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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3325886 [NCBI, ExPASy, EBI, Israel, Japan]
Curran T.,
Gordon M.B.,
Rubino K.L.,
Sambucetti L.C.;
"Isolation and characterization of the c-fos(rat) cDNA and analysis of post-translational modification in vitro.";
Oncogene 2:79-84(1987).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
Weiler E.;
"cFOS expression in rat.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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[3]
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DNA-BINDING.
DOI=10.1073/pnas.87.3.1032; PubMed=2105492 [NCBI, ExPASy, EBI, Israel, Japan]
Abate C.,
Luk D.,
Gentz R.,
Rauscher F.J. III,
Curran T.;
"Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly.";
Proc. Natl. Acad. Sci. U.S.A. 87:1032-1036(1990).
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[4]
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INTERACTION WITH MAFB.
DOI=10.1006/bbrc.1998.8447; PubMed=9571165 [NCBI, ExPASy, EBI, Israel, Japan]
Matsushima-Hibiya Y.,
Nishi S.,
Sakai M.;
"Rat maf-related factors: the specificities of DNA binding and heterodimer formation.";
Biochem. Biophys. Res. Commun. 245:412-418(1998).
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[5]
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PHOSPHORYLATION AT THR-232, FUNCTION, AND MUTAGENESIS OF THR-232.
DOI=10.1093/nar/22.24.5173; PubMed=7816602 [NCBI, ExPASy, EBI, Israel, Japan]
Bannister A.J.,
Brown H.J.,
Sutherland J.A.,
Kouzarides T.;
"Phosphorylation of the c-Fos and c-Jun HOB1 motif stimulates its activation capacity.";
Nucleic Acids Res. 22:5173-5176(1994).
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[6]
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PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF THR-325; THR-331; 343-PHE--TYR-345; SER-362 AND SER-374.
DOI=10.1111/j.1471-4159.2006.04250.x; PubMed=17223854 [NCBI, ExPASy, EBI, Israel, Japan]
Pellegrino M.J.,
Stork P.J.;
"Sustained activation of extracellular signal-regulated kinase by nerve growth factor regulates c-fos protein stabilization and transactivation in PC12 cells.";
J. Neurochem. 99:1480-1493(2006).
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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 (By similarity). Interacts with MAFB.
- 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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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 380 AA [This is the length of the unprocessed precursor] |
Molecular weight: 40927 Da [This is the MW of the unprocessed precursor] |
CRC64: E62D16A88CB2BEE9 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNTQDFC ADLSVSSANF
70 80 90 100 110 120
IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGLPT PSTGAYARAG VVKTMSGGRA
130 140 150 160 170 180
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
190 200 210 220 230 240
TEIANLLKEK EKLEFILAAH RPACKIPNDL GFPEEMSVTS LDLTGGLPEA TTPESEEAFT
250 260 270 280 290 300
LPLLNDPEPK PSLEPVKNIS NMELKAEPFD DFLFPASSRP SGSETARSVP DVDLSGSFYA
310 320 330 340 350 360
ADWEPLHSSS LGMGPMVTEL EPLCTPVVTC TPSCTTYTSS FVFTYPEADS FPSCAAAHRK
370 380
GSSSNEPSSD SLSSPTLLAL
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P12841 in FASTA format |
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ExPASy Home page
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