CYP26B1

From Wikipedia, the free encyclopedia

Cytochrome P450, family 26, subfamily B, polypeptide 1

Identifiers

CYP26B1; CYP26A2; DKFZp686G0638; MGC129613; P450RAI-2

External IDs

OMIM: 605207 MGI: 2176159 HomoloGene: 23179

Gene ontology
Molecular Function:	• monooxygenase activity • iron ion binding • heme binding • metal ion binding
Cellular Component:	• endoplasmic reticulum • microsome • membrane
Biological Process:	• electron transport • proximal/distal pattern formation • embryonic limb morphogenesis • retinoic acid receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_019885 (mRNA)
NP_063938 (protein)

NM_175475 (mRNA)
NP_780684 (protein)

Location

Chr 2: 72.21 - 72.23 Mb

Chr 6: 84.54 - 84.56 Mb

Pubmed search

[1]

[2]

Cytochrome P450, family 26, subfamily B, polypeptide 1, also known as CYP26B1, is a human gene.^[1]

This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases that catalyze many reactions involved in drug metabolism and the synthesis of cholesterol, steroids and other lipids. The enzyme encoded by this gene is involved in the specific inactivation of all-trans-retinoic acid to hydroxylated forms, such as 4-oxo-, 4-OH-, and 18-OH-all-trans-retinoic acid.^[1]

[edit] References

^ ^a ^b Entrez Gene: CYP26B1 cytochrome P450, family 26, subfamily B, polypeptide 1.

[edit] Further reading

Rat E, Billaut-Laden I, Allorge D, et al. (2006). "Evidence for a functional genetic polymorphism of the human retinoic acid-metabolizing enzyme CYP26A1, an enzyme that may be involved in spina bifida.". Birth Defects Res. Part A Clin. Mol. Teratol. 76 (6): 491-8. doi:10.1002/bdra.20275. PMID 16933217.
Bowles J, Knight D, Smith C, et al. (2006). "Retinoid signaling determines germ cell fate in mice.". Science 312 (5773): 596-600. doi:10.1126/science.1125691. PMID 16574820.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724-31. doi:10.1038/nature03466. PMID 15815621.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Trofimova-Griffin ME, Juchau MR (2002). "Developmental expression of cytochrome CYP26B1 (P450RAI-2) in human cephalic tissues.". Brain Res. Dev. Brain Res. 136 (2): 175-8. PMID 12101034.
Abu-Abed S, MacLean G, Fraulob V, et al. (2002). "Differential expression of the retinoic acid-metabolizing enzymes CYP26A1 and CYP26B1 during murine organogenesis.". Mech. Dev. 110 (1-2): 173-7. PMID 11744378.
White JA, Ramshaw H, Taimi M, et al. (2000). "Identification of the human cytochrome P450, P450RAI-2, which is predominantly expressed in the adult cerebellum and is responsible for all-trans-retinoic acid metabolism.". Proc. Natl. Acad. Sci. U.S.A. 97 (12): 6403-8. doi:10.1073/pnas.120161397. PMID 10823918.
Nelson DR (1999). "A second CYP26 P450 in humans and zebrafish: CYP26B1.". Arch. Biochem. Biophys. 371 (2): 345-7. doi:10.1006/abbi.1999.1438. PMID 10545224.