P20813 (CP2B6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 2B6
EC=1.14.13.-

Alternative name(s):
1,4-cineole 2-exo-monooxygenase
CYPIIB6
Cytochrome P450 IIB1

Gene names

Name:

CYP2B6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase. Ref.7
Catalytic activity	1,4-cineole + NADPH + O2 = 2-exo-hydroxy-1,4-cineole + NADP+ + H2O. Ref.7
Cofactor	Heme group.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Tissue specificity	Expressed in liver, lung and heart right ventricle. Ref.6
Induction	By phenobarbital.
Post-translational modification	Phosphorylation is accompanied by a decrease in enzyme activity By similarity.
Polymorphism	Genetic variations in CYP2B6 are responsible for poor metabolism of efavirenz and, therefore, susceptibility to efavirenz toxicity in the central nervous system [MIM:614546]. Efavirenz is a non-nucleoside reverse transcriptase inhibitor frequently prescribed with 2 nucleoside reverse transcriptase inhibitors as initial therapy for human immunodeficiency virus (HIV) infection. Up to half of patients treated with efavirenz, experience side effects in the central nervous system, including dizziness, insomnia, impaired concentration, somnolence, and abnormal dreams. Severe depression, aggressive behavior, and paranoid or manic reactions may also occur, depending on efavirenz concentration in the plasma.
Sequence similarities	Belongs to the cytochrome P450 family.
Biophysicochemical properties	Kinetic parameters: KM=360 µM for 1,4-cineole Ref.7 Vmax=3.4 nmol/min/nmol enzyme toward 2-exo-hydroxy-1,4-cineole

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular ketone metabolic process Inferred from direct assay PubMed 19651758. Source: BHF-UCL exogenous drug catabolic process Inferred from direct assay PubMed 19029318. Source: BHF-UCL steroid metabolic process Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from direct assay PubMed 19651758. Source: BHF-UCL 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 Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 491

491

Cytochrome P450 2B6

PRO_0000051683

Sites

Metal binding

436

1

Iron (heme axial ligand)

Amino acid modifications

Modified residue

128

1

Phosphoserine; by PKA By similarity

Natural variations

Natural variant

21

1

Q → L in allele CYP2B6*10. Ref.19
Corresponds to variant rs34883432 [ dbSNP | Ensembl ].

VAR_023563

Natural variant

22

1

R → C in allele CYP2B6*2 and allele CYP2B6*10. Ref.3 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20
Corresponds to variant rs8192709 [ dbSNP | Ensembl ].

VAR_016927

Natural variant

26

1

T → S. Ref.3
Corresponds to variant rs33973337 [ dbSNP | Ensembl ].

VAR_025206

Natural variant

28

1

D → G. Ref.3
Corresponds to variant rs33980385 [ dbSNP | Ensembl ].

VAR_025207

Natural variant

29

1

R → P.
Corresponds to variant rs34284776 [ dbSNP | Ensembl ].

VAR_033819

Natural variant

29

1

R → S. Ref.3
Corresponds to variant rs33926104 [ dbSNP | Ensembl ].

VAR_025208

Natural variant

46

1

M → V in allele CYP2B6*11. Ref.19
Corresponds to variant rs35303484 [ dbSNP | Ensembl ].

VAR_023564

Natural variant

99

1

G → E in allele CYP2B6*12. Ref.19
Corresponds to variant rs36060847 [ dbSNP | Ensembl ].

VAR_023565

Natural variant

139

1

K → E in allele CYP2B6*8 and allele CYP2B6*13. Ref.18 Ref.19

VAR_016948

Natural variant

140

1

R → Q in allele CYP2B6*14. Ref.19
Corresponds to variant rs35773040 [ dbSNP | Ensembl ].

VAR_023566

Natural variant

167

1

P → A. Ref.2 Ref.17
Corresponds to variant rs3826711 [ dbSNP | Ensembl ].

VAR_016924

Natural variant

172

1

Q → H in allele CYP2B6*6, allele CYP2B6*7, allele CYP2B6*9 and allele CYP2B6*13. Ref.2 Ref.3 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20
Corresponds to variant rs3745274 [ dbSNP | Ensembl ].

VAR_016925

Natural variant

259

1

S → R in allele CYP2B6*3. Ref.15 Ref.16
Corresponds to variant rs45482602 [ dbSNP | Ensembl ].

