MAFF (gene)

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V-maf musculoaponeurotic fibrosarcoma oncogene homolog F (avian)
Identifiers
Symbol(s) MAFF; U-MAF
External IDs OMIM: 604877 MGI: 96910 Homologene: 7825
RNA expression pattern

Image:PBB GE MAFF 36711 at tn.png

Image:PBB GE MAFF 205193 at tn.png

More reference expression data

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)
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 (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.[1]


See also

References

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


Template:Gene-22-stub This article incorporates text from the United States National Library of Medicine, which is in the public domain.

v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP) Activating transcription factor (1, 2, 3, 4, 5, 6) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3) • GABPA • MAF (B, F, G, K) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH) ATOH1 • AhR • AHRR • ARNT • ASCL1 • BMAL (ARNTL, ARNTL2) • CLOCK • HIF (1A, 3A) • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • NEUROD1 • Twist • USF1
(1.3) bHLH-ZIP Myc • MITF • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH) AP-2
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4) subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4 GATA (1, 2, 3, 4, 5, 6)
(2.3) Cys2His2 General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIH: 1, 2) • GLI-Krüppel family (1, 2, 3, YY1) • KLF (2, 4, 5, 6, 10, 11, 12, 13) • Sp1 • zinc finger (3, 35, 43, 146, 148, 165, 217, 268, 281, 350) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6 HIVEP1
(3) Helix-turn-helix
domains
(3.1) Homeo domain ARX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C6, C8, C9, C13, D1, D3, D4, D9, D10, D11, D12, D13) • NANOG • NKX (2-1, 2-5, 3-1) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7)
(3.2) Paired box PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
(3.3) Fork head / winged helix E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, L2, M1, N3, O3, O4, P1, P2, P3)
(3.4) Heat Shock Factors HSF1
(3.5) Tryptophan clusters ELF (4, 5) • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB
(3.6) TEA domain transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (5, C1, C2, C3, C4)
(4.2) STAT STAT (1, 2, 3, 4, 5, 6)
(4.3) p53 p53
(4.4) MADS box Mef2 (A, B, C, D) • SRF
(4.7) High mobility group HNF (1A, 1B) • LEF1 • SOX (3, 4, 6, 9, 10, 13, 18) • SRY • SSRP1
(4.10) Cold-shock domain CSDA
(0) Other
transcription factors
(0.2) HMGI(Y) HMGA (1, 2)
(0.3) Pocket domain Rb • RBL1 • RBL2
(0.6) Miscellaneous ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • Rho/Sigma • R-SMAD

Acknowledgement and Attribution Regarding Sources of Content

Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

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