Recombinant Mouse Transcription factor AP-1 (Jun)

Function

Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:14707112). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (PubMed:2498083). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 (By similarity). Binds to the USP28 promoter (By similarity)

Subcellular Location

Nucleus

Subunit

Heterodimer with either BATF3 or ATF7 (By similarity). Heterodimer with FOS (PubMed:29272704). Heterodimer with FOSB isoform 1 and 2 (PubMed:29272704). Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (PubMed:2498083). As part of the AP-1 transcription factor complex, forms heterodimers with FOSB, thereby binding to the AP-1 consensus sequence and stimulating transcription (PubMed:2498083). The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with SP1, SPIB and TCF20. Interacts with COPS5; the interaction leads indirectly to its phosphorylation. Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS heterodimer to activate transcription in response to TGF-beta (By similarity). Interacts (via its basic DNA binding and leucine zipper domains) with SMAD3 (via an N-terminal domain); the interaction is required for TGF-beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex (By similarity). Interacts with TSC22D3 (via N-terminus); the interaction inhibits the binding of active AP1 to its target DNA (PubMed:11397794). Interacts with HIVEP3 and MYBBP1A (PubMed:14707112, PubMed:9447996). Interacts with methylated RNF187 (PubMed:20852630). Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (By similarity). Interacts with PRR7 (PubMed:27458189). Found in a complex with PRR7 and FBXW7 (By similarity). Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (By similarity). Interacts with RBM39 (PubMed:11704680). Interacts with PAGE4 (By similarity). Interacts with FOSL1 and FOSL2 (PubMed:29272704). Interacts with ARK2N and CSNK2B; the interaction with ARK2N is mediated by CSNK2B (By similarity)

• Ryseck R.-P. et al. Transcriptional activation of c-jun during the G0/G1 transition in mouse fibroblasts. — Nature (1988)
• Lamph W.W. et al. Induction of proto-oncogene JUN/AP-1 by serum and TPA. — Nature (1988)
• Ryder K. et al. Induction of protooncogene c-jun by serum growth factors. — Proc. Natl. Acad. Sci. U.S.A. (1988)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Zerial M. et al. The product of a novel growth factor activated gene, fos B, interacts with JUN proteins enhancing their DNA binding activity. — EMBO J. (1989)
• Tavner F.J. et al. Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb. — Mol. Cell. Biol. (1998)
• Mittelstadt P.R. et al. Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ. — J. Biol. Chem. (2001)
• Jung D.-J. et al. Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors. — J. Biol. Chem. (2002)