MAFF_(gene)

Gene ontology

Molecular function:

• transcription factor activity
• sequence-specific DNA binding
• protein dimerization activity

Cellular component:

Biological process:

• in utero embryonic development
• transcription
• regulation of transcription, DNA-dependent
• transcription from RNA polymerase II promoter
• parturition
• regulation of epidermal cell differentiation

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

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:10.1016/j.abb.2006.02.011. 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:10.1095/biolreprod.105.045450. 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:10.1101/gr.2596504. 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:10.1038/ng1285. 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:10.1073/pnas.242603899. 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:10.1074/jbc.M007643200. PMID 11036080.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. 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:10.1006/bbrc.1999.1487. 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:10.1038/367568a0. PMID 8107826.

External links

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Contents

See also

References

Further reading

External links