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P23141

- EST1_HUMAN

UniProt

P23141 - EST1_HUMAN

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Protein

Liver carboxylesterase 1

Gene
CES1, CES2, SES1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.3 Publications
4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate.3 Publications

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-methylphenidate
  3. KM=663.5 µM for D-methylphenidate
  4. KM=116 µM for cocaine
  5. KM=43 mM for ethanol
  6. KM=0.8 mM for 4-methylumbelliferyl acetate
  7. KM=6.3 mM for heroin
  8. KM=8.3 mM for 6-monoacetylmorphine

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

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

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

pH dependencei

Optimum pH is 6.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211Acyl-ester intermediate1 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: UniProt
  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: Chromosome 16

Organism-specific databases

HGNCiHGNC:1863. CES1.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
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.

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

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

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.
GenevestigatoriP23141.

Organism-specific databases

HPAiHPA012023.
HPA046717.

Interactioni

Subunit structurei

Homotrimer and homohexamer. Binds to beta-glucuronidase.3 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 – 284
Beta strandi31 – 344
Beta strandi36 – 383
Beta strandi47 – 548
Helixi61 – 633
Beta strandi75 – 795
Beta strandi86 – 883
Helixi91 – 10111
Beta strandi104 – 1063
Beta strandi112 – 1143
Beta strandi118 – 1236
Turni127 – 1304
Beta strandi133 – 1397
Turni143 – 1453
Helixi149 – 1513
Helixi155 – 1617
Beta strandi164 – 1685
Helixi173 – 1775
Helixi183 – 1853
Helixi189 – 20416
Helixi205 – 2084
Beta strandi210 – 22011
Helixi222 – 23211
Helixi234 – 2363
Turni237 – 2393
Beta strandi241 – 2477
Helixi253 – 2553
Helixi262 – 27110
Helixi279 – 28810
Helixi291 – 30111
Turni302 – 3043
Beta strandi308 – 3103
Helixi312 – 3143
Beta strandi325 – 3273
Helixi332 – 3354
Beta strandi339 – 3413
Beta strandi346 – 3516
Turni352 – 3554
Helixi358 – 3614
Turni363 – 3653
Beta strandi369 – 3713
Helixi375 – 38410
Helixi386 – 3894
Helixi393 – 3953
Helixi396 – 4049
Helixi410 – 42516
Helixi427 – 43913
Beta strandi444 – 4507
Beta strandi458 – 4603
Turni468 – 4714
Helixi472 – 4754
Helixi478 – 4803
Helixi487 – 50620
Beta strandi521 – 5233
Beta strandi525 – 5328
Beta strandi534 – 5374
Helixi541 – 55212

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP23141.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839.
InParanoidiP23141.
KOiK01044.
OMAiRESQPFL.
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. Align

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

MWLRAFILAT LSASAAWGHP SSPPVVDTVH GKVLGKFVSL EGFAQPVAIF    50
LGIPFAKPPL GPLRFTPPQP AEPWSFVKNA TSYPPMCTQD PKAGQLLSEL 100
FTNRKENIPL KLSEDCLYLN IYTPADLTKK NRLPVMVWIH GGGLMVGAAS 150
TYDGLALAAH ENVVVVTIQY RLGIWGFFST GDEHSRGNWG HLDQVAALRW 200
VQDNIASFGG NPGSVTIFGE SAGGESVSVL VLSPLAKNLF HRAISESGVA 250
LTSVLVKKGD VKPLAEQIAI TAGCKTTTSA VMVHCLRQKT EEELLETTLK 300
MKFLSLDLQG DPRESQPLLG TVIDGMLLLK TPEELQAERN FHTVPYMVGI 350
NKQEFGWLIP MQLMSYPLSE GQLDQKTAMS LLWKSYPLVC IAKELIPEAT 400
EKYLGGTDDT VKKKDLFLDL IADVMFGVPS VIVARNHRDA GAPTYMYEFQ 450
YRPSFSSDMK PKTVIGDHGD ELFSVFGAPF LKEGASEEEI RLSKMVMKFW 500
ANFARNGNPN GEGLPHWPEY NQKEGYLQIG ANTQAAQKLK DKEVAFWTNL 550
FAKKAVEKPP QTEHIEL 567
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.

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. VSP_021026
Alternative sequencei362 – 3621Missing in isoform 3. VSP_047158

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21W → L in AAD53175. 1 Publication
Sequence conflicti4 – 74RAFI → PALV in BAA04650. 1 Publication
Sequence conflicti4 – 74RAFI → PALV in BAC87749. 1 Publication
Sequence conflicti4 – 74RAFI → PALV in BAC87751. 1 Publication
Sequence conflicti4 – 74RAFI → PALV in BAF83312. 1 Publication
Sequence conflicti4 – 74RAFI → PALV in BAF84898. 1 Publication
Sequence conflicti4 – 74RAFI → PALV in AAH12418. 1 Publication
Sequence conflicti12 – 121S → A in BAA04650. 1 Publication
Sequence conflicti12 – 121S → A in BAC87749. 1 Publication
Sequence conflicti12 – 121S → A in BAC87751. 1 Publication
Sequence conflicti12 – 121S → A in BAF83312. 1 Publication
Sequence conflicti12 – 121S → A in BAF84898. 1 Publication
Sequence conflicti12 – 121S → A in AAH12418. 1 Publication
Sequence conflicti19 – 213HPS → GPP AA sequence 1 Publication
Sequence conflicti19 – 191H → N AA sequence 1 Publication
Sequence conflicti21 – 244SSPP → EAVV AA sequence 1 Publication
Sequence conflicti27 – 282DT → AK AA sequence 1 Publication
Sequence conflicti28 – 292TV → DT AA sequence 1 Publication
Sequence conflicti56 – 561A → G in AAA16036. 1 Publication
Sequence conflicti56 – 561A → G in AAA35711. 1 Publication
Sequence conflicti64 – 641R → G in CAA37147. 1 Publication
Sequence conflicti65 – 651F → S in AAP20868. 1 Publication
Sequence conflicti75 – 751S → A AA sequence 1 Publication
Sequence conflicti78 – 781K → I AA sequence 1 Publication
Sequence conflicti89 – 891Q → R in AAP20868. 1 Publication
Sequence conflicti98 – 981S → F AA sequence 1 Publication
Sequence conflicti105 – 1073KEN → PAD AA sequence 1 Publication
Sequence conflicti115 – 1151D → H in AAA83932. 1 Publication
Sequence conflicti186 – 1861R → G in CAA37147. 1 Publication
Sequence conflicti247 – 2471S → I AA sequence 1 Publication
Sequence conflicti251 – 2511L → K AA sequence 1 Publication
Sequence conflicti253 – 2531S → G AA sequence 1 Publication
Sequence conflicti255 – 2551L → P in BAF83312. 1 Publication
Sequence conflicti258 – 2581K → Q AA sequence 1 Publication
Sequence conflicti281 – 2811V → A in AAA83932. 1 Publication
Sequence conflicti298 – 2981T → I AA sequence 1 Publication
Sequence conflicti302 – 3021K → A AA sequence 1 Publication
Sequence conflicti305 – 3051S → M AA sequence 1 Publication
Sequence conflicti337 – 3371A → R in AAA83932. 1 Publication
Sequence conflicti417 – 4171F → I in AAA83932. 1 Publication
Sequence conflicti512 – 5121E → K in AAA83932. 1 Publication
Sequence conflicti536 – 5361A → G in AAA16036. 1 Publication
Sequence conflicti536 – 5361A → G in AAA35711. 1 Publication
Sequence conflicti563 – 5631E → D in AAA83932. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi119576.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS32450.1. [P23141-2 ]
CCDS45488.1. [P23141-1 ]
CCDS45489.1. [P23141-3 ]
PIRi A41010.
RefSeqi NP_001020365.1. NM_001025194.1. [P23141-1 ]
NP_001020366.1. NM_001025195.1. [P23141-2 ]
NP_001257.4. NM_001266.4. [P23141-3 ]
UniGenei Hs.558865.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MX1 X-ray 2.40 A/B/C/D/E/F 19-567 [» ]
1MX5 X-ray 2.80 A/B/C/D/E/F 19-567 [» ]
1MX9 X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L 19-567 [» ]
1YA4 X-ray 3.20 A/B/C 21-552 [» ]
1YA8 X-ray 3.00 A/B/C 21-552 [» ]
1YAH X-ray 3.00 A/B/C 21-552 [» ]
1YAJ X-ray 3.20 A/B/C/D/E/F/G/H/I/J/K/L 21-552 [» ]
2DQY X-ray 3.00 A/B/C 19-561 [» ]
2DQZ X-ray 2.80 A/B/C 19-561 [» ]
2DR0 X-ray 3.20 A/B/C 19-561 [» ]
2H7C X-ray 2.00 A/B/C/D/E/F 19-561 [» ]
2HRQ X-ray 2.70 A/B/C/D/E/F 21-553 [» ]
2HRR X-ray 2.70 A/B/C 21-553 [» ]
3K9B X-ray 3.10 A/B/C 24-553 [» ]
4AB1 X-ray 2.20 A 21-553 [» ]
ProteinModelPortali P23141.
SMRi P23141. Positions 21-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107494. 2 interactions.
IntActi P23141. 1 interaction.
MINTi MINT-5004142.

