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P05181

- CP2E1_HUMAN

UniProt

P05181 - CP2E1_HUMAN

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Protein

Cytochrome P450 2E1

Gene

CYP2E1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

4-nitrophenol + NADPH + O2 = 4-nitrocatechol + NADP+ + H2O.1 Publication

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi437 – 4371Iron (heme axial ligand)

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: InterPro
  4. monooxygenase activity Source: BHF-UCL
  5. oxidoreductase activity Source: BHF-UCL
  6. 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 Source: UniProtKB
  7. 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 Source: Ensembl
  8. oxygen binding Source: ProtInc

GO - Biological processi

  1. drug metabolic process Source: BHF-UCL
  2. heterocycle metabolic process Source: BHF-UCL
  3. monoterpenoid metabolic process Source: BHF-UCL
  4. oxidation-reduction process Source: BHF-UCL
  5. response to drug Source: Ensembl
  6. response to ethanol Source: Ensembl
  7. response to organonitrogen compound Source: Ensembl
  8. response to ozone Source: Ensembl
  9. small molecule metabolic process Source: Reactome
  10. steroid metabolic process Source: BHF-UCL
  11. triglyceride metabolic process Source: Ensembl
  12. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS05414-MONOMER.
ReactomeiREACT_13543. Xenobiotics.
REACT_13797. CYP2E1 reactions.
SABIO-RKP05181.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 2E1 (EC:1.14.13.-)
Alternative name(s):
4-nitrophenol 2-hydroxylase (EC:1.14.13.n7)
CYPIIE1
Cytochrome P450-J
Cleaved into the following chain:
Gene namesi
Name:CYP2E1
Synonyms:CYP2E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:2631. CYP2E1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. Golgi membrane Source: Ensembl
  3. intrinsic component of endoplasmic reticulum membrane Source: Ensembl
  4. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Cytochrome P450 2E1PRO_0000051751Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 493492Cytochrome P450 2E1, N-terminally processedPRO_0000421771Add
BLAST

Proteomic databases

PaxDbiP05181.
PeptideAtlasiP05181.
PRIDEiP05181.

PTM databases

PhosphoSiteiP05181.

Expressioni

Inductioni

By ethanol and isoniazid.

Gene expression databases

BgeeiP05181.
CleanExiHS_CYP2E1.
ExpressionAtlasiP05181. baseline and differential.
GenevestigatoriP05181.

Organism-specific databases

HPAiHPA009128.
HPA029564.

Interactioni

Protein-protein interaction databases

BioGridi107944. 17 interactions.
IntActiP05181. 10 interactions.
STRINGi9606.ENSP00000252945.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni40 – 423Combined sources
Helixi45 – 473Combined sources
Helixi50 – 523Combined sources
Helixi53 – 6412Combined sources
Beta strandi66 – 727Combined sources
Beta strandi75 – 806Combined sources
Helixi83 – 919Combined sources
Turni94 – 974Combined sources
Helixi104 – 1096Combined sources
Beta strandi112 – 1143Combined sources
Helixi122 – 13514Combined sources
Helixi142 – 15918Combined sources
Turni160 – 1634Combined sources
Helixi169 – 1724Combined sources
Helixi174 – 18512Combined sources
Helixi194 – 20916Combined sources
Helixi213 – 2208Combined sources
Helixi222 – 2254Combined sources
Beta strandi228 – 2303Combined sources
Helixi231 – 25525Combined sources
Beta strandi259 – 2613Combined sources
Helixi265 – 27410Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi279 – 2813Combined sources
Helixi286 – 31732Combined sources
Helixi319 – 33214Combined sources
Turni333 – 3364Combined sources
Helixi341 – 3466Combined sources
Helixi348 – 36114Combined sources
Beta strandi376 – 3783Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi388 – 3914Combined sources
Helixi394 – 3974Combined sources
Turni400 – 4023Combined sources
Beta strandi403 – 4053Combined sources
Helixi411 – 4144Combined sources
Beta strandi419 – 4213Combined sources
Helixi433 – 4353Combined sources
Helixi440 – 45718Combined sources
Beta strandi458 – 4647Combined sources
Turni466 – 4683Combined sources
Beta strandi474 – 4818Combined sources
Beta strandi487 – 4915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E4EX-ray2.60A/B32-493[»]
3E6IX-ray2.20A/B32-493[»]
3GPHX-ray2.70A/B32-493[»]
3KOHX-ray2.90A/B32-493[»]
3LC4X-ray3.10A/B32-493[»]
3T3ZX-ray2.35A/B/C/D32-493[»]
ProteinModelPortaliP05181.
SMRiP05181. Positions 32-493.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05181.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3036Substrate bindingCurated

