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P11509

- CP2A6_HUMAN

UniProt

P11509 - CP2A6_HUMAN

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Protein

Cytochrome P450 2A6

Gene

CYP2A6

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

Functioni

Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethylation activity.6 Publications

Catalytic activityi

1,4-cineole + NADPH + O2 = 2-exo-hydroxy-1,4-cineole + NADP+ + H2O.1 Publication

Cofactori

Heme group.

Kineticsi

  1. KM=0.23 µM for coumarin2 Publications
  2. KM=530 µM for 1,4-cineole2 Publications

Vmax=3.5 nmol/min/nmol enzyme toward 2-exo-hydroxy-1,4-cineole2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071SubstrateCurated
Binding sitei297 – 2971Substrate
Metal bindingi439 – 4391Iron (heme axial ligand)

GO - Molecular functioni

  1. coumarin 7-hydroxylase activity Source: UniProtKB
  2. enzyme binding Source: BHF-UCL
  3. heme binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. 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: InterPro

GO - Biological processi

  1. coumarin catabolic process Source: BHF-UCL
  2. coumarin metabolic process Source: BHF-UCL
  3. drug metabolic process Source: BHF-UCL
  4. exogenous drug catabolic process Source: BHF-UCL
  5. small molecule metabolic process Source: Reactome
  6. steroid metabolic process Source: BHF-UCL
  7. 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:HS10343-MONOMER.
ReactomeiREACT_13543. Xenobiotics.
REACT_13797. CYP2E1 reactions.
SABIO-RKP11509.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 2A6 (EC:1.14.13.-)
Alternative name(s):
1,4-cineole 2-exo-monooxygenase
CYPIIA6
Coumarin 7-hydroxylase
Cytochrome P450 IIA3
Cytochrome P450(I)
Gene namesi
Name:CYP2A6
Synonyms:CYP2A3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:2610. CYP2A6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081I → S: Increases phenacetin O-deethylation activity 10 fold; when associated with F-300 and A-301. Increases phenacetin O-deethylation activity 38 fold; when associated with F-300; A-301 and G-369. 1 Publication
Mutagenesisi213 – 2131S → A: No effect on phenacetin O-deethylation activity. 1 Publication
Mutagenesisi300 – 3001I → F: Increases phenacetin O-deethylation activity 3 fold. Increases phenacetin O-deethylation activity 8 fold; when associated with A-301. Increases phenacetin O-deethylation activity 10 fold; when associated with S-208 and A-301. Increases phenacetin O-deethylation activity 12 fold; when associated with A-301 and G-369. Increases phenacetin O-deethylation activity 38 fold; when associated with S-208; A-301 and G-369. 1 Publication
Mutagenesisi301 – 3011G → A: Slightly decreases phenacetin O-deethylation activity. Increases phenacetin O-deethylation activity 8 fold; when associated with F-300. Increases phenacetin O-deethylation activity 10 fold; when associated with S-208 and F-300. Increases phenacetin O-deethylation activity 12 fold; when associated with F-300 and G-369. Increases phenacetin O-deethylation activity 38 fold; when associated with S-208; F-300 and G-369. 1 Publication
Mutagenesisi369 – 3691S → G: Increases phenacetin O-deethylation activity 3 fold. Increases phenacetin O-deethylation activity 38 fold; when associated with S-208; F-300 and A-301. 1 Publication
Mutagenesisi372 – 3721R → H: Increases phenacetin O-deethylation activity 2 fold. 1 Publication

Organism-specific databases

MIMi122720. gene+phenotype.
PharmGKBiPA121.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Cytochrome P450 2A6PRO_0000051668Add
BLAST

Proteomic databases

PaxDbiP11509.
PRIDEiP11509.

PTM databases

PhosphoSiteiP11509.

Expressioni

Tissue specificityi

Liver.2 Publications

Inductioni

By phenobarbital and dexamethasone.2 Publications

Gene expression databases

BgeeiP11509.
ExpressionAtlasiP11509. baseline and differential.
GenevestigatoriP11509.

Organism-specific databases

HPAiHPA046713.
HPA047262.

Interactioni

Protein-protein interaction databases

BioGridi107927. 2 interactions.

