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IID50165
UniprotP01101
ProteinProto-oncogene c-Fos
GeneFos
OrganismMus musculus
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 138-200 Hetero dimer : P54841
 Evidence X-RAY 2wt7 A Reference
       Region 2wt7 A 138-200 order
Seqphosphorylation
    10-10 Phosphotyrosine; by SRC
    374-374 Phosphoserine; by MAPK1 and MAPK3
    362-362 Phosphoserine; by MAPK1
    331-331 Phosphothreonine; by MAPK1 and MAPK3
    325-325 Phosphothreonine; by MAPK1 and MAPK3
    30-30 Phosphotyrosine; by SRC
    232-232 Phosphothreonine
 
Prediction
NeProc
Disorder 1-150,209-380
Order 151-208
ProS 1-13,58-76,123-139,145-150,230-235,261-269,286-291,302-306,321-332,340-347,371-380
AlphaFold
Disorder 1-70,74-74,77-133,209-291,293-341,343-343,345-380
Order 71-73,75-76,134-208,292-292,342-342,344-344
Pfam Hmmer
PF00170 135-199 4.9e-08
SEG 12-26 ,135-146 ,186-194 ,277-288 ,324-338 ,362-374
Function
Function in SwissProt
Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By similarity). 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.