Domain:The basic domain functions as a nuclear localization signal.,Domain:The basic leucine-zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE.,Function:Transcriptional factor that acts in the unfolded protein response (UPR) pathway by activating UPR target genes induced during ER stress. Binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is bound to ERSE.,PTM:During unfolded protein response an approximative 60 kDa fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage is probably performed sequentially by site-1 and site-2 proteases.,PTM:N-glycosylated.,similarity:Belongs to the bZIP family.,similarity:Belongs to the bZIP family. ATF subfamily.,similarity:Contains 1 bZIP domain.,subcellular location:Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.,subunit:Homodimer and heterodimer with ATF6-alpha. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC).,tissue specificity:Ubiquitous.,
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