[»]
5A7HX-ray2.01A22-553[»]
ProteinModelPortaliP23141.
SMRiP23141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107494. 3 interactors.
IntActiP23141. 5 interactors.
MINTiMINT-5004142.
STRINGi9606.ENSP00000353720.

Chemistry databases

BindingDBiP23141.
ChEMBLiCHEMBL2265.
DrugBankiDB01086. Benzocaine.
DB01101. Capecitabine.
DB02659. Cholic Acid.
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.
DB11362. Selexipag.
DB00675. Tamoxifen.
DB00519. Trandolapril.
GuidetoPHARMACOLOGYi2592.
SwissLipidsiSLP:000001265.

Protein family/group databases

ESTHERihuman-CES1. Carb_B_Chordata.
MEROPSiS09.982.

PTM databases

iPTMnetiP23141.
PhosphoSitePlusiP23141.

Polymorphism and mutation databases

BioMutaiCES1.
DMDMi119576.

Proteomic databases

MaxQBiP23141.
PaxDbiP23141.
PeptideAtlasiP23141.
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.4. human. [P23141-1]

Organism-specific databases

CTDi1066.
DisGeNETi1066.
GeneCardsiCES1.
HGNCiHGNC:1863. CES1.
HPAiHPA012023.
HPA046717.
MIMi114835. gene+phenotype.
neXtProtiNX_P23141.
OpenTargetsiENSG00000198848.
PharmGKBiPA107.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOVERGENiHBG008839.
InParanoidiP23141.
KOiK01044.
OMAiEYGPACA.
OrthoDBiEOG091G03ZC.
PhylomeDBiP23141.
TreeFamiTF315470.

Enzyme and pathway databases

BioCyciMetaCyc:HS11616-MONOMER.
ZFISH:HS02417-MONOMER.
ZFISH:HS11616-MONOMER.
BRENDAi3.1.1.1. 2681.
ReactomeiR-HSA-211945. Phase 1 - Functionalization of compounds.
SABIO-RKP23141.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000198848.
CleanExiHS_CES1.
HS_CES2.
ExpressionAtlasiP23141. baseline and differential.
GenevisibleiP23141. HS.

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...

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: November 30, 2016
This is version 178 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

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 one 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.