Fos
entrez
14281
canonical
uniprot
P01101
canonical
ensembl
ENSMUSG00000021250
resolver
ensp
ENSMUSP00000021674
resolver
enst
ENSMUST00000021674
resolver
genesymbol
Fos
resolver
uniprot_entry
FOS_MOUSE
resolver
amino_acid_sequence
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTQSAGAYARAGMVKTVSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEASTPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPDVDLSGSFYAADWEPLHSNSLGMGPMVTELEPLCTPVVTCTPGCTTYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
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. {ECO:0000250, ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069, ECO:0000269|PubMed:21998197, ECO:0000269|PubMed:22105363}.
uniprot
proteins
mass_dalton
40838
uniprot
proteins
mutagenesis
MUTAGEN 139; /note="K->N: No effect on activation of phospholipid synthesis."; /evidence="ECO:0000269|PubMed:22105363"; MUTAGEN 144; /note="R->N: No effect on activation of phospholipid synthesis, nor on CDS1-binding."; /evidence="ECO:0000269|PubMed:22105363"; MUTAGEN 146; /note="R->N: Complete loss of activation of phospholipid synthesis. No effect on CDS1-binding."; /evidence="ECO:0000269|PubMed:22105363"; MUTAGEN 165..193; /note="LQAETDQLEDEKSALQTEIANLLKEKEKL->AQAETDQAEDEKSAAQTEIANAAKEKEKA: Disrupts interaction with SMARCB1, SMARCD1, ARID1A and JUN."; /evidence="ECO:0000269|PubMed:29272704"; MUTAGEN 232; /note="T->A: No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-325; A-331 and A-374."; /evidence="ECO:0000269|PubMed:12972619"; MUTAGEN 325; /note="T->A: Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-331. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-331 and A-374."; /evidence="ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619"; MUTAGEN 331; /note="T->A: Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-325. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325;and A-374."; /evidence="ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619"; MUTAGEN 343; /note="F->A: Reduced phosphorylation by ERK. Reduced AP1 activity by 65%."; /evidence="ECO:0000269|PubMed:12134156"; MUTAGEN 345; /note="Y->A: Reduced phosphorylation by ERK."; /evidence="ECO:0000269|PubMed:12134156"; MUTAGEN 362; /note="S->D: Enhanced EGF- and RSK-mediated transformation; when associated with D-374."; /evidence="ECO:0000269|PubMed:12134156"; MUTAGEN 362; /note="S->E: Increased enhancement of EGF- and RSK-mediated transformation; when associated with E-374."; /evidence="ECO:0000269|PubMed:12134156"; MUTAGEN 374; /note="S->A: No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325 and A-331."; /evidence="ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619"; MUTAGEN 374; /note="S->D: Enhanced EGF- and RSK-mediated transformation; when associated with D-362."; /evidence="ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619"; MUTAGEN 374; /note="S->E: Enhanced EGF- and RSK-mediated transformation; when associated with E-362."; /evidence="ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619
uniprot
proteins
post_translational_modification
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). {ECO:0000250}.; 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. {ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
Fos subfamily
uniprot
proteins
pubmed
11397794
uniprot
proteins
pubmed
12134156
uniprot
proteins
pubmed
12972619
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15719069
uniprot
proteins
pubmed
21998197
uniprot
proteins
pubmed
22105363
uniprot
proteins
pubmed
29272704
uniprot
proteins
pubmed
2991903
uniprot
proteins
pubmed
6301687
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