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Protein

Cytochrome P450 2A6

Gene

CYP2A6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Kineticsi

  1. KM=0.23 µM for coumarin2 Publications
  2. KM=530 µM for 1,4-cineole2 Publications
  1. Vmax=3.5 nmol/min/nmol enzyme toward 2-exo-hydroxy-1,4-cineole2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei107SubstrateCurated1
Binding sitei297Substrate1
Metal bindingi439Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

  • coumarin catabolic process Source: BHF-UCL
  • coumarin metabolic process Source: BHF-UCL
  • drug metabolic process Source: BHF-UCL
  • epoxygenase P450 pathway Source: GO_Central
  • exogenous drug catabolic process Source: BHF-UCL
  • steroid metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS10343-MONOMER.
ZFISH:HS10343-MONOMER.
BRENDAi1.14.14.1. 2681.
ReactomeiR-HSA-211981. Xenobiotics.
R-HSA-211999. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:2610. CYP2A6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • organelle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi208I → 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 Publication1
Mutagenesisi213S → A: No effect on phenacetin O-deethylation activity. 1 Publication1
Mutagenesisi300I → 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 Publication1
Mutagenesisi301G → 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 Publication1
Mutagenesisi369S → 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 Publication1
Mutagenesisi372R → H: Increases phenacetin O-deethylation activity 2 fold. 1 Publication1

Organism-specific databases

DisGeNETi1548.
MalaCardsiCYP2A6.
MIMi122720. gene+phenotype.
PharmGKBiPA121.

Chemistry databases

ChEMBLiCHEMBL5282.
DrugBankiDB00316. 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.
DB09068. Vortioxetine.
DB00495. Zidovudine.
GuidetoPHARMACOLOGYi1321.

Polymorphism and mutation databases

BioMutaiCYP2A6.
DMDMi308153612.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000516681 – 494Cytochrome P450 2A6Add BLAST494

Proteomic databases

PaxDbiP11509.
PeptideAtlasiP11509.
PRIDEiP11509.

PTM databases

iPTMnetiP11509.
PhosphoSitePlusiP11509.

Expressioni

Tissue specificityi

Liver.2 Publications

Inductioni

By phenobarbital and dexamethasone.2 Publications

Gene expression databases

BgeeiENSG00000255974.
ExpressionAtlasiP11509. baseline and differential.
GenevisibleiP11509. HS.

Organism-specific databases

HPAiHPA046713.
HPA047262.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107927. 4 interactors.
STRINGi9606.ENSP00000301141.

Chemistry databases

BindingDBiP11509.