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118775.
HOGENOMiHOG000036992.
HOVERGENiHBG015789.
InParanoidiP05181.
KOiK07415.
OMAiGCIPPRY.
OrthoDBiEOG7RBZ85.
PhylomeDBiP05181.
TreeFamiTF352043.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008070. Cyt_P450_E_grp-I_CYP2E-like.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR01687. EP450ICYP2E.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05181-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSALGVTVAL LVWAAFLLLV SMWRQVHSSW NLPPGPFPLP IIGNLFQLEL
60 70 80 90 100
KNIPKSFTRL AQRFGPVFTL YVGSQRMVVM HGYKAVKEAL LDYKDEFSGR
110 120 130 140 150
GDLPAFHAHR DRGIIFNNGP TWKDIRRFSL TTLRNYGMGK QGNESRIQRE
160 170 180 190 200
AHFLLEALRK TQGQPFDPTF LIGCAPCNVI ADILFRKHFD YNDEKFLRLM
210 220 230 240 250
YLFNENFHLL STPWLQLYNN FPSFLHYLPG SHRKVIKNVA EVKEYVSERV
260 270 280 290 300
KEHHQSLDPN CPRDLTDCLL VEMEKEKHSA ERLYTMDGIT VTVADLFFAG
310 320 330 340 350
TETTSTTLRY GLLILMKYPE IEEKLHEEID RVIGPSRIPA IKDRQEMPYM
360 370 380 390 400
DAVVHEIQRF ITLVPSNLPH EATRDTIFRG YLIPKGTVVV PTLDSVLYDN
410 420 430 440 450
QEFPDPEKFK PEHFLNENGK FKYSDYFKPF STGKRVCAGE GLARMELFLL
460 470 480 490
LCAILQHFNL KPLVDPKDID LSPIHIGFGC IPPRYKLCVI PRS
Length:493
Mass (Da):56,849
Last modified:April 1, 1988 - v1
Checksum:iED0399E32A005644
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21Missing AA sequence (PubMed:3675576)Curated
Sequence conflicti23 – 231W → A AA sequence (PubMed:8031147)Curated
Sequence conflicti32 – 321L → N AA sequence (PubMed:8031147)Curated
Sequence conflicti71 – 711Y → C in AAH67433. (PubMed:15489334)Curated
Sequence conflicti235 – 2351V → A in AAF13601. 1 PublicationCurated
Sequence conflicti355 – 3551H → R in AAH67433. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761R → H in allele CYP2E1*2; reduced activity. 1 Publication
Corresponds to variant rs72559710 [ dbSNP | Ensembl ].
VAR_008360
Natural varianti179 – 1791V → I in allele CYP2E1*4. 2 Publications
Corresponds to variant rs6413419 [ dbSNP | Ensembl ].
VAR_008361
Natural varianti219 – 2191N → D.1 Publication
Corresponds to variant rs41299426 [ dbSNP | Ensembl ].
VAR_055382
Natural varianti366 – 3661S → C.1 Publication
Corresponds to variant rs41299434 [ dbSNP | Ensembl ].
VAR_055383
Natural varianti389 – 3891V → I in allele CYP2E1*3. 1 Publication
Corresponds to variant rs55897648 [ dbSNP | Ensembl ].
VAR_008362
Natural varianti457 – 4571H → L.2 Publications
Corresponds to variant rs28969387 [ dbSNP | Ensembl ].
VAR_024727

