MAFF (gene)
| V-maf avian musculoaponeurotic fibrosarcoma oncogene homolog F | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | MAFF ; U-MAF; hMafF | ||||||||||||
| External IDs | OMIM: 604877 MGI: 96910 HomoloGene: 7825 GeneCards: MAFF Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 23764 | 17133 | |||||||||||
| Ensembl | ENSG00000185022 | ENSMUSG00000042622 | |||||||||||
| UniProt | Q9ULX9 | O54791 | |||||||||||
| RefSeq (mRNA) | NM_001161572 | NM_010755 | |||||||||||
| RefSeq (protein) | NP_001155044 | NP_034885 | |||||||||||
| Location (UCSC) | Chr 22: 38.6 – 38.61 Mb | Chr 15: 79.35 – 79.36 Mb | |||||||||||
| PubMed search | |||||||||||||
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 (OTR) 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
References
- ↑ 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.
- ↑ 2.0 2.1 "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/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. PMC 528928. 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. PMC 139241. 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. PMC 1222317. 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. PMC 146217. 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
- MAFF protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- FactorBook MafF
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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