Structurei

Secondary structure

1
494
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni41 – 433
Helixi46 – 483
Helixi51 – 533
Helixi54 – 6512
Beta strandi67 – 737
Beta strandi76 – 816
Helixi84 – 918
Turni92 – 987
Helixi105 – 1117
Beta strandi115 – 1184
Helixi121 – 13717
Turni138 – 1414
Helixi143 – 16220
Turni163 – 1653
Helixi171 – 18717
Helixi196 – 21217
Helixi215 – 22713
Beta strandi230 – 2323
Helixi233 – 25624
Helixi267 – 27711
Turni278 – 2803
Helixi288 – 31932
Helixi321 – 33414
Beta strandi337 – 3393
Helixi343 – 3486
Helixi350 – 36314
Beta strandi378 – 3803
Beta strandi383 – 3853
Beta strandi390 – 3934
Helixi395 – 3995
Turni402 – 4043
Helixi413 – 4164
Beta strandi419 – 4213
Helixi442 – 45918
Beta strandi460 – 4667
Helixi468 – 4703
Beta strandi476 – 4838
Beta strandi489 – 4935

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z10X-ray1.90A/B/C/D29-494[»]
1Z11X-ray2.05A/B/C/D29-494[»]
2FDUX-ray1.85A/B/C/D29-494[»]
2FDVX-ray1.65A/B/C/D29-494[»]
2FDWX-ray2.05A/B/C/D29-494[»]
2FDYX-ray1.95A/B/C/D29-494[»]
3EBSX-ray2.15A/B/C/D29-494[»]
3T3QX-ray2.10A/B/C/D29-494[»]
3T3RX-ray2.40A/B/C/D29-494[»]
4EJJX-ray2.30A/B/C/D29-494[»]
ProteinModelPortaliP11509.
SMRiP11509. Positions 30-494.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11509.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118775.
HOVERGENiHBG015789.
InParanoidiP11509.
KOiK17683.
OMAiDTHGANI.
OrthoDBiEOG7RBZ85.
PhylomeDBiP11509.
TreeFamiTF352043.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008067. Cyt_P450_E_grp-I_CYP2A-like.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR01684. EP450ICYP2A.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11509-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLASGMLLVA LLVCLTVMVL MSVWQQRKSK GKLPPGPTPL PFIGNYLQLN
60 70 80 90 100
TEQMYNSLMK ISERYGPVFT IHLGPRRVVV LCGHDAVREA LVDQAEEFSG
110 120 130 140 150
RGEQATFDWV FKGYGVVFSN GERAKQLRRF SIATLRDFGV GKRGIEERIQ
160 170 180 190 200
EEAGFLIDAL RGTGGANIDP TFFLSRTVSN VISSIVFGDR FDYKDKEFLS
210 220 230 240 250
LLRMMLGIFQ FTSTSTGQLY EMFSSVMKHL PGPQQQAFQL LQGLEDFIAK
260 270 280 290 300
KVEHNQRTLD PNSPRDFIDS FLIRMQEEEK NPNTEFYLKN LVMTTLNLFI
310 320 330 340 350
GGTETVSTTL RYGFLLLMKH PEVEAKVHEE IDRVIGKNRQ PKFEDRAKMP
360 370 380 390 400
YMEAVIHEIQ RFGDVIPMSL ARRVKKDTKF RDFFLPKGTE VFPMLGSVLR
410 420 430 440 450
DPSFFSNPQD FNPQHFLNEK GQFKKSDAFV PFSIGKRNCF GEGLARMELF
460 470 480 490
LFFTTVMQNF RLKSSQSPKD IDVSPKHVGF ATIPRNYTMS FLPR
Length:494
Mass (Da):56,501
Last modified:October 5, 2010 - v3
Checksum:i8C05CBF0EFC698AF
GO