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02625 mRNA. Translation: AAA35743.1.
J02843 Genomic DNA. Translation: AAA52155.1.
AF182276 mRNA. Translation: AAF13601.1.
DQ515958 Genomic DNA. Translation: ABF47105.1.
AL161645 Genomic DNA. Translation: CAH70047.1.
CH471211 Genomic DNA. Translation: EAW61357.1.
BC067433 mRNA. Translation: AAH67433.1.
AF084225 mRNA. Translation: AAD13753.1.
D50111 Genomic DNA. Translation: BAA08796.1.
CCDSiCCDS7686.1.
PIRiA31949.
RefSeqiNP_000764.1. NM_000773.3.
UniGeneiHs.12907.

Genome annotation databases

EnsembliENST00000252945; ENSP00000252945; ENSG00000130649.
ENST00000463117; ENSP00000440689; ENSG00000130649.
GeneIDi1571.
KEGGihsa:1571.
UCSCiuc001lnj.1. human.

Polymorphism databases

DMDMi117250.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Cytochrome P450 Allele Nomenclature Committee

CYP2E1 alleles

Wikipedia

CYP2E1 entry

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02625 mRNA. Translation: AAA35743.1 .
J02843 Genomic DNA. Translation: AAA52155.1 .
AF182276 mRNA. Translation: AAF13601.1 .
DQ515958 Genomic DNA. Translation: ABF47105.1 .
AL161645 Genomic DNA. Translation: CAH70047.1 .
CH471211 Genomic DNA. Translation: EAW61357.1 .
BC067433 mRNA. Translation: AAH67433.1 .
AF084225 mRNA. Translation: AAD13753.1 .
D50111 Genomic DNA. Translation: BAA08796.1 .
CCDSi CCDS7686.1.
PIRi A31949.
RefSeqi NP_000764.1. NM_000773.3.
UniGenei Hs.12907.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E4E X-ray 2.60 A/B 32-493 [» ]
3E6I X-ray 2.20 A/B 32-493 [» ]
3GPH X-ray 2.70 A/B 32-493 [» ]
3KOH X-ray 2.90 A/B 32-493 [» ]
3LC4 X-ray 3.10 A/B 32-493 [» ]
3T3Z X-ray 2.35 A/B/C/D 32-493 [» ]
ProteinModelPortali P05181.
SMRi P05181. Positions 32-493.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107944. 17 interactions.
IntActi P05181. 10 interactions.
STRINGi 9606.ENSP00000252945.

