FOS
entrez
2353
canonical
uniprot
P01100
canonical
ensembl
ENSG00000170345
resolver
ensp
ENSP00000306245
resolver
genesymbol
FOS
resolver
genesymbol_syn
G0S7
resolver
hgnc
HGNC:3796
resolver
uniprot
A8K4E2
resolver
uniprot
B4DQ65
resolver
uniprot
P18849
resolver
uniprot
Q6FG41
resolver
uniprot_entry
FOS_HUMAN
resolver
uniprot_entry
Q6FG41_HUMAN
resolver
uniprot_sec
A8K4E2
resolver
uniprot_sec
B4DQ65
resolver
uniprot_sec
P18849
resolver
amino_acid_sequence
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363, ECO:0000269|PubMed:7588633, ECO:0000269|PubMed:9732876}.
uniprot
proteins
mass_dalton
40695
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="Y->E: Loss of activation of phospholipid synthesis; when associated with E-30."; /evidence="ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363"; MUTAGEN 10; /note="Y->F: Overall loss of Tyr-phosphorylation, including that of Y-30 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells."; /evidence="ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363"; MUTAGEN 30; /note="Y->E: Loss of activation of phospholipid synthesis; when associated with E-10."; /evidence="ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363"; MUTAGEN 30; /note="Y->F: Overall loss of Tyr-phosphorylation, including that of Y-10 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells."; /evidence="ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363"; MUTAGEN 106; /note="Y->F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells."; /evidence="ECO:0000269|PubMed:17160021"; MUTAGEN 128; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16055710"; MUTAGEN 192; /note="K->R: No change in sumoylation."; /evidence="ECO:0000269|PubMed:16055710"; MUTAGEN 232; /note="T->D: Decreased sumoylation levels."; /evidence="ECO:0000269|PubMed:16055710"; MUTAGEN 265; /note="K->R: Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN."; /evidence="ECO:0000269|PubMed:16055710"; MUTAGEN 325; /note="T->D: No change in sumoylation levels."; /evidence="ECO:0000269|PubMed:16055710"; MUTAGEN 331; /note="T->D: No change in sumoylation levels."; /evidence="ECO:0000269|PubMed:16055710"; MUTAGEN 337; /note="Y->F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells."; /evidence="ECO:0000269|PubMed:17160021"; MUTAGEN 362; /note="S->A: Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374."; /evidence="ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:7588633"; MUTAGEN 362; /note="S->D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374."; /evidence="ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:7588633"; MUTAGEN 374; /note="S->A: No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362."; /evidence="ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:7588633"; MUTAGEN 374; /note="S->D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362."; /evidence="ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:7588633
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. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17709345}.; 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:17160021, ECO:0000269|PubMed:22105363}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
Fos subfamily
uniprot
proteins
pubmed
12134156
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16055710
uniprot
proteins
pubmed
1658710
uniprot
proteins
pubmed
17160021
uniprot
proteins
pubmed
17709345
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
22105363
uniprot
proteins
pubmed
2511004
uniprot
proteins
pubmed
2516827
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
6574479
uniprot
proteins
pubmed
7588633
uniprot
proteins
pubmed
7816143
uniprot
proteins
pubmed
9732876
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Endoplasmic reticulum. Cytoplasm, cytosol. 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.
uniprot
proteins