Sequence cautioni

The sequence AAA52147.1 differs from that shown. Reason: Numerous conflicts and frameshifts.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 75Missing in CAA32097. (PubMed:2726448)Curated
Sequence conflicti255 – 2551N → K in CAA32097. (PubMed:2726448)Curated
Sequence conflicti326 – 3261K → Q in CAA32097. (PubMed:2726448)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51G → R in allele CYP2A6*13. 2 Publications
Corresponds to variant rs28399434 [ dbSNP | Ensembl ].
VAR_018330
Natural varianti29 – 291S → N in allele CYP2A6*14. 3 Publications
Corresponds to variant rs28399435 [ dbSNP | Ensembl ].
VAR_018331
Natural varianti110 – 1101V → L in allele CYP2A6*24, increases phenacetin O-deethylation activity 4 fold. 1 Publication
Corresponds to variant rs72549435 [ dbSNP | Ensembl ].
VAR_055035
Natural varianti118 – 1181F → L in allele CYP2A6*25 and allele CYP2A6*26. 2 Publications
Corresponds to variant rs28399440 [ dbSNP | Ensembl ].
VAR_024711
Natural varianti128 – 1281R → L in allele CYP2A6*26. 1 Publication
VAR_055036
Natural varianti128 – 1281R → Q in allele CYP2A6*6; loss of activity. 2 Publications
Corresponds to variant rs4986891 [ dbSNP | Ensembl ].
VAR_011577
Natural varianti131 – 1311S → A in allele CYP2A6*26. 1 Publication
Corresponds to variant rs59552350 [ dbSNP | Ensembl ].
VAR_055037
Natural varianti160 – 1601L → H in allele CYP2A6*2; unable to catalyze 7-hydroxylation of coumarin; causes switching from coumarin 7-hydroxylation to 3-hydroxylation. 4 Publications
Corresponds to variant rs1801272 [ dbSNP | Ensembl ].
VAR_001249
Natural varianti194 – 1941K → E in allele CYP2A6*15. 1 Publication
VAR_018332
Natural varianti203 – 2031R → C in allele CYP2A6*23; greatly reduced activity toward nicotine C-oxidation as well as reduced coumarin 7-hydroxylation. 2 Publications
Corresponds to variant rs56256500 [ dbSNP | Ensembl ].
VAR_055034
Natural varianti203 – 2031R → S in allele CYP2A6*16. 2 Publications
Corresponds to variant rs56256500 [ dbSNP | Ensembl ].
VAR_018333
Natural varianti224 – 2241S → P.1 Publication
Corresponds to variant rs111033610 [ dbSNP | Ensembl ].
VAR_024712
Natural varianti292 – 2921V → M.
Corresponds to variant rs2644906 [ dbSNP | Ensembl ].
VAR_059149
Natural varianti294 – 2941T → S.
Corresponds to variant rs4997557 [ dbSNP | Ensembl ].
VAR_048448
Natural varianti365 – 3651V → M in allele CYP2A6*17, increases phenacetin O-deethylation activity 2 fold. 3 Publications
Corresponds to variant rs28399454 [ dbSNP | Ensembl ].
VAR_024713
Natural varianti392 – 3921F → Y.9 Publications
Corresponds to variant rs1809810 [ dbSNP | Ensembl ].
VAR_055033
Natural varianti418 – 4181N → D in allele CYP2A6*28. 3 Publications
Corresponds to variant rs28399463 [ dbSNP | Ensembl ].
VAR_024714
Natural varianti419 – 4191E → D in allele CYP2A6*28. 4 Publications
Corresponds to variant rs8192730 [ dbSNP | Ensembl ].
VAR_018375
Natural varianti438 – 4381N → Y in allele CYP2A6*24. 1 Publication
VAR_055038
Natural varianti471 – 4711I → T in allele CYP2A6*7. 3 Publications
Corresponds to variant rs5031016 [ dbSNP | Ensembl ].
VAR_011578
Natural varianti476 – 4761K → R.2 Publications
Corresponds to variant rs6413474 [ dbSNP | Ensembl ].
VAR_024715
Natural varianti479 – 4791G → V in allele CYP2A6*5; loss of activity. 1 Publication
Corresponds to variant rs5031017 [ dbSNP | Ensembl ].
VAR_008356
Natural varianti485 – 4851R → L in allele CYP2A6*8. 2 Publications
Corresponds to variant rs28399468 [ dbSNP | Ensembl ].
VAR_011579

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13897 mRNA. Translation: CAA32097.1.
X13929 mRNA. Translation: CAA32117.1.
X13930 mRNA. Translation: CAA32118.1.
M33318 mRNA. Translation: AAA52067.1.
AF182275 mRNA. Translation: AAF13600.1.
AK312964 mRNA. Translation: BAG35803.1.
EU135979 Genomic DNA. Translation: ABV02584.1.
FJ440681 Genomic DNA. Translation: ACK44068.1.
AC008537 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57012.1.
BC096253 mRNA. Translation: AAH96253.3.
BC096254 mRNA. Translation: AAH96254.1.
BC096255 mRNA. Translation: AAH96255.1.
BC096256 mRNA. Translation: AAH96256.1.
AF326721 Genomic DNA. Translation: AAG45229.1.
K03192 mRNA. Translation: AAA52147.1. Sequence problems.
CCDSiCCDS12568.1.
PIRiA00190. O4HUPB.
S04698. O4HUA6.
RefSeqiNP_000753.3. NM_000762.5.
UniGeneiHs.250615.

