Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P20813 (CP2B6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence 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 Ref.8 Ref.9 Ref.10

Catalytic activity

1,4-cineole + NADPH + O2 = 2-exo-hydroxy-1,4-cineole + NADP+ + H2O. Ref.7

Cofactor

Heme group. Ref.8 Ref.9 Ref.10

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 componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular ketone metabolic process

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

drug metabolic process

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

exogenous drug catabolic process

Inferred from direct assay PubMed 19029318. Source: BHF-UCL

oxidation-reduction process

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid metabolic process

Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL

xenobiotic metabolic process

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

   Molecular_functionheme binding

Inferred from direct assay Ref.8. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Cytochrome P450 2B6
PRO_0000051683

Sites

Metal binding4361Iron (heme axial ligand)

Amino acid modifications

Modified residue1281Phosphoserine; by PKA By similarity

Natural variations

Natural variant211Q → L in allele CYP2B6*10. Ref.19
Corresponds to variant rs34883432 [ dbSNP | Ensembl ].
VAR_023563
Natural variant221R → 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 variant261T → S. Ref.3
Corresponds to variant rs33973337 [ dbSNP | Ensembl ].
VAR_025206
Natural variant281D → G. Ref.3
Corresponds to variant rs33980385 [ dbSNP | Ensembl ].
VAR_025207
Natural variant291R → P.
Corresponds to variant rs34284776 [ dbSNP | Ensembl ].
VAR_033819
Natural variant291R → S. Ref.3
Corresponds to variant rs33926104 [ dbSNP | Ensembl ].
VAR_025208
Natural variant461M → V in allele CYP2B6*11. Ref.19
Corresponds to variant rs35303484 [ dbSNP | Ensembl ].
VAR_023564
Natural variant991G → E in allele CYP2B6*12. Ref.19
Corresponds to variant rs36060847 [ dbSNP | Ensembl ].
VAR_023565
Natural variant1391K → E in allele CYP2B6*8 and allele CYP2B6*13. Ref.18 Ref.19
Corresponds to variant rs12721655 [ dbSNP | Ensembl ].
VAR_016948
Natural variant1401R → Q in allele CYP2B6*14. Ref.19
Corresponds to variant rs35773040 [ dbSNP | Ensembl ].
VAR_023566
Natural variant1671P → A. Ref.2 Ref.17
Corresponds to variant rs3826711 [ dbSNP | Ensembl ].
VAR_016924
Natural variant1721Q → 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 variant2591S → R in allele CYP2B6*3. Ref.15 Ref.16
Corresponds to variant rs45482602 [ dbSNP | Ensembl ].
VAR_016928
Natural variant2621K → R in allele CYP2B6*4, allele CYP2B6*6, allele CYP2B6*7 and allele CYP2B6*13; slight decrease in activity. Ref.2 Ref.3 Ref.8 Ref.9 Ref.15 Ref.16 Ref.20
Corresponds to variant rs2279343 [ dbSNP | Ensembl ].
VAR_016926
Natural variant2891N → K. Ref.3
Corresponds to variant rs34277950 [ dbSNP | Ensembl ].
VAR_025209
Natural variant3061T → S. Ref.3
Corresponds to variant rs34698757 [ dbSNP | Ensembl ].
VAR_025210
Natural variant3281I → T. Ref.3 Ref.20
Corresponds to variant rs28399499 [ dbSNP | Ensembl ].
VAR_024716
Natural variant3911I → N in allele CYP2B6*15. Ref.19
Corresponds to variant rs35979566 [ dbSNP | Ensembl ].
VAR_023567
Natural variant4871R → 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 conflict1461I → T in AAF13602. Ref.2
Sequence conflict2381L → P in AAF13602. Ref.2

Secondary structure

........................................................................ 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20813 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: B9799164BE8FBF1D

FASTA49156,278
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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.

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.
CCDSCCDS12570.1.
PIRA32969.
RefSeqNP_000758.1. NM_000767.4.
UniGeneHs.1360.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IBDX-ray2.00A30-491[»]
3QOAX-ray2.10A27-491[»]
3QU8X-ray2.80A/B/C/D/E/F27-491[»]
3UA5X-ray2.80A/B27-491[»]
4I91X-ray2.00A27-491[»]
ProteinModelPortalP20813.
SMRP20813. Positions 42-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107933. 1 interaction.
STRING9606.ENSP00000324648.

Chemistry

BindingDBP20813.
ChEMBLCHEMBL4729.
DrugBankDB01156. 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.

PTM databases

PhosphoSiteP20813.

Polymorphism databases

DMDM117205.

Proteomic databases

PaxDbP20813.
PRIDEP20813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324071; ENSP00000324648; ENSG00000197408.
GeneID1555.
KEGGhsa:1555.
UCSCuc002opr.1. human.

Organism-specific databases

CTD1555.
GeneCardsGC19P041497.
HGNCHGNC:2615. CYP2B6.
HPACAB033866.
HPA048124.
MIM123930. gene.
614546. phenotype.
neXtProtNX_P20813.
Orphanet240869. Efavirenz toxicity.
240969. Susceptibility to adverse reaction due to efavirenz treatment.
PharmGKBPA123.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036992.
HOVERGENHBG015789.
InParanoidP20813.
KOK17709.
OMAYREIEQV.
OrthoDBEOG7RBZ85.
PhylomeDBP20813.
TreeFamTF352043.

Enzyme and pathway databases

BioCycMetaCyc:HS09587-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP20813.

Gene expression databases

ArrayExpressP20813.
BgeeP20813.
CleanExHS_CYP2B6.
GenevestigatorP20813.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01685. EP450ICYP2B.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20813.
GeneWikiCYP2B6.
GenomeRNAi1555.
NextBio6423.
PROP20813.
SOURCESearch...

Entry information

Entry nameCP2B6_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM