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P23141 (EST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Liver carboxylesterase 1
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase
Short name=ACAT
Brain carboxylesterase hBr1
Carboxylesterase 1
Short name=CE-1
Short name=hCE-1
EC=3.1.1.1
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 names
Name:CES1
Synonyms:CES2, SES1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.20

Catalytic activity

A carboxylic ester + H2O = an alcohol + a carboxylate. Ref.13 Ref.14 Ref.20

4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate. Ref.13 Ref.14 Ref.20

Enzyme regulation

Activated by CHAPS. Ref.14

Subunit structure

Homotrimer and homohexamer. Binds to beta-glucuronidase. Ref.5 Ref.13 Ref.15

Subcellular location

Endoplasmic reticulum lumen Ref.5.

Tissue specificity

Expressed predominantly in liver with lower levels in heart and lung. Ref.5

Post-translational modification

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.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Biophysicochemical properties

Kinetic parameters:

KM=106.6 µM for p-nitrophenyl acetate Ref.13 Ref.14 Ref.20 Ref.21

KM=775.7 µM for L-methylphenidate

KM=663.5 µM for D-methylphenidate

KM=116 µM for cocaine

KM=43 mM for ethanol

KM=0.8 mM for 4-methylumbelliferyl acetate

KM=6.3 mM for heroin

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 dependence:

Optimum pH is 6.5.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23141-1)

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.
Isoform 2 (identifier: P23141-2)

The sequence of this isoform differs from the canonical sequence as follows:
     17-17: W → WA
Isoform 3 (identifier: P23141-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.13 Ref.14
Chain18 – 567550Liver carboxylesterase 1
PRO_0000391359

Sites

Active site2211Acyl-ester intermediate Ref.16
Active site3541Charge relay system Ref.16
Active site4681Charge relay system Ref.16

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Ref.16
Disulfide bond87 ↔ 116
Disulfide bond274 ↔ 285

Natural variations

Alternative sequence171W → WA in isoform 2.
VSP_021026
Alternative sequence3621Missing in isoform 3.
VSP_047158
Natural variant181G → GA.
VAR_002357
Natural variant751S → N.
Corresponds to variant rs2307240 [ dbSNP | Ensembl ].
VAR_014314
Natural variant1431G → 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. Ref.21
Corresponds to variant rs71647871 [ dbSNP | Ensembl ].
VAR_046954
Natural variant1991R → H.
Corresponds to variant rs2307243 [ dbSNP | Ensembl ].
VAR_014594
Natural variant2031D → E.
Corresponds to variant rs2307227 [ dbSNP | Ensembl ].
VAR_014595

Experimental info

Mutagenesis791N → A: Abolishes glycosylation. Ref.16
Mutagenesis2211S → A: Loss of activity. Ref.16
Mutagenesis3541E → A: Loss of activity. Ref.16
Mutagenesis4681H → A: Loss of activity. Ref.16
Mutagenesis564 – 5674Missing: Does not result in secretion. Ref.16
Sequence conflict21W → L in AAD53175. Ref.5
Sequence conflict4 – 74RAFI → PALV in BAA04650. Ref.3
Sequence conflict4 – 74RAFI → PALV in BAC87749. Ref.8
Sequence conflict4 – 74RAFI → PALV in BAC87751. Ref.8
Sequence conflict4 – 74RAFI → PALV in BAF83312. Ref.9
Sequence conflict4 – 74RAFI → PALV in BAF84898. Ref.9
Sequence conflict4 – 74RAFI → PALV in AAH12418. Ref.11
Sequence conflict121S → A in BAA04650. Ref.3
Sequence conflict121S → A in BAC87749. Ref.8
Sequence conflict121S → A in BAC87751. Ref.8
Sequence conflict121S → A in BAF83312. Ref.9
Sequence conflict121S → A in BAF84898. Ref.9
Sequence conflict121S → A in AAH12418. Ref.11
Sequence conflict19 – 213HPS → GPP AA sequence Ref.15
Sequence conflict191H → N AA sequence Ref.14
Sequence conflict21 – 244SSPP → EAVV AA sequence Ref.14
Sequence conflict27 – 282DT → AK AA sequence Ref.14
Sequence conflict28 – 292TV → DT AA sequence Ref.15
Sequence conflict561A → G in AAA16036. Ref.2
Sequence conflict561A → G in AAA35711. Ref.2
Sequence conflict641R → G in CAA37147. Ref.18
Sequence conflict651F → S in AAP20868. Ref.6
Sequence conflict751S → A AA sequence Ref.14
Sequence conflict781K → I AA sequence Ref.14
Sequence conflict891Q → R in AAP20868. Ref.6
Sequence conflict981S → F AA sequence Ref.14
Sequence conflict105 – 1073KEN → PAD AA sequence Ref.14
Sequence conflict1151D → H in AAA83932. Ref.19
Sequence conflict1861R → G in CAA37147. Ref.18
Sequence conflict2471S → I AA sequence Ref.14
Sequence conflict2511L → K AA sequence Ref.14
Sequence conflict2531S → G AA sequence Ref.14
Sequence conflict2551L → P in BAF83312. Ref.9
Sequence conflict2581K → Q AA sequence Ref.14
Sequence conflict2811V → A in AAA83932. Ref.19
Sequence conflict2981T → I AA sequence Ref.14
Sequence conflict3021K → A AA sequence Ref.14
Sequence conflict3051S → M AA sequence Ref.14
Sequence conflict3371A → R in AAA83932. Ref.19
Sequence conflict4171F → I in AAA83932. Ref.19
Sequence conflict5121E → K in AAA83932. Ref.19
Sequence conflict5361A → G in AAA16036. Ref.2
Sequence conflict5361A → G in AAA35711. Ref.2
Sequence conflict5631E → D in AAA83932. Ref.19