Chemistry

BindingDBi P05181.
ChEMBLi CHEMBL5281.
DrugBanki DB00316. Acetaminophen.
DB00041. Aldesleukin.
DB00918. Almotriptan.
DB00969. Alosetron.
DB01223. Aminophylline.
DB00321. Amitriptyline.
DB01435. Antipyrine.
DB00972. Azelastine.
DB06770. Benzyl alcohol.
DB04794. Bifonazole.
DB01558. Bromazepam.
DB00835. Brompheniramine.
DB01156. Bupropion.
DB00201. Caffeine.
DB00748. Carbinoxamine.
DB01136. Carvedilol.
DB00477. Chlorpromazine.
DB00356. Chlorzoxazone.
DB00501. Cimetidine.
DB00215. Citalopram.
DB04920. Clevidipine.
DB00636. Clofibrate.
DB00882. Clomifene.
DB01068. Clonazepam.
DB00257. Clotrimazole.
DB00363. Clozapine.
DB01394. Colchicine.
DB00851. Dacarbazine.
DB06637. Dalfampridine.
DB00250. Dapsone.
DB01151. Desipramine.
DB01234. Dexamethasone.
DB01191. Dexfenfluramine.
DB00633. Dexmedetomidine.
DB00514. Dextromethorphan.
DB00829. Diazepam.
DB00586. Diclofenac.
DB00255. Diethylstilbestrol.
DB00822. Disulfiram.
DB01127. Econazole.
DB00228. Enflurane.
DB00109. Enfuvirtide.
DB00655. Estrone.
DB00898. Ethanol.
DB06689. Ethanolamine Oleate.
DB00593. Ethosuximide.
DB00773. Etoposide.
DB01628. Etoricoxib.
DB00949. Felbamate.
DB08868. Fingolimod.
DB01544. Flunitrazepam.
DB00623. Fluphenazine.
DB00690. Flurazepam.
DB00176. Fluvoxamine.
DB00158. Folic Acid.
DB01213. Fomepizole.
DB01296. Glucosamine.
DB01159. Halothane.
DB01355. Hexobarbital.
DB04946. Iloperidone.
DB00458. Imipramine.
DB00753. Isoflurane.
DB00951. Isoniazid.
DB00883. Isosorbide Dinitrate.
DB01167. Itraconazole.
DB00170. Menadione.
DB00371. Meprobamate.
DB00703. Methazolamide.
DB00763. Methimazole.
DB01403. Methotrimeprazine.
DB01028. Methoxyflurane.
DB01011. Metyrapone.
DB00379. Mexiletine.
DB01110. Miconazole.
DB00683. Midazolam.
DB01204. Mitoxantrone.
DB00622. Nicardipine.
DB00184. Nicotine.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB01595. Nitrazepam.
DB00540. Nortriptyline.
DB00904. Ondansetron.
DB01173. Orphenadrine.
DB00526. Oxaliplatin.
DB00617. Paramethadione.
DB00780. Phenelzine.
DB01174. Phenobarbital.
DB01085. Pilocarpine.
DB01100. Pimozide.
DB01131. Proguanil.
DB00818. Propofol.
DB00908. Quinidine.
DB00468. Quinine.
DB01045. Rifampicin.
DB00503. Ritonavir.
DB06201. Rufinamide.
DB00118. S-Adenosylmethionine.
DB01037. Selegiline.
DB01236. Sevoflurane.
DB00203. Sildenafil.
DB00428. Streptozocin.
DB00359. Sulfadiazine.
DB00259. Sulfanilamide.
DB00675. Tamoxifen.
DB01041. Thalidomide.
DB01412. Theobromine.
DB00277. Theophylline.
DB00599. Thiopental.
DB00679. Thioridazine.
DB00208. Ticlopidine.
DB01007. Tioconazole.
DB05109. Trabectedin.
DB00752. Tranylcypromine.
DB00347. Trimethadione.
DB01586. Ursodeoxycholic acid.
DB00549. Zafirlukast.
DB01198. Zopiclone.

PTM databases

PhosphoSitei P05181.

Polymorphism databases

DMDMi 117250.

Proteomic databases

PaxDbi P05181.
PeptideAtlasi P05181.
PRIDEi P05181.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252945 ; ENSP00000252945 ; ENSG00000130649 .
ENST00000463117 ; ENSP00000440689 ; ENSG00000130649 .
GeneIDi 1571.
KEGGi hsa:1571.
UCSCi uc001lnj.1. human.

Organism-specific databases

CTDi 1571.
GeneCardsi GC10P135352.
HGNCi HGNC:2631. CYP2E1.
HPAi HPA009128.
HPA029564.
MIMi 124040. gene.
neXtProti NX_P05181.
PharmGKBi PA129.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000118775.
HOGENOMi HOG000036992.
HOVERGENi HBG015789.
InParanoidi P05181.
KOi K07415.
OMAi GCIPPRY.
OrthoDBi EOG7RBZ85.
PhylomeDBi P05181.
TreeFami TF352043.