VAR_016928

Natural variant

262

1

K → R in allele CYP2B6*4, allele CYP2B6*6, allele CYP2B6*7 and allele CYP2B6*13; slight decrease in activity. Ref.2 Ref.3 Ref.15 Ref.16 Ref.20
Corresponds to variant rs2279343 [ dbSNP | Ensembl ].

VAR_016926

Natural variant

289

1

N → K. Ref.3
Corresponds to variant rs34277950 [ dbSNP | Ensembl ].

VAR_025209

Natural variant

306

1

T → S. Ref.3
Corresponds to variant rs34698757 [ dbSNP | Ensembl ].

VAR_025210

Natural variant

328

1

I → T. Ref.3 Ref.20
Corresponds to variant rs28399499 [ dbSNP | Ensembl ].

VAR_024716

Natural variant

391

1

I → N in allele CYP2B6*15. Ref.19
Corresponds to variant rs35979566 [ dbSNP | Ensembl ].

VAR_023567

Natural variant

487

1

R → C in allele CYP2B6*5 and allele CYP2B6*7. Ref.3 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20
Corresponds to variant rs3211371 [ dbSNP | Ensembl ].

VAR_016929

Experimental info

Sequence conflict

146

1

I → T in AAF13602. Ref.2

Sequence conflict

238

1

L → P in AAF13602. Ref.2

Secondary structure

1

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491

Helix Strand Turn

Details...

Turn

38 – 40

3

Helix

43 – 45

3

Helix

51 – 62

12

Beta strand

64 – 70

7

Beta strand

73 – 78

6

Helix

81 – 88

8

Turn

89 – 93

5

Helix

94 – 96

3

Turn

102 – 104

3

Helix

105 – 108

4

Turn

113 – 115

3

Helix

118 – 134

17

Turn

135 – 137

3

Helix

142 – 159

18

Turn

160 – 162

3

Helix

168 – 184

17

Helix

193 – 209

17

Helix

212 – 224

13

Helix

230 – 254

25

Helix

264 – 274

11

Beta strand

275 – 278

4

Helix

283 – 285

3

Helix

288 – 316

29

Helix

318 – 331

14

Turn

332 – 335

4

Helix

340 – 345

6

Helix

347 – 360

14

Beta strand

375 – 377

3

Beta strand

380 – 382

3

Beta strand

387 – 390

4

Helix

392 – 396

5

Turn

399 – 401

3

Beta strand

402 – 404

3

Helix

410 – 413

4

Helix

432 – 434

3

Helix

439 – 456

18

Beta strand

457 – 460

4

Helix

465 – 467

3

Beta strand

473 – 480

8

Beta strand

486 – 490

5

Sequences

	Sequence		Length	Mass (Da)
	P20813 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: B9799164BE8FBF1D	FASTA	491	56,278
	10 20 30 40 50 60 MELSVLLFLA LLTGLLLLLV QRHPNTHDRL PPGPRPLPLL GNLLQMDRRG LLKSFLRFRE 70 80 90 100 110 120 KYGDVFTVHL GPRPVVMLCG VEAIREALVD KAEAFSGRGK IAMVDPFFRG YGVIFANGNR 130 140 150 160 170 180 WKVLRRFSVT TMRDFGMGKR SVEERIQEEA QCLIEELRKS KGALMDPTFL FQSITANIIC 190 200 210 220 230 240 SIVFGKRFHY QDQEFLKMLN LFYQTFSLIS SVFGQLFELF SGFLKYFPGA HRQVYKNLQE 250 260 270 280 290 300 INAYIGHSVE KHRETLDPSA PKDLIDTYLL HMEKEKSNAH SEFSHQNLNL NTLSLFFAGT 310 320 330 340 350 360 ETTSTTLRYG FLLMLKYPHV AERVYREIEQ VIGPHRPPEL HDRAKMPYTE AVIYEIQRFS 370 380 390 400 410 420 DLLPMGVPHI VTQHTSFRGY IIPKDTEVFL ILSTALHDPH YFEKPDAFNP DHFLDANGAL 430 440 450 460 470 480 KKTEAFIPFS LGKRICLGEG IARAELFLFF TTILQNFSMA SPVAPEDIDL TPQECGVGKI 490 PPTYQIRFLP R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and sequence and cDNA-directed expression of human P450 IIB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver." Yamano S., Nhamburo P.T., Aoyama T., Meyer U.A., Inaba T., Kalow W., Gelboin H.V., McBride O.W., Gonzalez F.J. Biochemistry 28:7340-7348(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Sequence of a new human cytochrome P450-2B6 cDNA." Zhuge J., Qian Y., Xie H., Yu Y. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-167; HIS-172 AND ARG-262. Tissue: Liver.
[3]	NIEHS SNPs program Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-22; SER-26; GLY-28; SER-29; HIS-172; ARG-262; LYS-289; SER-306; THR-328 AND CYS-487.
[4]	"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].
[5]	"Alternative splicing in the human cytochrome P450IIB6 gene generates a high level of aberrant messages." Miles J.S., McLaren A.W., Wolf C.R. Nucleic Acids Res. 17:8241-8255(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-491.
[6]	"Gene expression in distinct regions of the heart." Thum T., Borlak J. Lancet 355:979-983(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"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.
[8]	"Crystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole at 2.0-A resolution." Gay S.C., Shah M.B., Talakad J.C., Maekawa K., Roberts A.G., Wilderman P.R., Sun L., Yang J.Y., Huelga S.C., Hong W.X., Zhang Q., Stout C.D., Halpert J.R. Mol. Pharmacol. 77:529-538(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-491 OF VARIANT ARG-262 IN COMPLEX WITH HEME AND SYNTHETIC INHIBITOR, FUNCTION, COFACTOR, MASS SPECTROMETRY.
[9]	"Structures of cytochrome P450 2B6 bound to 4-benzylpyridine and 4-(4-nitrobenzyl)pyridine: insight into inhibitor binding and rearrangement of active site side chains." Shah M.B., Pascual J., Zhang Q., Stout C.D., Halpert J.R. Mol. Pharmacol. 80:1047-1055(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 30-491 OF VARIANT ARG-262 IN COMPLEX WITH HEME AND SYNTHETIC INHIBITOR, FUNCTION, COFACTOR.
[10]	"Conformational adaptation of human cytochrome P450 2B6 and rabbit cytochrome P450 2B4 revealed upon binding multiple amlodipine molecules." Shah M.B., Wilderman P.R., Pascual J., Zhang Q., Stout C.D., Halpert J.R. Biochemistry 51:7225-7238(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-491 IN COMPLEX WITH HEME AND AMLODIPINE, FUNCTION, COFACTOR.
[11]	"Pharmacogenetics of efavirenz and central nervous system side effects: an Adult AIDS Clinical Trials Group study." Haas D.W., Ribaudo H.J., Kim R.B., Tierney C., Wilkinson G.R., Gulick R.M., Clifford D.B., Hulgan T., Marzolini C., Acosta E.P. AIDS 18:2391-2400(2004) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM, INVOLVEMENT IN EFAVIRENZ POOR METABOLISM, SUSCEPTIBILITY TO EFAVIRENZ TOXICITY.
[12]	"Haplotype structure of CYP2B6 and association with plasma efavirenz concentrations in a Chilean HIV cohort." Carr D.F., la Porte C.J., Pirmohamed M., Owen A., Cortes C.P. J. Antimicrob. Chemother. 65:1889-1893(2010) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM, INVOLVEMENT IN EFAVIRENZ POOR METABOLISM, SUSCEPTIBILITY TO EFAVIRENZ TOXICITY.
[13]	"Influence of host genetic factors on efavirenz plasma and intracellular pharmacokinetics in HIV-1-infected patients." Elens L., Vandercam B., Yombi J.C., Lison D., Wallemacq P., Haufroid V. Pharmacogenomics 11:1223-1234(2010) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM, INVOLVEMENT IN EFAVIRENZ POOR METABOLISM, SUSCEPTIBILITY TO EFAVIRENZ TOXICITY.
[14]	"A single nucleotide polymorphism of CYP2b6 found in Japanese enhances catalytic activity by autoactivation." Ariyoshi N., Miyazaki M., Toide K., Sawamura Y.I., Kamataki T. Biochem. Biophys. Res. Commun. 281:1256-1260(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-172.
[15]	"Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver." Lang T., Klein K., Fischer J., Nussler A.K., Neuhaus P., Hofmann U., Eichelbaum M., Schwab M., Zanger U.M. Pharmacogenetics 11:399-415(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CYS-22; HIS-172; ARG-259; ARG-262 AND CYS-487.
[16]	"Functional characterization of cytochrome P450 2B6 allelic variants." Jinno H., Tanaka-Kagawa T., Ohno A., Makino Y., Matsushima E., Hanioka N., Ando M. Drug Metab. Dispos. 31:398-403(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS CYS-22; HIS-172; ARG-259; ARG-262 AND CYS-487.
[17]	"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 CYS-22; ALA-167; HIS-172 AND CYS-487.
[18]	"Hepatic CYP2B6 expression: gender and ethnic differences and relationship to CYP2B6 genotype and CAR (constitutive androstane receptor) expression." Lamba V., Lamba J., Yasuda K., Strom S., Davila J., Hancock M.L., Fackenthal J.D., Rogan P.K., Ring B., Wrighton S.A., Schuetz E.G. J. Pharmacol. Exp. Ther. 307:906-922(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CYS-22; GLU-139; HIS-172 AND CYS-487.
[19]	"Multiple novel nonsynonymous CYP2B6 gene polymorphisms in Caucasians: demonstration of phenotypic null alleles." Lang T., Klein K., Richter T., Zibat A., Kerb R., Eichelbaum M., Schwab M., Zanger U.M. J. Pharmacol. Exp. Ther. 311:34-43(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-21; VAL-46; GLU-99; GLU-139; GLN-140 AND ASN-391.
[20]	"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 CYS-22; HIS-172; ARG-262; THR-328 AND CYS-487.
+	Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP2B6 alleles