Secondary structure

............................................................................................................. 567
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: D3A00BDCDC7E5DFF

FASTA56762,521
        10         20         30         40         50         60 
MWLRAFILAT LSASAAWGHP SSPPVVDTVH GKVLGKFVSL EGFAQPVAIF LGIPFAKPPL 

        70         80         90        100        110        120 
GPLRFTPPQP AEPWSFVKNA TSYPPMCTQD PKAGQLLSEL FTNRKENIPL KLSEDCLYLN 

       130        140        150        160        170        180 
IYTPADLTKK NRLPVMVWIH GGGLMVGAAS TYDGLALAAH ENVVVVTIQY RLGIWGFFST 

       190        200        210        220        230        240 
GDEHSRGNWG HLDQVAALRW VQDNIASFGG NPGSVTIFGE SAGGESVSVL VLSPLAKNLF 

       250        260        270        280        290        300 
HRAISESGVA LTSVLVKKGD VKPLAEQIAI TAGCKTTTSA VMVHCLRQKT EEELLETTLK 

       310        320        330        340        350        360 
MKFLSLDLQG DPRESQPLLG TVIDGMLLLK TPEELQAERN FHTVPYMVGI NKQEFGWLIP 

       370        380        390        400        410        420 
MQLMSYPLSE GQLDQKTAMS LLWKSYPLVC IAKELIPEAT EKYLGGTDDT VKKKDLFLDL 

       430        440        450        460        470        480 
IADVMFGVPS VIVARNHRDA GAPTYMYEFQ YRPSFSSDMK PKTVIGDHGD ELFSVFGAPF 

       490        500        510        520        530        540 
LKEGASEEEI RLSKMVMKFW ANFARNGNPN GEGLPHWPEY NQKEGYLQIG ANTQAAQKLK 

       550        560 
DKEVAFWTNL FAKKAVEKPP QTEHIEL 

« Hide

Isoform 2 [UniParc].

Checksum: AEC3C3DB33D1DDAC
Show »

FASTA56862,592
Isoform 3 [UniParc].

Checksum: AE8F6F2B7004416D
Show »

FASTA56662,393

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32450.1. [P23141-2]
CCDS45488.1. [P23141-1]
CCDS45489.1. [P23141-3]
PIRA41010.
RefSeqNP_001020365.1. NM_001025194.1. [P23141-1]
NP_001020366.1. NM_001025195.1. [P23141-2]
NP_001257.4. NM_001266.4. [P23141-3]
UniGeneHs.558865.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP23141.
SMRP23141. Positions 21-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107494. 2 interactions.
IntActP23141. 1 interaction.
MINTMINT-5004142.

Chemistry

BindingDBP23141.
ChEMBLCHEMBL2265.
DrugBankDB00357. Aminoglutethimide.
DB01393. Bezafibrate.
DB01432. Cholestyramine.
DB00691. Moexipril.
GuidetoPHARMACOLOGY2592.

Protein family/group databases

MEROPSS09.982.

PTM databases

PhosphoSiteP23141.

Polymorphism databases

DMDM119576.

Proteomic databases

MaxQBP23141.
PRIDEP23141.

Protocols and materials databases

DNASU1066.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360526; ENSP00000353720; ENSG00000198848. [P23141-2]
ENST00000361503; ENSP00000355193; ENSG00000198848. [P23141-1]
ENST00000422046; ENSP00000390492; ENSG00000198848. [P23141-3]
ENST00000571922; ENSP00000460045; ENSG00000262243.
ENST00000574513; ENSP00000461208; ENSG00000262243.
ENST00000576783; ENSP00000458586; ENSG00000262243.
GeneID1066.
KEGGhsa:1066.
UCSCuc002eil.3. human. [P23141-2]
uc002eim.3. human. [P23141-1]

Organism-specific databases

CTD1066.
GeneCardsGC16M055836.
HGNCHGNC:1863. CES1.
HPAHPA012023.
HPA046717.
MIM114835. gene+phenotype.
neXtProtNX_P23141.
PharmGKBPA107.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG008839.
InParanoidP23141.
KOK01044.
OMARESQPFL.
OrthoDBEOG75XGKD.
PhylomeDBP23141.
TreeFamTF315470.

Enzyme and pathway databases

BioCycMetaCyc:HS11616-MONOMER.
BRENDA3.1.1.1. 2681.
SABIO-RKP23141.

Gene expression databases

BgeeP23141.
CleanExHS_CES1.
HS_CES2.
GenevestigatorP23141.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23141.
GeneWikiCarboxylesterase_1.
GenomeRNAi1066.
NextBio4450.
PROP23141.
SOURCESearch...

Entry information

Entry nameEST1_HUMAN
AccessionPrimary (citable) accession number: P23141
Secondary accession number(s): A6NIM1 expand/collapse secondary AC list , A8K3K8, A8K844, E9PAU8, P82127, Q00015, Q13657, Q14062, Q16737, Q16788, Q549X7, Q549X8, Q86UK2, Q96EE8, Q9UC52, Q9UDG8, Q9UK77, Q9ULY2
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM