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Cytochrome P450 2E1 (EC 1.14.13.-) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-J) [Cleaved into: Cytochrome P450 2E1, N-terminally processed]

 CP2E1_HUMAN             Reviewed;         493 AA.
P05181; Q5VZD5; Q6NWT9; Q9UK47;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
30-AUG-2017, entry version 188.
RecName: Full=Cytochrome P450 2E1;
EC=1.14.13.-;
AltName: Full=4-nitrophenol 2-hydroxylase;
EC=1.14.13.n7;
AltName: Full=CYPIIE1;
AltName: Full=Cytochrome P450-J;
Name=CYP2E1; Synonyms=CYP2E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3782137;
Song B.-J., Gelboin H.V., Park S.-S., Yang C.S., Gonzalez F.J.;
"Complementary DNA and protein sequences of ethanol-inducible rat and
human cytochrome P-450s. Transcriptional and post-transcriptional
regulation of the rat enzyme.";
J. Biol. Chem. 261:16689-16697(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3233219; DOI=10.1021/bi00425a019;
Umeno M., McBride O.W., Yang C.S., Gelboin H.V., Gonzalez F.J.;
"Human ethanol-inducible P450IIE1: complete gene sequence, promoter
characterization, chromosome mapping, and cDNA-directed expression.";
Biochemistry 27:9006-9013(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Zhuge J., Qian Y., Xie H., Yu Y.;
"Sequence of a new human cytochrome P450-2E1 cDNA and establishing the
transgenic cell line.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-219; CYS-366 AND
LEU-457.
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-493.
TISSUE=Brain;
Yoo M., Shin S.W.;
"Partial sequence of human brain cytochrome P450 2E1.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 387-432.
Iwahashi K., Okuyama E., Nakamura K., Furukawa A., Ichikawa Y.;
"Rapid detection of a novel mutation in the human CYP2EI exon VIII by
the PCR method.";
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 1-20.
TISSUE=Liver;
PubMed=3675576; DOI=10.1016/0006-291X(87)91100-4;
Lasker J.M., Raucy J., Kubota S., Bloswick B.P., Black M.,
Lieber C.S.;
"Purification and characterization of human liver cytochrome P-450-
ALC.";
Biochem. Biophys. Res. Commun. 148:232-238(1987).
[11]
PROTEIN SEQUENCE OF 3-20.
PubMed=2587619; DOI=10.1159/000138590;
Robinson R.C., Shorr R.G., Varrichio A., Park S.S., Gelboin H.V.,
Miller H., Friedman F.K.;
"Human liver cytochrome P-450 related to a rat acetone-inducible,
nitrosamine-metabolizing cytochrome P-450: identification and
isolation.";
Pharmacology 39:137-144(1989).
[12]
PROTEIN SEQUENCE OF 23-42.
PubMed=8031147; DOI=10.1006/abbi.1994.1280;
Gillam E.M., Guo Z., Guengerich F.P.;
"Expression of modified human cytochrome P450 2E1 in Escherichia coli,
purification, and spectral and catalytic properties.";
Arch. Biochem. Biophys. 312:59-66(1994).
[13]
CATALYTIC ACTIVITY.
PubMed=9348445; DOI=10.1021/tx970048z;
Zerilli A., Ratanasavanh D., Lucas D., Goasduff T., Dreano Y.,
Menard C., Picart D., Berthou F.;
"Both cytochromes P450 2E1 and 3A are involved in the O-hydroxylation
of p-nitrophenol, a catalytic activity known to be specific for P450
2E1.";
Chem. Res. Toxicol. 10:1205-1212(1997).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 32-493 IN COMPLEX WITH THE
INHIBITORS INDAZOLE AND 4-METHYLPYRAZOLE AND HEME.
PubMed=18818195; DOI=10.1074/jbc.M805999200;
Porubsky P.R., Meneely K.M., Scott E.E.;
"Structures of human cytochrome P-450 2E1. Insights into the binding
of inhibitors and both small molecular weight and fatty acid
substrates.";
J. Biol. Chem. 283:33698-33707(2008).
[16]
VARIANTS CYP2E1*2 HIS-76 AND CYP2E1*3 ILE-389.
PubMed=9058590;
Hu Y., Oscarson M., Johansson I., Yue Q.Y., Dahl M.L., Tabone M.,
Arinco S., Albano E., Ingelman-Sundberg M.;
"Genetic polymorphism of human CYP2E1: characterization of two variant
alleles.";
Mol. Pharmacol. 51:370-376(1997).
[17]
VARIANT CYP2E1*4 ILE-179.
PubMed=9918138;
Fairbrother K.S., Grove J., de Waziers I., Steimel D.T., Day C.P.,
Crespi C.L., Daly A.K.;
"Detection and characterization of novel polymorphisms in the CYP2E1
gene.";
Pharmacogenetics 8:543-552(1998).
[18]
VARIANTS ILE-179 AND LEU-457.
PubMed=15469410; DOI=10.1517/14622416.5.7.895;
Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q.,
McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.;
"Genetic variation in eleven phase I drug metabolism genes in an
ethnically diverse population.";
Pharmacogenomics 5:895-931(2004).
-!- FUNCTION: Metabolizes several precarcinogens, drugs, and solvents
to reactive metabolites. Inactivates a number of drugs and
xenobiotics and also bioactivates many xenobiotic substrates to
their hepatotoxic or carcinogenic forms.
-!- CATALYTIC ACTIVITY: 4-nitrophenol + NADPH + O(2) = 4-nitrocatechol
+ NADP(+) + H(2)O. {ECO:0000269|PubMed:9348445}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- INDUCTION: By ethanol and isoniazid.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
Note=CYP2E1 alleles;
URL="http://www.cypalleles.ki.se/cyp2e1.htm";
-!- WEB RESOURCE: Name=Wikipedia; Note=CYP2E1 entry;
URL="https://en.wikipedia.org/wiki/CYP2E1";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyp2e1/";
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EMBL; J02625; AAA35743.1; -; mRNA.
EMBL; J02843; AAA52155.1; -; Genomic_DNA.
EMBL; AF182276; AAF13601.1; -; mRNA.
EMBL; DQ515958; ABF47105.1; -; Genomic_DNA.
EMBL; AL161645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471211; EAW61357.1; -; Genomic_DNA.
EMBL; BC067433; AAH67433.1; -; mRNA.
EMBL; AF084225; AAD13753.1; -; mRNA.
EMBL; D50111; BAA08796.1; -; Genomic_DNA.
CCDS; CCDS7686.1; -.
PIR; A31949; A31949.
RefSeq; NP_000764.1; NM_000773.3.
UniGene; Hs.12907; -.
PDB; 3E4E; X-ray; 2.60 A; A/B=32-493.
PDB; 3E6I; X-ray; 2.20 A; A/B=32-493.
PDB; 3GPH; X-ray; 2.70 A; A/B=32-493.
PDB; 3KOH; X-ray; 2.90 A; A/B=32-493.
PDB; 3LC4; X-ray; 3.10 A; A/B=32-493.
PDB; 3T3Z; X-ray; 2.35 A; A/B/C/D=32-493.
PDBsum; 3E4E; -.
PDBsum; 3E6I; -.
PDBsum; 3GPH; -.
PDBsum; 3KOH; -.
PDBsum; 3LC4; -.
PDBsum; 3T3Z; -.
ProteinModelPortal; P05181; -.
SMR; P05181; -.
BioGrid; 107944; 18.
IntAct; P05181; 10.
STRING; 9606.ENSP00000252945; -.
BindingDB; P05181; -.
ChEMBL; CHEMBL5281; -.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB00041; Aldesleukin.
DrugBank; DB00918; Almotriptan.
DrugBank; DB00969; Alosetron.
DrugBank; DB01223; Aminophylline.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB06728; Aniline.
DrugBank; DB01435; Antipyrine.
DrugBank; DB00972; Azelastine.
DrugBank; DB06770; Benzyl alcohol.
DrugBank; DB04794; Bifonazole.
DrugBank; DB01558; Bromazepam.
DrugBank; DB00835; Brompheniramine.
DrugBank; DB01156; Bupropion.
DrugBank; DB00201; Caffeine.
DrugBank; DB06774; Capsaicin.
DrugBank; DB00748; Carbinoxamine.
DrugBank; DB01136; Carvedilol.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB00356; Chlorzoxazone.
DrugBank; DB00501; Cimetidine.
DrugBank; DB00215; Citalopram.
DrugBank; DB04920; Clevidipine.
DrugBank; DB00636; Clofibrate.
DrugBank; DB00882; Clomifene.
DrugBank; DB01068; Clonazepam.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB00363; Clozapine.
DrugBank; DB01394; Colchicine.
DrugBank; DB00851; Dacarbazine.
DrugBank; DB06637; Dalfampridine.
DrugBank; DB00250; Dapsone.
DrugBank; DB01151; Desipramine.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB01191; Dexfenfluramine.
DrugBank; DB00633; Dexmedetomidine.
DrugBank; DB00514; Dextromethorphan.
DrugBank; DB00829; Diazepam.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB00822; Disulfiram.
DrugBank; DB01127; Econazole.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB00228; Enflurane.
DrugBank; DB00109; Enfuvirtide.
DrugBank; DB00655; Estrone.
DrugBank; DB00898; Ethanol.
DrugBank; DB06689; Ethanolamine Oleate.
DrugBank; DB00593; Ethosuximide.
DrugBank; DB00773; Etoposide.
DrugBank; DB01628; Etoricoxib.
DrugBank; DB00949; Felbamate.
DrugBank; DB08868; Fingolimod.
DrugBank; DB01544; Flunitrazepam.
DrugBank; DB00623; Fluphenazine.
DrugBank; DB00690; Flurazepam.
DrugBank; DB00176; Fluvoxamine.
DrugBank; DB00158; Folic Acid.
DrugBank; DB01213; Fomepizole.
DrugBank; DB01296; Glucosamine.
DrugBank; DB04077; Glycerol.
DrugBank; DB05708; GTS-21.
DrugBank; DB01159; Halothane.
DrugBank; DB01355; Hexobarbital.
DrugBank; DB04946; Iloperidone.
DrugBank; DB00458; Imipramine.
DrugBank; DB00753; Isoflurane.
DrugBank; DB00951; Isoniazid.
DrugBank; DB00883; Isosorbide Dinitrate.
DrugBank; DB01167; Itraconazole.
DrugBank; DB00170; Menadione.
DrugBank; DB00371; Meprobamate.
DrugBank; DB00703; Methazolamide.
DrugBank; DB00763; Methimazole.
DrugBank; DB01403; Methotrimeprazine.
DrugBank; DB01028; Methoxyflurane.
DrugBank; DB01011; Metyrapone.
DrugBank; DB00379; Mexiletine.
DrugBank; DB01110; Miconazole.
DrugBank; DB00683; Midazolam.
DrugBank; DB01204; Mitoxantrone.
DrugBank; DB00622; Nicardipine.
DrugBank; DB02701; Nicotinamide.
DrugBank; DB00184; Nicotine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB06712; Nilvadipine.
DrugBank; DB01595; Nitrazepam.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00904; Ondansetron.
DrugBank; DB01173; Orphenadrine.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB00617; Paramethadione.
DrugBank; DB03783; Phenacetin.
DrugBank; DB00780; Phenelzine.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01085; Pilocarpine.
DrugBank; DB01100; Pimozide.
DrugBank; DB04977; Plitidepsin.
DrugBank; DB01131; Proguanil.
DrugBank; DB00818; Propofol.
DrugBank; DB00908; Quinidine.
DrugBank; DB00468; Quinine.
DrugBank; DB01045; Rifampicin.
DrugBank; DB00503; Ritonavir.
DrugBank; DB06201; Rufinamide.
DrugBank; DB00118; S-Adenosylmethionine.
DrugBank; DB01037; Selegiline.
DrugBank; DB01236; Sevoflurane.
DrugBank; DB00203; Sildenafil.
DrugBank; DB00428; Streptozocin.
DrugBank; DB00359; Sulfadiazine.
DrugBank; DB00259; Sulfanilamide.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB01079; Tegaserod.
DrugBank; DB01041; Thalidomide.
DrugBank; DB01412; Theobromine.
DrugBank; DB00277; Theophylline.
DrugBank; DB00599; Thiopental.
DrugBank; DB00679; Thioridazine.
DrugBank; DB00208; Ticlopidine.
DrugBank; DB01007; Tioconazole.
DrugBank; DB04858; Tirapazamine.
DrugBank; DB05109; Trabectedin.
DrugBank; DB00752; Tranylcypromine.
DrugBank; DB00347; Trimethadione.
DrugBank; DB01586; Ursodeoxycholic acid.
DrugBank; DB00549; Zafirlukast.
DrugBank; DB01198; Zopiclone.
GuidetoPHARMACOLOGY; 1330; -.
SwissLipids; SLP:000001596; -.
iPTMnet; P05181; -.
PhosphoSitePlus; P05181; -.
BioMuta; CYP2E1; -.
DMDM; 117250; -.
PaxDb; P05181; -.
PeptideAtlas; P05181; -.
PRIDE; P05181; -.
Ensembl; ENST00000252945; ENSP00000252945; ENSG00000130649.
Ensembl; ENST00000463117; ENSP00000440689; ENSG00000130649.
GeneID; 1571; -.
KEGG; hsa:1571; -.
UCSC; uc001lnj.1; human.
CTD; 1571; -.
DisGeNET; 1571; -.
GeneCards; CYP2E1; -.
HGNC; HGNC:2631; CYP2E1.
HPA; HPA009128; -.
HPA; HPA029564; -.
MIM; 124040; gene.
neXtProt; NX_P05181; -.
OpenTargets; ENSG00000130649; -.
PharmGKB; PA129; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00880000137861; -.
HOGENOM; HOG000036992; -.
HOVERGEN; HBG015789; -.
InParanoid; P05181; -.
KO; K07415; -.
OMA; HEATQDT; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; P05181; -.
TreeFam; TF352043; -.
BioCyc; MetaCyc:HS05414-MONOMER; -.
Reactome; R-HSA-211981; Xenobiotics.
Reactome; R-HSA-211999; CYP2E1 reactions.
SABIO-RK; P05181; -.
SIGNOR; P05181; -.
EvolutionaryTrace; P05181; -.
GeneWiki; CYP2E1; -.
GenomeRNAi; 1571; -.
PRO; PR:P05181; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000130649; -.
CleanEx; HS_CYP2E1; -.
ExpressionAtlas; P05181; baseline and differential.
Genevisible; P05181; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:BHF-UCL.
GO; GO:0016491; F:oxidoreductase activity; IDA:BHF-UCL.
GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; TAS:UniProtKB.
GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:Ensembl.
GO; GO:0019825; F:oxygen binding; TAS:Reactome.
GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
GO; GO:0018910; P:benzene metabolic process; TAS:Reactome.
GO; GO:0018885; P:carbon tetrachloride metabolic process; TAS:Reactome.
GO; GO:0017144; P:drug metabolic process; IDA:BHF-UCL.
GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
GO; GO:0042197; P:halogenated hydrocarbon metabolic process; TAS:Reactome.
GO; GO:0046483; P:heterocycle metabolic process; IDA:BHF-UCL.
GO; GO:0016098; P:monoterpenoid metabolic process; IDA:BHF-UCL.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0010193; P:response to ozone; IEA:Ensembl.
GO; GO:0008202; P:steroid metabolic process; IMP:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008070; Cyt_P450_E_grp-I_CYP2E-like.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01687; EP450ICYP2E.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
Monooxygenase; NADP; Oxidoreductase; Polymorphism; Reference proteome.
CHAIN 1 493 Cytochrome P450 2E1.
/FTId=PRO_0000051751.
REGION 298 303 Substrate binding. {ECO:0000305}.
METAL 437 437 Iron (heme axial ligand).
VARIANT 76 76 R -> H (in allele CYP2E1*2; reduced
activity; dbSNP:rs72559710).
{ECO:0000269|PubMed:9058590}.
/FTId=VAR_008360.
VARIANT 179 179 V -> I (in allele CYP2E1*4;
dbSNP:rs6413419).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:9918138}.
/FTId=VAR_008361.
VARIANT 219 219 N -> D (in dbSNP:rs41299426).
{ECO:0000269|Ref.4}.
/FTId=VAR_055382.
VARIANT 366 366 S -> C (in dbSNP:rs41299434).
{ECO:0000269|Ref.4}.
/FTId=VAR_055383.
VARIANT 389 389 V -> I (in allele CYP2E1*3;
dbSNP:rs55897648).
{ECO:0000269|PubMed:9058590}.
/FTId=VAR_008362.
VARIANT 457 457 H -> L (in dbSNP:rs28969387).
{ECO:0000269|PubMed:15469410,
ECO:0000269|Ref.4}.
/FTId=VAR_024727.
CONFLICT 2 2 Missing (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 23 23 W -> A (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 32 32 L -> N (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 71 71 Y -> C (in Ref. 7; AAH67433).
{ECO:0000305}.
CONFLICT 235 235 V -> A (in Ref. 3; AAF13601).
{ECO:0000305}.
CONFLICT 355 355 H -> R (in Ref. 7; AAH67433).
{ECO:0000305}.
TURN 40 42 {ECO:0000244|PDB:3E6I}.
HELIX 45 47 {ECO:0000244|PDB:3E6I}.
HELIX 50 52 {ECO:0000244|PDB:3T3Z}.
HELIX 53 64 {ECO:0000244|PDB:3E6I}.
STRAND 66 72 {ECO:0000244|PDB:3E6I}.
STRAND 75 80 {ECO:0000244|PDB:3E6I}.
HELIX 83 91 {ECO:0000244|PDB:3E6I}.
TURN 94 97 {ECO:0000244|PDB:3E6I}.
HELIX 104 109 {ECO:0000244|PDB:3E6I}.
STRAND 112 114 {ECO:0000244|PDB:3E6I}.
HELIX 122 135 {ECO:0000244|PDB:3E6I}.
HELIX 142 159 {ECO:0000244|PDB:3E6I}.
TURN 160 163 {ECO:0000244|PDB:3E6I}.
HELIX 169 172 {ECO:0000244|PDB:3E6I}.
HELIX 174 185 {ECO:0000244|PDB:3E6I}.
HELIX 194 209 {ECO:0000244|PDB:3E6I}.
HELIX 213 220 {ECO:0000244|PDB:3E6I}.
HELIX 222 225 {ECO:0000244|PDB:3E6I}.
STRAND 228 230 {ECO:0000244|PDB:3T3Z}.
HELIX 231 255 {ECO:0000244|PDB:3E6I}.
STRAND 259 261 {ECO:0000244|PDB:3KOH}.
HELIX 265 274 {ECO:0000244|PDB:3E6I}.
STRAND 275 278 {ECO:0000244|PDB:3E6I}.
STRAND 279 281 {ECO:0000244|PDB:3T3Z}.
HELIX 286 317 {ECO:0000244|PDB:3E6I}.
HELIX 319 332 {ECO:0000244|PDB:3E6I}.
TURN 333 336 {ECO:0000244|PDB:3E6I}.
HELIX 341 346 {ECO:0000244|PDB:3E6I}.
HELIX 348 361 {ECO:0000244|PDB:3E6I}.
STRAND 376 378 {ECO:0000244|PDB:3E6I}.
STRAND 381 383 {ECO:0000244|PDB:3E6I}.
STRAND 388 391 {ECO:0000244|PDB:3E6I}.
HELIX 394 397 {ECO:0000244|PDB:3E6I}.
TURN 400 402 {ECO:0000244|PDB:3E6I}.
STRAND 403 405 {ECO:0000244|PDB:3E6I}.
HELIX 411 414 {ECO:0000244|PDB:3E6I}.
STRAND 419 421 {ECO:0000244|PDB:3E6I}.
HELIX 433 435 {ECO:0000244|PDB:3LC4}.
HELIX 440 457 {ECO:0000244|PDB:3E6I}.
STRAND 458 464 {ECO:0000244|PDB:3E6I}.
TURN 466 468 {ECO:0000244|PDB:3E6I}.
STRAND 474 481 {ECO:0000244|PDB:3E6I}.
STRAND 487 491 {ECO:0000244|PDB:3E6I}.
SEQUENCE 493 AA; 56849 MW; ED0399E32A005644 CRC64;
MSALGVTVAL LVWAAFLLLV SMWRQVHSSW NLPPGPFPLP IIGNLFQLEL KNIPKSFTRL
AQRFGPVFTL YVGSQRMVVM HGYKAVKEAL LDYKDEFSGR GDLPAFHAHR DRGIIFNNGP
TWKDIRRFSL TTLRNYGMGK QGNESRIQRE AHFLLEALRK TQGQPFDPTF LIGCAPCNVI
ADILFRKHFD YNDEKFLRLM YLFNENFHLL STPWLQLYNN FPSFLHYLPG SHRKVIKNVA
EVKEYVSERV KEHHQSLDPN CPRDLTDCLL VEMEKEKHSA ERLYTMDGIT VTVADLFFAG
TETTSTTLRY GLLILMKYPE IEEKLHEEID RVIGPSRIPA IKDRQEMPYM DAVVHEIQRF
ITLVPSNLPH EATRDTIFRG YLIPKGTVVV PTLDSVLYDN QEFPDPEKFK PEHFLNENGK
FKYSDYFKPF STGKRVCAGE GLARMELFLL LCAILQHFNL KPLVDPKDID LSPIHIGFGC
IPPRYKLCVI PRS


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