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P23141

- EST1_HUMAN

UniProt

P23141 - EST1_HUMAN

Protein

Liver carboxylesterase 1

Gene

CES1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    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 intermediate1 PublicationPROSITE-ProRule annotation
    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

    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

    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.

    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.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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    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. 1 PublicationCurated
    Sequence conflicti4 – 74RAFI → PALV in BAC87751. 1 PublicationCurated
    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. 1 PublicationCurated
    Sequence conflicti12 – 121S → A in BAC87751. 1 PublicationCurated
    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:
    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

    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: October 1, 2014
    This is version 156 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