Chemistry

BindingDBi P23141.
ChEMBLi CHEMBL2265.
DrugBanki DB00357. Aminoglutethimide.
DB01393. Bezafibrate.
DB01432. Cholestyramine.
DB00691. Moexipril.
GuidetoPHARMACOLOGYi 2592.

Protein family/group databases

MEROPSi S09.982.

PTM databases

PhosphoSitei P23141.

Polymorphism databases

DMDMi 119576.

Proteomic databases

MaxQBi P23141.
PRIDEi P23141.

Protocols and materials databases

DNASUi 1066.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360526 ; ENSP00000353720 ; ENSG00000198848 . [P23141-2 ]
ENST00000361503 ; ENSP00000355193 ; ENSG00000198848 . [P23141-1 ]
ENST00000422046 ; ENSP00000390492 ; ENSG00000198848 . [P23141-3 ]
ENST00000571922 ; ENSP00000460045 ; ENSG00000262243 .
ENST00000574513 ; ENSP00000461208 ; ENSG00000262243 .
ENST00000576783 ; ENSP00000458586 ; ENSG00000262243 .
GeneIDi 1066.
KEGGi hsa:1066.
UCSCi uc002eil.3. human. [P23141-2 ]
uc002eim.3. human. [P23141-1 ]

Organism-specific databases

CTDi 1066.
GeneCardsi GC16M055836.
HGNCi HGNC:1863. CES1.
HPAi HPA012023.
HPA046717.
MIMi 114835. gene+phenotype.
neXtProti NX_P23141.
PharmGKBi PA107.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG008839.
InParanoidi P23141.
KOi K01044.
OMAi RESQPFL.
OrthoDBi EOG75XGKD.
PhylomeDBi P23141.
TreeFami TF315470.

Enzyme and pathway databases

BioCyci MetaCyc:HS11616-MONOMER.
BRENDAi 3.1.1.1. 2681.
SABIO-RK P23141.

Miscellaneous databases

EvolutionaryTracei P23141.
GeneWikii Carboxylesterase_1.
GenomeRNAii 1066.
NextBioi 4450.
PROi P23141.
SOURCEi Search...

Gene expression databases

Bgeei P23141.
CleanExi HS_CES1.
HS_CES2.
Genevestigatori P23141.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  23. "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: July 9, 2014
This is version 155 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

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