Genome annotation databases

EnsembliENST00000301141; ENSP00000301141; ENSG00000255974.
GeneIDi1548.
KEGGihsa:1548.
UCSCiuc002opl.4. human.

Polymorphism databases

DMDMi308153612.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Cytochrome P450 Allele Nomenclature Committee

CYP2A6 alleles

NIEHS-SNPs
Wikipedia

CYP2A6 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13897 mRNA. Translation: CAA32097.1 .
X13929 mRNA. Translation: CAA32117.1 .
X13930 mRNA. Translation: CAA32118.1 .
M33318 mRNA. Translation: AAA52067.1 .
AF182275 mRNA. Translation: AAF13600.1 .
AK312964 mRNA. Translation: BAG35803.1 .
EU135979 Genomic DNA. Translation: ABV02584.1 .
FJ440681 Genomic DNA. Translation: ACK44068.1 .
AC008537 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57012.1 .
BC096253 mRNA. Translation: AAH96253.3 .
BC096254 mRNA. Translation: AAH96254.1 .
BC096255 mRNA. Translation: AAH96255.1 .
BC096256 mRNA. Translation: AAH96256.1 .
AF326721 Genomic DNA. Translation: AAG45229.1 .
K03192 mRNA. Translation: AAA52147.1 . Sequence problems.
CCDSi CCDS12568.1.
PIRi A00190. O4HUPB.
S04698. O4HUA6.
RefSeqi NP_000753.3. NM_000762.5.
UniGenei Hs.250615.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z10 X-ray 1.90 A/B/C/D 29-494 [» ]
1Z11 X-ray 2.05 A/B/C/D 29-494 [» ]
2FDU X-ray 1.85 A/B/C/D 29-494 [» ]
2FDV X-ray 1.65 A/B/C/D 29-494 [» ]
2FDW X-ray 2.05 A/B/C/D 29-494 [» ]
2FDY X-ray 1.95 A/B/C/D 29-494 [» ]
3EBS X-ray 2.15 A/B/C/D 29-494 [» ]
3T3Q X-ray 2.10 A/B/C/D 29-494 [» ]
3T3R X-ray 2.40 A/B/C/D 29-494 [» ]
4EJJ X-ray 2.30 A/B/C/D 29-494 [» ]
ProteinModelPortali P11509.
SMRi P11509. Positions 30-494.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107927. 2 interactions.

Chemistry

BindingDBi P11509.
ChEMBLi CHEMBL5282.
DrugBanki DB00316. Acetaminophen.
DB01118. Amiodarone.
DB00381. Amlodipine.
DB01351. Amobarbital.
DB00182. Amphetamine.
DB01435. Antipyrine.
DB01274. Arformoterol.
DB00972. Azelastine.
DB00207. Azithromycin.
DB00921. Buprenorphine.
DB01156. Bupropion.
DB00356. Chlorzoxazone.
DB00568. Cinnarizine.
DB00604. Cisapride.
DB00636. Clofibrate.
DB00882. Clomifene.
DB00257. Clotrimazole.
DB00363. Clozapine.
DB00531. Cyclophosphamide.
DB06292. Dapagliflozin.
DB01151. Desipramine.
DB01234. Dexamethasone.
DB01191. Dexfenfluramine.
DB00255. Diethylstilbestrol.
DB00470. Dronabinol.
DB00216. Eletriptan.
DB04953. Ezogabine.
DB04841. Flunarizine.
DB01544. Flunitrazepam.
DB00544. Fluorouracil.
DB00690. Flurazepam.
DB01213. Fomepizole.
DB00983. Formoterol.
DB01159. Halothane.
DB01181. Ifosfamide.
DB00951. Isoniazid.
DB01026. Ketoconazole.
DB01006. Letrozole.
DB00281. Lidocaine.
DB04871. Lorcaserin.
DB01043. Memantine.
DB00170. Menadione.
DB00763. Methimazole.
DB00553. Methoxsalen.
DB01028. Methoxyflurane.
DB01011. Metyrapone.
DB01110. Miconazole.
DB00471. Montelukast.
DB00238. Nevirapine.
DB00184. Nicotine.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB01059. Norfloxacin.
DB00312. Pentobarbital.
DB01174. Phenobarbital.
DB01085. Pilocarpine.
DB00860. Prednisolone.
DB00396. Progesterone.
DB00818. Propofol.
DB01045. Rifampicin.
DB00412. Rosiglitazone.
DB01037. Selegiline.
DB01236. Sevoflurane.
DB06729. Sulfaphenazole.
DB00675. Tamoxifen.
DB00752. Tranylcypromine.
DB00755. Tretinoin.
DB01361. Troleandomycin.
DB00313. Valproic Acid.
DB00495. Zidovudine.

