Search Keyword:


Search option:


IID00436
UniprotP01100
ProteinProto-oncogene c-Fos
GeneFOS
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
380
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 138-193 Hetero trimer : IID00437Complex,IID00470Complex
 Evidence X-RAY 1a02 F Reference
       Region 1a02 F 138-139 disorder
       Region 1a02 F 140-192 order
       Region 1a02 F 193-193 disorder
 Evidence X-RAY 1s9k D Reference
       Region 1s9k D 140-192 order
Seq 139-200 Hetero dimer : IID00437Complex
 Evidence X-RAY 1fos E Reference
       Region 1fos E 139-198 order
       Region 1fos E 199-200 disorder
 Evidence X-RAY 1fos G Reference
       Region 1fos G 139-139 disorder
       Region 1fos G 140-198 order
       Region 1fos G 199-200 disorder
Seqphosphorylation
    362-362 Phosphoserine; by MAPK1
    10-10 Phosphotyrosine; by SRC
    30-30 Phosphotyrosine; by SRC
    232-232 Phosphothreonine
    325-325 Phosphothreonine; by MAPK1 and MAPK3
    331-331 Phosphothreonine; by MAPK1 and MAPK3
    374-374 Phosphoserine; by MAPK1 and MAPK3
 
Prediction
NeProc
Disorder 1-150,208-380
Order 151-207
ProS 1-12,58-80,122-135,146-150,261-269,287-292,325-347,355-360,370-380
AlphaFold
Disorder 1-70,74-74,77-132,209-291,293-380
Order 71-73,75-76,133-208,292-292
Pfam Hmmer
PF00170 135-199 4.9e-08
SEG 12-26 ,135-146 ,186-194 ,324-335 ,362-374
Function
Function in SwissProt
Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. 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. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.
Biological Process
See also
Diagram with PDB data
NFATC2/FOS/JUN/DNASTRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA