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.
basic-leucine zipper transcription factor MafK; Erythroid transcription factor NF-E2 p18 subunit; FLJ32205; MGC71717; nuclear factor erythroid-2, ubiquitous (p18); Transcription factor MafK; v-maf avian musculoaponeurotic fibrosarcoma oncogene family, protein K; v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog K; v-maf musculoaponeurotic fibrosarcoma oncogene homolog K
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