PTM databases

PhosphoSitei P11509.

Polymorphism databases

DMDMi 308153612.

Proteomic databases

PaxDbi P11509.
PRIDEi P11509.

Protocols and materials databases

DNASUi 1548.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301141 ; ENSP00000301141 ; ENSG00000255974 .
GeneIDi 1548.
KEGGi hsa:1548.
UCSCi uc002opl.4. human.

Organism-specific databases

CTDi 1548.
GeneCardsi GC19M041352.
HGNCi HGNC:2610. CYP2A6.
HPAi HPA046713.
HPA047262.
MIMi 122720. gene+phenotype.
neXtProti NX_P11509.
PharmGKBi PA121.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000118775.
HOVERGENi HBG015789.
InParanoidi P11509.
KOi K17683.
OMAi DTHGANI.
OrthoDBi EOG7RBZ85.
PhylomeDBi P11509.
TreeFami TF352043.

Enzyme and pathway databases

BioCyci MetaCyc:HS10343-MONOMER.
Reactomei REACT_13543. Xenobiotics.
REACT_13797. CYP2E1 reactions.
SABIO-RK P11509.

Miscellaneous databases

ChiTaRSi CYP2A6. human.
EvolutionaryTracei P11509.
GeneWikii CYP2A6.
GenomeRNAii 1548.
NextBioi 6401.
PROi P11509.
SOURCEi Search...

Gene expression databases

Bgeei P11509.
ExpressionAtlasi P11509. baseline and differential.
Genevestigatori P11509.