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29874 mRNA. Translation: AAA52144.1.
AF182277 mRNA. Translation: AAF13602.1.
DQ298753 Genomic DNA. Translation: ABB84469.1.
AC023172 Genomic DNA. Translation: AAF32444.1.
X13494 mRNA. No translation available.

IPI

IPI00025829.

PIR

A32969.

RefSeq

NP_000758.1. NM_000767.4.

UniGene

Hs.1360.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IBD	X-ray	2.00	A	30-491	[»]
3QOA	X-ray	2.10	A	30-491	[»]
3QU8	X-ray	2.80	A/B/C/D/E/F	30-491	[»]
3UA5	X-ray	2.80	A/B	30-491	[»]

ProteinModelPortal

P20813.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000324648.

PTM databases

PhosphoSite

P20813.

Polymorphism databases

DMDM

117205.

Proteomic databases

PaxDb

P20813.

PRIDE

P20813.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324071; ENSP00000324648; ENSG00000197408.

GeneID

1555.

KEGG

hsa:1555.

UCSC

uc002opr.1. human.

Organism-specific databases

CTD

1555.

GeneCards

GC19P041497.

HGNC

HGNC:2615. CYP2B6.

HPA

HPA048124.

MIM

123930. gene.
614546. phenotype.

neXtProt

NX_P20813.

Orphanet

240869. Efavirenz toxicity.
240969. Susceptibility to adverse reaction due to efavirenz treatment.

PharmGKB

PA123.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036992.

HOVERGEN

HBG015789.

InParanoid

P20813.

KO

K07412.

OMA

GRGKIAM.

OrthoDB

EOG40K7ZR.

PhylomeDB

P20813.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09587-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P20813.

Gene expression databases

ArrayExpress

P20813.

Bgee

P20813.

CleanEx

HS_CYP2B6.

Genevestigator

P20813.

GermOnline

ENSG00000197408. Homo sapiens.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR01685. EP450ICYP2B.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P20813.

ChEMBL

CHEMBL4729.

DrugBank

DB01156. Bupropion.
DB00241. Butalbital.
DB00564. Carbamazepine.
DB00758. Clopidogrel.
DB00531. Cyclophosphamide.
DB00625. Efavirenz.
DB01181. Ifosfamide.
DB01043. Memantine.
DB00454. Meperidine.
DB00532. Mephenytoin.
DB00333. Methadone.
DB00849. Methylphenobarbital.
DB00683. Midazolam.
DB00220. Nelfinavir.
DB00238. Nevirapine.
DB00184. Nicotine.
DB01173. Orphenadrine.
DB00252. Phenytoin.
DB00818. Propofol.
DB00503. Ritonavir.
DB01037. Selegiline.
DB01104. Sertraline.
DB00208. Ticlopidine.
DB01361. Troleandomycin.

EvolutionaryTrace

P20813.

GenomeRNAi

1555.

NextBio

6423.

SOURCE

Search...

Entry information

Entry name

CP2B6_HUMAN

Accession

Primary (citable) accession number: P20813
Secondary accession number(s): Q2V565, Q9UK46

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.