[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(83)90306-9; PubMed=6301687 [NCBI, ExPASy, EBI, Israel, Japan]
van Beveren C.,
van Straaten F.,
Curran T.,
Mueller R.,
Verma I.M.;
"Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that viral and cellular fos gene products have different carboxy termini.";
Cell 32:1241-1255(1983).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1073/pnas.82.15.4987; PubMed=2991903 [NCBI, ExPASy, EBI, Israel, Japan]
Meijlink F.,
Curran T.,
Miller A.D.,
Verma I.M.;
"Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:4987-4991(1985).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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INTERACTION WITH DSIPI.
DOI=10.1074/jbc.M101522200; PubMed=11397794 [NCBI, ExPASy, EBI, Israel, Japan]
Mittelstadt P.R.,
Ashwell J.D.;
"Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ.";
J. Biol. Chem. 276:29603-29610(2001).
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[5]
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PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF THR-325; THR-331; PHE-343; TYR-345; SER-362 AND SER-374.
PubMed=12134156 [NCBI, ExPASy, EBI, Israel, Japan]
Murphy L.O.,
Smith S.,
Chen R.H.,
Fingar D.C.,
Blenis J.;
"Molecular interpretation of ERK signal duration by immediate early gene products.";
Nat. Cell Biol. 4:556-564(2002).
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[6]
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PHOSPHORYLATION AT THR-232; THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF THR-232; THR-325; THR-331 AND SER-374.
DOI=10.1128/MCB.23.19.7030-7043.2003; PubMed=12972619 [NCBI, ExPASy, EBI, Israel, Japan]
Monje P.,
Marinissen M.J.,
Gutkind J.S.;
"Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor.";
Mol. Cell. Biol. 23:7030-7043(2003).
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[7]
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PHOSPHORYLATION AT SER-362, AND FUNCTION.
PubMed=15719069 [NCBI, ExPASy, EBI, Israel, Japan]
David J.-P.,
Mehic D.,
Bakiri L.,
Schilling A.F.,
Mandic V.,
Priemel M.,
Idarraga M.H.,
Reschke M.O.,
Hoffmann O.,
Amling M.,
Wagner E.F.;
"Essential role of RSK2 in c-Fos-dependent osteosarcoma development.";
J. Clin. Invest. 115:664-672(2005).
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- FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation.
- SUBUNIT: Heterodimer. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with MAFB (By similarity).
- SUBCELLULAR LOCATION: Nucleus.
- PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity).
- PTM: Constitutively sumoylated by SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232 (By similarity).
- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
- SIMILARITY: Contains 1 bZIP domain.
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