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.
IPR008067. Cyt_P450_E_grp-I_CYP2A-like.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR01684. EP450ICYP2A.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity."
    Miles J.S., Bickmore W., Brook J.D., McLaren A.W., Meehan R., Wolf C.R.
    Nucleic Acids Res. 17:2907-2917(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-29 AND TYR-392.
    Tissue: Liver.
  2. "cDNA and deduced amino acid sequences of human P450 IIA3 (CYP2A3)."
    Yamano S., Nagata K., Yamazoe Y., Kato R., Gelboin H.V., Gonzalez F.J.
    Nucleic Acids Res. 17:4888-4888(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-160 AND TYR-392.
    Tissue: Hepatocyte.
  3. "The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes."
    Yamano S., Tatsuno J., Gonzalez F.J.
    Biochemistry 29:1322-1329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-160 AND TYR-392, CHARACTERIZATION OF VARIANT HIS-160.
    Tissue: Hepatocyte.
  4. "Sequence of a new human cytochrome P450-2A6 cDNA."
    Zhuge J., Qian Y., Xie H., Yu Y.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-392.
    Tissue: Liver.
  5. "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], VARIANT TYR-392.
    Tissue: Mammary gland.
  6. NIEHS SNPs program
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-160; CYS-203; MET-365; TYR-392; ASP-418 AND ASP-419.
  7. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TYR-392.
  9. "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], VARIANTS HIS-160; TYR-392 AND ARG-476.
  10. "Isolation and characterization of a cytochrome P450 of the IIA subfamily from human liver microsomes."
    Maurice M., Emiliani S., Dalet-Beluche I., Derancourt J., Lange R.
    Eur. J. Biochem. 200:511-517(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
  11. "Purification and characterization of human liver microsomal cytochrome P-450 2A6."
    Yun C.H., Shimada T., Guengerich F.P.
    Mol. Pharmacol. 40:679-685(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
  12. "CYP2A6*6, a novel polymorphism in cytochrome p450 2A6, has a single amino acid substitution (R128Q) that inactivates enzymatic activity."
    Kitagawa K., Kunugita N., Kitagawa M., Kawamoto T.
    J. Biol. Chem. 276:17830-17835(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-164, VARIANT CYP2A6*6 GLN-128.
  13. "Isolation and sequence of a human cytochrome P-450 cDNA clone."
    Phillips I.R., Shephard E.A., Ashworth A., Rabin B.R.
    Proc. Natl. Acad. Sci. U.S.A. 82:983-987(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 163-494, VARIANT TYR-392.
  14. "Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes."
    Miyazawa M., Shindo M., Shimada T.
    Xenobiotica 31:713-723(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION AS 1,4-CINEOLE 2-EXO-MONOOXYGENASE, BIOPHYSICOCHEMICAL PROPERTIES.
  15. "Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen."
    Yano J.K., Hsu M.H., Griffin K.J., Stout C.D., Johnson E.F.
    Nat. Struct. Mol. Biol. 12:822-823(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-494 IN COMPLEX WITH COUMARIN; HEME AND THE INHIBITOR METHOXSALEN, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  16. "Synthetic inhibitors of cytochrome P-450 2A6: inhibitory activity, difference spectra, mechanism of inhibition, and protein cocrystallization."
    Yano J.K., Denton T.T., Cerny M.A., Zhang X., Johnson E.F., Cashman J.R.
    J. Med. Chem. 49:6987-7001(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-494 IN COMPLEX WITH PHENACETIN AND HEME, FUNCTION.
  17. "Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes."
    DeVore N.M., Smith B.D., Urban M.J., Scott E.E.
    Drug Metab. Dispos. 36:2582-2590(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 29-494 IN COMPLEX WITH PHENACETIN AND HEME, FUNCTION, CHARACTERIZATION OF VARIANTS LEU-110 AND MET-365, MUTAGENESIS OF ILE-208; SER-213; ILE-300; GLY-301; SER-369 AND ARG-372.
  18. "A single amino acid substitution (Leu160His) in cytochrome P450 CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of coumarin."
    Hadidi H., Zahlsen K., Idle J.R., Cholerton S.
    Food Chem. Toxicol. 35:903-907(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CYP2A6*2 HIS-160.
  19. "Identification and characterisation of novel polymorphisms in the CYP2A locus: implications for nicotine metabolism."
    Oscarson M., McLellan R.A., Gullsten H., Agundez J.A., Benitez J., Rautio A., Raunio H., Pelkonen O., Ingelman-Sundberg M.
    FEBS Lett. 460:321-327(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CYP2A6*5 VAL-479.
  20. "A novel single nucleotide polymorphism altering stability and activity of CYP2a6."
    Ariyoshi N., Sawamura Y., Kamataki T.
    Biochem. Biophys. Res. Commun. 281:810-814(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYP2A6*7 THR-471 AND CYP2A6*8 LEU-485.
  21. "Twenty one novel single nucleotide polymorphisms (SNPs) of the CYP2A6 gene in Japanese and Caucasians."
    Kiyotani K., Fujieda M., Yamazaki H., Shimada T., Guengerich F.P., Parkinson A., Nakagawa K., Ishizaki T., Kamataki T.
    Drug Metab. Pharmacokinet. 17:482-487(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYP2A6*13 ARG-5; CYP2A6*14 ASN-29; CYP2A6*15 GLU-194 AND CYP2A6*16 SER-203.
  22. "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."
    Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.
    J. Hum. Genet. 48:249-270(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ASP-419 AND THR-471.
  23. "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 ARG-5; ASN-29; LEU-118; GLN-128; PRO-224; MET-365; ASP-418; ASP-419; THR-471; ARG-476 AND LEU-485.
  24. "Novel and established CYP2A6 alleles impair in vivo nicotine metabolism in a population of Black African descent."
    Mwenifumbo J.C., Al Koudsi N., Ho M.K., Zhou Q., Hoffmann E.B., Sellers E.M., Tyndale R.F.
    Hum. Mutat. 29:679-688(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LEU-110; LEU-118; LEU-128; ALA-131; ASP-418; ASP-419 AND TYR-438.
  25. "A novel CYP2A6 allele, CYP2A6*23, impairs enzyme function in vitro and in vivo and decreases smoking in a population of Black-African descent."
    Ho M.K., Mwenifumbo J.C., Zhao B., Gillam E.M., Tyndale R.F.
    Pharmacogenet. Genomics 18:67-75(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYS-203; SER-203 AND MET-365, CHARACTERIZATION OF VARIANT CYS-203.

Entry informationi

Entry nameiCP2A6_HUMAN
AccessioniPrimary (citable) accession number: P11509
Secondary accession number(s): A7YAE5
, B2R7F6, P00190, P10890, Q16803, Q4VAT9, Q4VAU0, Q4VAU1, Q9H1Z7, Q9UCU0, Q9UK48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 175 of the entry and version 3 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 19
    Human chromosome 19: 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