Fos
entrez
314322
canonical
uniprot
P12841
canonical
ensembl
ENSRNOG00000008015
resolver
ensembl
ENSRNOG00055025291
resolver
ensembl
ENSRNOG00060023383
resolver
ensembl
ENSRNOG00065024997
resolver
ensp
ENSRNOP00000010712
resolver
ensp
ENSRNOP00055035598
resolver
ensp
ENSRNOP00060033445
resolver
ensp
ENSRNOP00065035153
resolver
enst
ENSRNOT00000010712
resolver
enst
ENSRNOT00055043608
resolver
enst
ENSRNOT00060040477
resolver
enst
ENSRNOT00065042954
resolver
genesymbol
Fos
resolver
uniprot
Q4FDN1
resolver
uniprot_entry
FOS_RAT
resolver
uniprot_sec
Q4FDN1
resolver
amino_acid_sequence
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTPSTGAYARAGVVKTMSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPNDLGFPEEMSVTSLDLTGGLPEATTPESEEAFTLPLLNDPEPKPSLEPVKNISNMELKAEPFDDFLFPASSRPSGSETARSVPDVDLSGSFYAADWEPLHSSSLGMGPMVTELEPLCTPVVTCTPSCTTYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
uniprot
proteins
function
FUNCTION: 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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:17223854, ECO:0000269|PubMed:7816602}.
uniprot
proteins
mass_dalton
40927
uniprot
proteins
mutagenesis
MUTAGEN 232; /note="T->A: Abolishes HA-RAS-mediated activation. Loss of in vitro ERK2-mediated phosphorylation. No change in sumoylation levels."; /evidence="ECO:0000269|PubMed:7816602"; MUTAGEN 325; /note="T->A: Loss of NGF-mediated phosphorylation; when associated with A-331."; /evidence="ECO:0000269|PubMed:17223854"; MUTAGEN 331; /note="T->A: Loss of NGF-mediated phosphorylation; when associated with A-325."; /evidence="ECO:0000269|PubMed:17223854"; MUTAGEN 343..345; /note="FTY->ATA: Decreased phosphorylation levels. Reduced NGF-mediated enhanced transactivation."; /evidence="ECO:0000269|PubMed:17223854"; MUTAGEN 362; /note="S->A: Some loss of protein stabilization on NGF-treatment; when associated with D-374."; /evidence="ECO:0000269|PubMed:17223854"; MUTAGEN 362; /note="S->D: Increased protein stabilization on NGF-treatment, but no increase when treated with MAPK-inhibitor; when associated with D-374."; /evidence="ECO:0000269|PubMed:17223854"; MUTAGEN 374; /note="S->A: Greatly reduced protein stabilization on NGF stimulation."; /evidence="ECO:0000269|PubMed:17223854"; MUTAGEN 374; /note="S->D: Increased protein stabilization on NGF-treatment, but no increase when treated with MAPK-inhibitor; when associated with D-362. Some loss of protein stabilization on NGF-treatment; wnen associated with A-362."; /evidence="ECO:0000269|PubMed:17223854
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF) (By similarity). 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. {ECO:0000250, ECO:0000269|PubMed:17223854, ECO:0000269|PubMed:7816602}.; PTM: Constitutively sumoylated with 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). {ECO:0000250}.; PTM: In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
Fos subfamily
uniprot
proteins
pubmed
17223854
uniprot
proteins
pubmed
2105492
uniprot
proteins
pubmed
3325886
uniprot
proteins
pubmed
7816602
uniprot
proteins
pubmed
9571165
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30 (By similarity). {ECO:0000250}.
uniprot
proteins