7x5f

Structural highlights

Function

MAFG_HUMAN Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:11154691). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding sites (PubMed:8932385, PubMed:9421508, PubMed:11154691). Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NFE2L2 transcription factor (PubMed:11154691). Transcription factor, component of erythroid-specific transcription factor NFE2L2 (PubMed:11154691). Activates globin gene expression when associated with NFE2L2 (PubMed:11154691). May be involved in signal transduction of extracellular H(+) (By similarity).[UniProtKB:Q76MX4]^{[1] [2] [3]}

References

1. ↑ Hung HL, Kim AY, Hong W, Rakowski C, Blobel GA. Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation. J Biol Chem. 2001 Apr 6;276(14):10715-21. Epub 2001 Jan 11. PMID:11154691 doi:10.1074/jbc.M007846200
2. ↑ Johnsen O, Skammelsrud N, Luna L, Nishizawa M, Prydz H, Kolsto AB. Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1. Nucleic Acids Res. 1996 Nov 1;24(21):4289-97. doi: 10.1093/nar/24.21.4289. PMID:8932385 doi:http://dx.doi.org/10.1093/nar/24.21.4289
3. ↑ Johnsen O, Murphy P, Prydz H, Kolsto AB. Interaction of the CNC-bZIP factor TCF11/LCR-F1/Nrf1 with MafG: binding-site selection and regulation of transcription. Nucleic Acids Res. 1998 Jan 15;26(2):512-20. doi: 10.1093/nar/26.2.512. PMID:9421508 doi:http://dx.doi.org/10.1093/nar/26.2.512