Structurei

Secondary structure

1494
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni41 – 43Combined sources3
Helixi46 – 48Combined sources3
Helixi51 – 53Combined sources3
Helixi54 – 65Combined sources12
Beta strandi67 – 73Combined sources7
Beta strandi76 – 81Combined sources6
Helixi84 – 91Combined sources8
Turni92 – 98Combined sources7
Helixi105 – 111Combined sources7
Beta strandi115 – 118Combined sources4
Helixi121 – 137Combined sources17
Turni138 – 141Combined sources4
Helixi143 – 162Combined sources20
Turni163 – 165Combined sources3
Helixi171 – 187Combined sources17
Helixi196 – 212Combined sources17
Helixi215 – 227Combined sources13
Beta strandi230 – 232Combined sources3
Helixi233 – 256Combined sources24
Helixi267 – 277Combined sources11
Turni278 – 280Combined sources3
Helixi288 – 319Combined sources32
Helixi321 – 334Combined sources14
Beta strandi337 – 339Combined sources3
Helixi343 – 348Combined sources6
Helixi350 – 363Combined sources14
Beta strandi378 – 380Combined sources3
Beta strandi383 – 385Combined sources3
Beta strandi390 – 393Combined sources4
Helixi395 – 399Combined sources5
Turni402 – 404Combined sources3
Beta strandi405 – 407Combined sources3
Helixi413 – 416Combined sources4
Beta strandi419 – 421Combined sources3
Helixi442 – 459Combined sources18
Beta strandi460 – 466Combined sources7
Helixi468 – 470Combined sources3
Beta strandi476 – 483Combined sources8
Beta strandi489 – 493Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RUIX-ray2.61A/B/C/D/E/F29-494[»]
ProteinModelPortaliP11509.
SMRiP11509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11509.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiKOG0156. Eukaryota.
COG2124. LUCA.
HOVERGENiHBG015789.
InParanoidiP11509.
KOiK17683.
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 differs from that shown. Numerous conflicts and frameshifts.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3 – 7Missing in CAA32097 (PubMed:2726448).Curated5
Sequence conflicti255N → K in CAA32097 (PubMed:2726448).Curated1
Sequence conflicti326K → Q in CAA32097 (PubMed:2726448).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0183305G → R in allele CYP2A6*13. 2 PublicationsCorresponds to variant rs28399434dbSNPEnsembl.1
Natural variantiVAR_01833129S → N in allele CYP2A6*14. 3 PublicationsCorresponds to variant rs28399435dbSNPEnsembl.1
Natural variantiVAR_055035110V → L in allele CYP2A6*24; increases phenacetin O-deethylation activity 4 fold. 2 PublicationsCorresponds to variant rs72549435dbSNPEnsembl.1
Natural variantiVAR_024711118F → L in allele CYP2A6*25 and allele CYP2A6*26. 2 PublicationsCorresponds to variant rs28399440dbSNPEnsembl.1
Natural variantiVAR_055036128R → L in allele CYP2A6*26. 1 Publication1
Natural variantiVAR_011577128R → Q in allele CYP2A6*6; loss of activity. 2 PublicationsCorresponds to variant rs4986891dbSNPEnsembl.1
Natural variantiVAR_055037131S → A in allele CYP2A6*26. 1 PublicationCorresponds to variant rs59552350dbSNPEnsembl.1
Natural variantiVAR_001249160L → H in allele CYP2A6*2; unable to catalyze 7-hydroxylation of coumarin; causes switching from coumarin 7-hydroxylation to 3-hydroxylation. 5 PublicationsCorresponds to variant rs1801272dbSNPEnsembl.1
Natural variantiVAR_018332194K → E in allele CYP2A6*15. 1 Publication1
Natural variantiVAR_055034203R → C in allele CYP2A6*23; greatly reduced activity toward nicotine C-oxidation as well as reduced coumarin 7-hydroxylation. 2 PublicationsCorresponds to variant rs56256500dbSNPEnsembl.1
Natural variantiVAR_018333203R → S in allele CYP2A6*16. 2 PublicationsCorresponds to variant rs56256500dbSNPEnsembl.1
Natural variantiVAR_024712224S → P.1 PublicationCorresponds to variant rs111033610dbSNPEnsembl.1
Natural variantiVAR_059149292V → M.Corresponds to variant rs2644906dbSNPEnsembl.1
Natural variantiVAR_048448294T → S.Corresponds to variant rs4997557dbSNPEnsembl.1
Natural variantiVAR_024713365V → M in allele CYP2A6*17, increases phenacetin O-deethylation activity 2 fold. 4 PublicationsCorresponds to variant rs28399454dbSNPEnsembl.1
Natural variantiVAR_055033392F → Y.9 PublicationsCorresponds to variant rs1809810dbSNPEnsembl.1
Natural variantiVAR_024714418N → D in allele CYP2A6*28. 3 PublicationsCorresponds to variant rs28399463dbSNPEnsembl.1
Natural variantiVAR_018375419E → D in allele CYP2A6*28. 4 PublicationsCorresponds to variant rs8192730dbSNPEnsembl.1
Natural variantiVAR_055038438N → Y in allele CYP2A6*24. 1 Publication1
Natural variantiVAR_011578471I → T in allele CYP2A6*7. 3 PublicationsCorresponds to variant rs5031016dbSNPEnsembl.1
Natural variantiVAR_024715476K → R.2 PublicationsCorresponds to variant rs6413474dbSNPEnsembl.1
Natural variantiVAR_008356479G → V in allele CYP2A6*5; loss of activity. 1 PublicationCorresponds to variant rs5031017dbSNPEnsembl.1
Natural variantiVAR_011579485R → L in allele CYP2A6*8. 2 PublicationsCorresponds to variant rs28399468dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RUIX-ray2.61A/B/C/D/E/F29-494[»]
ProteinModelPortaliP11509.
SMRiP11509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107927. 4 interactors.
STRINGi9606.ENSP00000301141.

Chemistry databases

BindingDBiP11509.
ChEMBLiCHEMBL5282.
DrugBankiDB00316. 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.
DB09068. Vortioxetine.
DB00495. Zidovudine.
GuidetoPHARMACOLOGYi1321.

PTM databases

iPTMnetiP11509.
PhosphoSitePlusiP11509.

Polymorphism and mutation databases

BioMutaiCYP2A6.
DMDMi308153612.

Proteomic databases

PaxDbiP11509.
PeptideAtlasiP11509.
PRIDEiP11509.

Protocols and materials databases

DNASUi1548.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1548.
DisGeNETi1548.
GeneCardsiCYP2A6.
HGNCiHGNC:2610. CYP2A6.
HPAiHPA046713.
HPA047262.
MalaCardsiCYP2A6.
MIMi122720. gene+phenotype.
neXtProtiNX_P11509.
PharmGKBiPA121.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0156. Eukaryota.
COG2124. LUCA.
HOVERGENiHBG015789.
InParanoidiP11509.
KOiK17683.
PhylomeDBiP11509.
TreeFamiTF352043.

Enzyme and pathway databases

BioCyciMetaCyc:HS10343-MONOMER.
ZFISH:HS10343-MONOMER.
BRENDAi1.14.14.1. 2681.
ReactomeiR-HSA-211981. Xenobiotics.
R-HSA-211999. CYP2E1 reactions.
SABIO-RKP11509.

Miscellaneous databases

EvolutionaryTraceiP11509.
GeneWikiiCYP2A6.
GenomeRNAii1548.
PROiP11509.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000255974.
ExpressionAtlasiP11509. baseline and differential.
GenevisibleiP11509. HS.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 196 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.