CYP2S1

From Wikipedia, the free encyclopedia

Cytochrome P450, family 2, subfamily S, polypeptide 1

Identifiers

External IDs

MGI: 1921384 HomoloGene: 75274

Gene ontology
Molecular Function:	• iron ion binding • heme binding • metal ion binding • unspecific monooxygenase activity
Cellular Component:	• endoplasmic reticulum • microsome • membrane
Biological Process:	• electron transport

Orthologs

Human

Mouse

Refseq

NM_030622 (mRNA)
NP_085125 (protein)

NM_028775 (mRNA)
NP_083051 (protein)

Location

Chr 19: 46.39 - 46.41 Mb

Chr 7: 25.51 - 25.53 Mb

Pubmed search

[1]

[2]

Cytochrome P450, family 2, subfamily S, polypeptide 1, also known as CYP2S1, is a human gene.^[1]

This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. In rodents, the homologous protein has been shown to metabolize certain carcinogens; however, the specific function of the human protein has not been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1.

[edit] Further reading

Adams MD, Kerlavage AR, Fleischmann RD, et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence.". Nature 377 (6547 Suppl): 3–174. PMID 7566098.
Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M (2001). "Identification and tissue distribution of the novel human cytochrome P450 2S1 (CYP2S1).". Biochem. Biophys. Res. Commun. 281 (2): 529–35. doi:10.1006/bbrc.2001.4390. PMID 11181079.
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.
Smith G, Wolf CR, Deeni YY, et al. (2003). "Cutaneous expression of cytochrome P450 CYP2S1: individuality in regulation by therapeutic agents for psoriasis and other skin diseases.". Lancet 361 (9366): 1336–43. PMID 12711469.
Saito S, Iida A, Sekine A, et al. (2003). "Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population.". J. Hum. Genet. 48 (5): 249–70. doi:10.1007/s10038-003-0021-7. PMID 12721789.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Rivera SP, Wang F, Saarikoski ST, et al. (2007). "A novel promoter element containing multiple overlapping xenobiotic and hypoxia response elements mediates induction of cytochrome P4502S1 by both dioxin and hypoxia.". J. Biol. Chem. 282 (15): 10881–93. doi:10.1074/jbc.M609617200. PMID 17277313.
Marek CJ, Tucker SJ, Koruth M, et al. (2007). "Expression of CYP2S1 in human hepatic stellate cells.". FEBS Lett. 581 (4): 781–6. doi:10.1016/j.febslet.2007.01.056. PMID 17280660.
Hanzawa Y, Sasaki T, Hiratsuka M, et al. (2007). "Three novel single nucleotide polymorphisms (SNPs) of CYP2S1 gene in Japanese individuals.". Drug Metab. Pharmacokinet. 22 (2): 136–40. PMID 17495422.
Jang YJ, Cha EY, Kim WY, et al. (2007). "CYP2S1 gene polymorphisms in a Korean population.". Therapeutic drug monitoring 29 (3): 292–8. doi:10.1097/FTD.0b013e318058a4e0. PMID 17529885.