MAFF (gene)
From Wikipedia, the free encyclopedia
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V-maf musculoaponeurotic fibrosarcoma oncogene homolog F (avian)
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| Identifiers | ||||||||||||||
| Symbol(s) | MAFF; U-MAF | |||||||||||||
| External IDs | OMIM: 604877 MGI: 96910 HomoloGene: 7825 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 23764 | 17133 | ||||||||||||
| Ensembl | ENSG00000185022 | ENSMUSG00000042622 | ||||||||||||
| Uniprot | Q9ULX9 | Q3U0G5 | ||||||||||||
| Refseq | NM_012323 (mRNA) NP_036455 (protein) |
NM_010755 (mRNA) NP_034885 (protein) |
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| Location | Chr 22: 36.93 - 36.94 Mb | Chr 15: 79.17 - 79.19 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
V-maf musculoaponeurotic fibrosarcoma oncogene homolog F (avian), also known as MAFF, is a human gene.[1]
The protein encoded by this gene is a basic leucine zipper (bZIP) transcription factor that lacks a transactivation domain. It is known to bind the US-2 DNA element in the promoter of the oxytocin receptor gene and most likely heterodimerizes with other leucine zipper-containing proteins to enhance expression of the OTR gene during term pregnancy. The encoded protein can also form homodimers, and since it lacks a transactivation domain, the homodimer may act as a repressor of transcription. This gene may also be involved in the cellular stress response. Two transcript variants encoding the same protein have been found for this gene.[1]
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[edit] See also
[edit] References
[edit] Further reading
- Ye X, Li Y, Huang Q, et al. (2006). "The novel human gene MIP functions as a co-activator of hMafF.". Arch. Biochem. Biophys. 449 (1-2): 87–93. doi:. PMID 16549056.
- Massrieh W, Derjuga A, Doualla-Bell F, et al. (2006). "Regulation of the MAFF transcription factor by proinflammatory cytokines in myometrial cells.". Biol. Reprod. 74 (4): 699–705. doi:. PMID 16371591.
- 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:. PMID 15489334.
- 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:. PMID 14702039.
- Marini MG, Asunis I, Chan K, et al. (2003). "Cloning MafF by recognition site screening with the NFE2 tandem repeat of HS2: analysis of its role in globin and GCSl genes regulation.". Blood Cells Mol. Dis. 29 (2): 145–58. PMID 12490281.
- 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:. PMID 12477932.
- Moran JA, Dahl EL, Mulcahy RT (2002). "Differential induction of mafF, mafG and mafK expression by electrophile-response-element activators.". Biochem. J. 361 (Pt 2): 371–7. PMID 11772409.
- Kataoka K, Yoshitomo-Nakagawa K, Shioda S, Nishizawa M (2001). "A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA binding, transactivation, and transforming activities.". J. Biol. Chem. 276 (1): 819–26. doi:. PMID 11036080.
- Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:. PMID 10591208.
- Kimura T, Ivell R, Rust W, et al. (1999). "Molecular cloning of a human MafF homologue, which specifically binds to the oxytocin receptor gene in term myometrium.". Biochem. Biophys. Res. Commun. 264 (1): 86–92. doi:. PMID 10527846.
- Johnsen O, Skammelsrud N, Luna L, et al. (1996). "Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1.". Nucleic Acids Res. 24 (21): 4289–97. PMID 8932385.
- Igarashi K, Kataoka K, Itoh K, et al. (1994). "Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins.". Nature 367 (6463): 568–72. doi:. PMID 8107826.
[edit] External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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