proto-oncogene protein c-Fos; cellular oncogene protein fos; G0/G1 switch regulatory protein 7 (FOS, G0S7)

^[1]^[2]^[3]^[4]^[5]^[6]

Function

nuclear phosphoprotein
heterodimer with JUN
forms a tight but non-covalent complex with JUN, the AP-1 transcription factor
in the AP-1 heterodimer, c-fos & JUN basic regions each seem to interact with symmetrical DNA half sites
regulates development of cells destined to form & maintain the skeleton
role in signal transduction, cell proliferation & differentiation
interacts with DSIPI; interaction inhibits the binding of active AP1 to its target DNA
interacts with MAFB (putative)
basic amino acids flanking Cys-154 probably stablilize the anionic form of Cys; oxidation of Cys-154, presumably to sulfenic (RSOH) or sulfinic (RSO2H) acid or disulfide, may inactivate DNA-binding capacity

C-fos expression increases upon a variety of stimuli, including growth factors, cytokines, neurotransmitters, polypeptide hormones, stress & cell injury

↑ Kouzarides T, Ziff E. The role of the leucine zipper in the fos-jun interaction. Nature. 1988 Dec 15;336(6200):646-51. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2974122
↑ Dwarki VJ, Montminy M, Verma IM. Both the basic region and the 'leucine zipper' domain of the cyclic AMP response element binding (CREB) protein are essential for transcriptional activation. EMBO J. 1990 Jan;9(1):225-32. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2136830
↑ Abate C, Patel L, Rauscher FJ 3rd, Curran T. Redox regulation of fos and jun DNA-binding activity in vitro. Science. 1990 Sep 7;249(4973):1157-61. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2118682
↑ Rogers S et al, Amino acids common to rapidly degraded proteins: The PEST hypothesis Science 234:364 1986 (1/2life) PMID: https://www.ncbi.nlm.nih.gov/pubmed/2876518
↑ UniProt http://www.uniprot.org/uniprot/P01100.html
↑ NIEHS-SNPs http://egp.gs.washington.edu/data/fos/