Enzyme and pathway databases

BioCyci MetaCyc:HS05414-MONOMER.
Reactomei REACT_13543. Xenobiotics.
REACT_13797. CYP2E1 reactions.
SABIO-RK P05181.

Miscellaneous databases

EvolutionaryTracei P05181.
GeneWikii CYP2E1.
GenomeRNAii 1571.
NextBioi 6461.
PROi P05181.
SOURCEi Search...

Gene expression databases

Bgeei P05181.
CleanExi HS_CYP2E1.
ExpressionAtlasi P05181. baseline and differential.
Genevestigatori P05181.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008070. Cyt_P450_E_grp-I_CYP2E-like.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR01687. EP450ICYP2E.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme."
    Song B.-J., Gelboin H.V., Park S.-S., Yang C.S., Gonzalez F.J.
    J. Biol. Chem. 261:16689-16697(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human ethanol-inducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression."
    Umeno M., McBride O.W., Yang C.S., Gelboin H.V., Gonzalez F.J.
    Biochemistry 27:9006-9013(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of a new human cytochrome P450-2E1 cDNA and establishing the transgenic cell line."
    Zhuge J., Qian Y., Xie H., Yu Y.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. NIEHS SNPs program
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-219; CYS-366 AND LEU-457.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    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.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
  8. "Partial sequence of human brain cytochrome P450 2E1."
    Yoo M., Shin S.W.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-493.
    Tissue: Brain.
  9. "Rapid detection of a novel mutation in the human CYP2EI exon VIII by the PCR method."
    Iwahashi K., Okuyama E., Nakamura K., Furukawa A., Ichikawa Y.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 387-432.
  10. "Purification and characterization of human liver cytochrome P-450-ALC."
    Lasker J.M., Raucy J., Kubota S., Bloswick B.P., Black M., Lieber C.S.
    Biochem. Biophys. Res. Commun. 148:232-238(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Tissue: Liver.
  11. "Human liver cytochrome P-450 related to a rat acetone-inducible, nitrosamine-metabolizing cytochrome P-450: identification and isolation."
    Robinson R.C., Shorr R.G., Varrichio A., Park S.S., Gelboin H.V., Miller H., Friedman F.K.
    Pharmacology 39:137-144(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-20.
  12. "Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties."
    Gillam E.M., Guo Z., Guengerich F.P.
    Arch. Biochem. Biophys. 312:59-66(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-42.
  13. "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."
    Zerilli A., Ratanasavanh D., Lucas D., Goasduff T., Dreano Y., Menard C., Picart D., Berthou F.
    Chem. Res. Toxicol. 10:1205-1212(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  14. "Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates."
    Porubsky P.R., Meneely K.M., Scott E.E.
    J. Biol. Chem. 283:33698-33707(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 32-493 IN COMPLEX WITH THE INHIBITORS INDAZOLE AND 4-METHYLPYRAZOLE AND HEME.
  15. "Genetic polymorphism of human CYP2E1: characterization of two variant alleles."
    Hu Y., Oscarson M., Johansson I., Yue Q.Y., Dahl M.L., Tabone M., Arinco S., Albano E., Ingelman-Sundberg M.
    Mol. Pharmacol. 51:370-376(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYP2E1*2 HIS-76 AND CYP2E1*3 ILE-389.
  16. "Detection and characterization of novel polymorphisms in the CYP2E1 gene."
    Fairbrother K.S., Grove J., de Waziers I., Steimel D.T., Day C.P., Crespi C.L., Daly A.K.
    Pharmacogenetics 8:543-552(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CYP2E1*4 ILE-179.
  17. "Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population."
    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.
    Pharmacogenomics 5:895-931(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ILE-179 AND LEU-457.

Entry informationi

Entry nameiCP2E1_HUMAN
AccessioniPrimary (citable) accession number: P05181
Secondary accession number(s): Q5VZD5, Q6NWT9, Q9UK47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 162 of the entry and version 1 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 10
    Human chromosome 10: 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

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