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{{Cytochrome P450}}
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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{protein
{{PBB_Controls
⚫
| Name = cytochrome P450, family 1, subfamily B, polypeptide 1
| caption =
| update_page = yes
| require_manual_inspection = no
| image =
| update_protein_box = yes
| width =
| HGNCid = 2597
| update_summary = no
| update_citations = yes
| Symbol = CYP1B1
}}
⚫
| AltSymbols =

| EntrezGene = 1545
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
⚫
| OMIM = 601771
{{GNF_Protein_box
⚫
| RefSeq = NM_000104
| UniProt = Q16678
| image =
| PDB =
| image_source =
| ECnumber =
| PDB =
⚫
| Name = Cytochrome P450, family 1, subfamily B, polypeptide 1
| Chromosome = 2
| Arm = p
| HGNCid = 2597
| Band = 21
| Symbol = CYP1B1
⚫
| AltSymbols =; CP1B; GLC3A
| LocusSupplementaryData =
⚫
| OMIM = 601771
| ECnumber =
| Homologene = 68035
| MGIid = 88590
| GeneAtlas_image1 = PBB_GE_CYP1B1_202437_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYP1B1_202434_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CYP1B1_202435_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1545
| Hs_Ensembl = ENSG00000138061
| Hs_RefseqProtein = NP_000095
⚫
| Hs_RefseqmRNA = NM_000104
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 38148154
| Hs_GenLoc_end = 38156796
| Hs_Uniprot = Q16678
| Mm_EntrezGene = 13078
| Mm_Ensembl = ENSMUSG00000024087
| Mm_RefseqmRNA = NM_009994
| Mm_RefseqProtein = NP_034124
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 79615279
| Mm_GenLoc_end = 79623367
| Mm_Uniprot = Q3UTK2
}}
}}
}}
CYP1B1 belongs to the [[cytochrome P450 ]] superfamily of enzymes.
CYP1B1 belongs to the [[cytochrome P450 ]] superfamily of enzymes.
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* {{MeshName|cytochrome+P-450+CYP1B1}}
* {{MeshName|cytochrome+P-450+CYP1B1}}
* {{MeshName|CYP1B1+protein,+human}}
* {{MeshName|CYP1B1+protein,+human}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Sasaki M, Kaneuchi M, Fujimoto S, ''et al.'' |title=CYP1B1 gene in endometrial cancer. |journal=Mol. Cell. Endocrinol. |volume=202 |issue= 1-2 |pages= 171-6 |year= 2004 |pmid= 12770747 |doi= }}
*{{cite journal | author=Nelson DR, Zeldin DC, Hoffman SM, ''et al.'' |title=Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. |journal=Pharmacogenetics |volume=14 |issue= 1 |pages= 1-18 |year= 2004 |pmid= 15128046 |doi= }}
*{{cite journal | author=Paracchini V, Raimondi S, Gram IT, ''et al.'' |title=Meta- and pooled analyses of the cytochrome P-450 1B1 Val432Leu polymorphism and breast cancer: a HuGE-GSEC review. |journal=Am. J. Epidemiol. |volume=165 |issue= 2 |pages= 115-25 |year= 2007 |pmid= 17053044 |doi= 10.1093/aje/kwj365 }}
*{{cite journal | author=Coca-Prados M, Escribano J |title=New perspectives in aqueous humor secretion and in glaucoma: the ciliary body as a multifunctional neuroendocrine gland. |journal=Progress in retinal and eye research |volume=26 |issue= 3 |pages= 239-62 |year= 2007 |pmid= 17321191 |doi= 10.1016/j.preteyeres.2007.01.002 }}
*{{cite journal | author=Sutter TR, Guzman K, Dold KM, Greenlee WF |title=Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta. |journal=Science |volume=254 |issue= 5030 |pages= 415-8 |year= 1991 |pmid= 1925598 |doi= }}
*{{cite journal | author=Sutter TR, Tang YM, Hayes CL, ''et al.'' |title=Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. |journal=J. Biol. Chem. |volume=269 |issue= 18 |pages= 13092-9 |year= 1994 |pmid= 8175734 |doi= }}
*{{cite journal | author=Tang YM, Wo YY, Stewart J, ''et al.'' |title=Isolation and characterization of the human cytochrome P450 CYP1B1 gene. |journal=J. Biol. Chem. |volume=271 |issue= 45 |pages= 28324-30 |year= 1996 |pmid= 8910454 |doi= }}
*{{cite journal | author=Stoilov I, Akarsu AN, Sarfarazi M |title=Identification of three different truncating mutations in cytochrome P4501B1 (CYP1B1) as the principal cause of primary congenital glaucoma (Buphthalmos) in families linked to the GLC3A locus on chromosome 2p21. |journal=Hum. Mol. Genet. |volume=6 |issue= 4 |pages= 641-7 |year= 1997 |pmid= 9097971 |doi= }}
*{{cite journal | author=Bejjani BA, Lewis RA, Tomey KF, ''et al.'' |title=Mutations in CYP1B1, the gene for cytochrome P4501B1, are the predominant cause of primary congenital glaucoma in Saudi Arabia. |journal=Am. J. Hum. Genet. |volume=62 |issue= 2 |pages= 325-33 |year= 1998 |pmid= 9463332 |doi= }}
*{{cite journal | author=Stoilov I, Akarsu AN, Alozie I, ''et al.'' |title=Sequence analysis and homology modeling suggest that primary congenital glaucoma on 2p21 results from mutations disrupting either the hinge region or the conserved core structures of cytochrome P4501B1. |journal=Am. J. Hum. Genet. |volume=62 |issue= 3 |pages= 573-84 |year= 1998 |pmid= 9497261 |doi= }}
*{{cite journal | author=Bailey LR, Roodi N, Dupont WD, Parl FF |title=Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid receptor status in breast cancer. |journal=Cancer Res. |volume=58 |issue= 22 |pages= 5038-41 |year= 1998 |pmid= 9823305 |doi= }}
*{{cite journal | author=Plásilová M, Stoilov I, Sarfarazi M, ''et al.'' |title=Identification of a single ancestral CYP1B1 mutation in Slovak Gypsies (Roms) affected with primary congenital glaucoma. |journal=J. Med. Genet. |volume=36 |issue= 4 |pages= 290-4 |year= 1999 |pmid= 10227395 |doi= }}
*{{cite journal | author=Lewis DF, Lake BG, George SG, ''et al.'' |title=Molecular modelling of CYP1 family enzymes CYP1A1, CYP1A2, CYP1A6 and CYP1B1 based on sequence homology with CYP102. |journal=Toxicology |volume=139 |issue= 1-2 |pages= 53-79 |year= 2000 |pmid= 10614688 |doi= }}
*{{cite journal | author=Vincent A, Billingsley G, Priston M, ''et al.'' |title=Phenotypic heterogeneity of CYP1B1: mutations in a patient with Peters' anomaly. |journal=J. Med. Genet. |volume=38 |issue= 5 |pages= 324-6 |year= 2001 |pmid= 11403040 |doi= }}
*{{cite journal | author=Bofinger DP, Feng L, Chi LH, ''et al.'' |title=Effect of TCDD exposure on CYP1A1 and CYP1B1 expression in explant cultures of human endometrium. |journal=Toxicol. Sci. |volume=62 |issue= 2 |pages= 299-314 |year= 2001 |pmid= 11452143 |doi= }}
*{{cite journal | author=Michels-Rautenstrauss KG, Mardin CY, Zenker M, ''et al.'' |title=Primary congenital glaucoma: three case reports on novel mutations and combinations of mutations in the GLC3A (CYP1B1) gene. |journal=J. Glaucoma |volume=10 |issue= 4 |pages= 354-7 |year= 2002 |pmid= 11558822 |doi= }}
*{{cite journal | author=Lai J, Vesprini D, Chu W, ''et al.'' |title=CYP gene polymorphisms and early menarche. |journal=Mol. Genet. Metab. |volume=74 |issue= 4 |pages= 449-57 |year= 2002 |pmid= 11749050 |doi= 10.1006/mgme.2001.3260 }}
*{{cite journal | author=Vincent AL, Billingsley G, Buys Y, ''et al.'' |title=Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene. |journal=Am. J. Hum. Genet. |volume=70 |issue= 2 |pages= 448-60 |year= 2002 |pmid= 11774072 |doi= }}
}}
{{refend}}


{{enzyme-stub}}
{{enzyme-stub}}

Revision as of 18:35, 16 December 2007

Template:PBB Controls

CYP1B1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCYP1B1, CP1B, CYPIB1, GLC3A, P4501B1, cytochrome P450 family 1 subfamily B member 1, ASGD6
External IDsOMIM: 601771; MGI: 88590; HomoloGene: 68035; GeneCards: CYP1B1; OMA:CYP1B1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

1545

13078

Ensembl

ENSG00000138061

ENSMUSG00000024087

UniProt

Q16678

Q64429

RefSeq (mRNA)

NM_000104

NM_009994
NM_001364889

RefSeq (protein)

NP_000095

NP_034124
NP_001351818

Location (UCSC)Chr 2: 38.07 – 38.11 MbChr 17: 80.01 – 80.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CYP1B1 belongs to the cytochrome P450 superfamily of enzymes.

Despite over 20 years of research of CYP1A1 and CYP1A2, CYP1B1 was not identified and sequenced until 1994. Nucleic and amino acid analysis showed approximately 40% identity with CYP1A1. Despite this similarity, these two enzymes have very different catalytic efficiencies and metabolites when incubated with common substrates, such as retinoic acid and arachidonic acid. Recently CYP1B1 has been shown to be physiologically important in fetal development, since mutations in CYP1B1 are linked with a form of primary congenital glaucoma.

CYP1A1 and CYP1B1 are regulated by the Aryl hydrocarbon receptor, a ligand activated transcription factor. They are part of the Phase I reactions in drug metabolism.

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138061 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024087 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

Further reading

Template:PBB Further reading

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