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MAFF (gene): Wikis


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V-maf musculoaponeurotic fibrosarcoma oncogene homolog F (avian)
Symbols MAFF; U-MAF
External IDs OMIM604877 MGI96910 HomoloGene7825 GeneCards: MAFF Gene
RNA expression pattern
PBB GE MAFF 36711 at tn.png
PBB GE MAFF 205193 at tn.png
More reference expression data
Species Human Mouse
Entrez 23764 17133
Ensembl ENSG00000185022 ENSMUSG00000042622
UniProt Q9ULX9 Q3U0G5
RefSeq (mRNA) NM_012323 NM_010755
RefSeq (protein) NP_036455 NP_034885
Location (UCSC) Chr 22:
36.93 - 36.94 Mb
Chr 15:
79.17 - 79.19 Mb
PubMed search [1] [2]

Transcription factor MafF is a protein that in humans is encoded by the MAFF gene.[1][2]

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.[2]


See also


  1. ^ Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al. (Dec 1999). "The DNA sequence of human chromosome 22". Nature 402 (6761): 489-95. doi:10.1038/990031. PMID 10591208. 
  2. ^ a b "Entrez Gene: MAFF v-maf musculoaponeurotic fibrosarcoma oncogene homolog F (avian)". 

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/ 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. doi:10.1006/bcmd.2002.0550. 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. doi:10.1042/0264-6021:3610371. 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. 
  • 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. doi:10.1093/nar/24.21.4289. 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

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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