1k1v

Structural highlights

Function

[MAFG_MOUSE] Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NF-E2. Activates globin gene expression when associated with NF-E2. May be involved in signal transduction of extracellular H(+) (By similarity).^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Shavit JA, Motohashi H, Onodera K, Akasaka J, Yamamoto M, Engel JD. Impaired megakaryopoiesis and behavioral defects in mafG-null mutant mice. Genes Dev. 1998 Jul 15;12(14):2164-74. PMID:9679061
2. ↑ Motohashi H, Katsuoka F, Miyoshi C, Uchimura Y, Saitoh H, Francastel C, Engel JD, Yamamoto M. MafG sumoylation is required for active transcriptional repression. Mol Cell Biol. 2006 Jun;26(12):4652-63. PMID:16738329 doi:http://dx.doi.org/10.1128/MCB.02193-05
3. ↑ Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T. Solution structure of the DNA-binding domain of MafG. Nat Struct Biol. 2002 Apr;9(4):252-6. PMID:11875518 doi:10.1038/nsb771