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Proto-oncogene c-Fos (Cellular oncogene fos)

 FOS_MOUSE               Reviewed;         380 AA.
P01101;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 155.
RecName: Full=Proto-oncogene c-Fos;
AltName: Full=Cellular oncogene fos;
Name=Fos;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6301687; DOI=10.1016/0092-8674(83)90306-9;
van Beveren C., van Straaten F., Curran T., Mueller R., Verma I.M.;
"Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that
viral and cellular fos gene products have different carboxy termini.";
Cell 32:1241-1255(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2991903; DOI=10.1073/pnas.82.15.4987;
Meijlink F., Curran T., Miller A.D., Verma I.M.;
"Removal of a 67-base-pair sequence in the noncoding region of
protooncogene fos converts it to a transforming gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:4987-4991(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH DSIPI.
PubMed=11397794; DOI=10.1074/jbc.M101522200;
Mittelstadt P.R., Ashwell J.D.;
"Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ.";
J. Biol. Chem. 276:29603-29610(2001).
[5]
PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION,
AND MUTAGENESIS OF THR-325; THR-331; PHE-343; TYR-345; SER-362 AND
SER-374.
PubMed=12134156; DOI=10.1038/ncb822;
Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.;
"Molecular interpretation of ERK signal duration by immediate early
gene products.";
Nat. Cell Biol. 4:556-564(2002).
[6]
PHOSPHORYLATION AT THR-232; THR-325; THR-331; SER-362 AND SER-374,
FUNCTION, AND MUTAGENESIS OF THR-232; THR-325; THR-331 AND SER-374.
PubMed=12972619; DOI=10.1128/MCB.23.19.7030-7043.2003;
Monje P., Marinissen M.J., Gutkind J.S.;
"Phosphorylation of the carboxyl-terminal transactivation domain of c-
Fos by extracellular signal-regulated kinase mediates the
transcriptional activation of AP-1 and cellular transformation induced
by platelet-derived growth factor.";
Mol. Cell. Biol. 23:7030-7043(2003).
[7]
PHOSPHORYLATION AT SER-362, AND FUNCTION.
PubMed=15719069; DOI=10.1172/JCI200522877;
David J.-P., Mehic D., Bakiri L., Schilling A.F., Mandic V.,
Priemel M., Idarraga M.H., Reschke M.O., Hoffmann O., Amling M.,
Wagner E.F.;
"Essential role of RSK2 in c-Fos-dependent osteosarcoma development.";
J. Clin. Invest. 115:664-672(2005).
[8]
FUNCTION.
PubMed=21998197; DOI=10.1091/mbc.E11-03-0259;
Alfonso Pecchio A.R., Cardozo Gizzi A.M., Renner M.L.,
Molina-Calavita M., Caputto B.L.;
"c-Fos activates and physically interacts with specific enzymes of the
pathway of synthesis of polyphosphoinositides.";
Mol. Biol. Cell 22:4716-4725(2011).
[9]
FUNCTION, INTERACTION WITH CDS1 AND PI4K2A, TYROSINE PHOSPHORYLATION
BY SRC, AND MUTAGENESIS OF LYS-139; ARG-144 AND ARG-146.
PubMed=22105363; DOI=10.1038/onc.2011.510;
Ferrero G.O., Velazquez F.N., Caputto B.L.;
"The kinase c-Src and the phosphatase TC45 coordinately regulate c-Fos
tyrosine phosphorylation and c-Fos phospholipid synthesis activation
capacity.";
Oncogene 31:3381-3391(2012).
-!- 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}.
-!- SUBUNIT: Heterodimer; with JUN (By similarity). Interacts with
MAFB. Component of the SMAD3/SMAD4/JUN/FOS complex required for
synergistic TGF-beta-mediated transcription at the AP1 promoter
site. Interacts with SMAD3; the interaction is weak even on TGF-
beta activation. Interacts with MAFB (By similarity). Interacts
with DSIPI; this interaction inhibits the binding of active AP1 to
its target DNA. Interacts with CDS1 and PI4K2A, but not with
CDIPT, nor PI4K2B. {ECO:0000250, ECO:0000269|PubMed:11397794,
ECO:0000269|PubMed:22105363}.
-!- INTERACTION:
O08537:Esr2; NbExp=2; IntAct=EBI-4288185, EBI-2526214;
-!- 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V00727; CAA24105.1; -; Genomic_DNA.
EMBL; J00370; AAA96699.1; -; Genomic_DNA.
EMBL; BC029814; AAH29814.1; -; mRNA.
CCDS; CCDS26059.1; -.
PIR; A01343; TVMSF.
RefSeq; NP_034364.1; NM_010234.2.
UniGene; Mm.246513; -.
PDB; 2WT7; X-ray; 2.30 A; A=138-200.
PDBsum; 2WT7; -.
ProteinModelPortal; P01101; -.
SMR; P01101; -.
BioGrid; 199726; 21.
DIP; DIP-1066N; -.
ELM; P01101; -.
IntAct; P01101; 2.
MINT; MINT-1500015; -.
STRING; 10090.ENSMUSP00000021674; -.
iPTMnet; P01101; -.
PhosphoSitePlus; P01101; -.
MaxQB; P01101; -.
PaxDb; P01101; -.
PRIDE; P01101; -.
Ensembl; ENSMUST00000021674; ENSMUSP00000021674; ENSMUSG00000021250.
GeneID; 14281; -.
KEGG; mmu:14281; -.
UCSC; uc007oha.2; mouse.
CTD; 2353; -.
MGI; MGI:95574; Fos.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00730000110541; -.
HOGENOM; HOG000234334; -.
HOVERGEN; HBG005743; -.
InParanoid; P01101; -.
KO; K04379; -.
OMA; HRPACKM; -.
OrthoDB; EOG091G0GGW; -.
PhylomeDB; P01101; -.
TreeFam; TF326301; -.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
ChiTaRS; Fos; mouse.
PRO; PR:P01101; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021250; -.
CleanEx; MM_FOS; -.
Genevisible; P01101; MM.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0035976; C:transcription factor AP-1 complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IMP:MGI.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IDA:MGI.
GO; GO:0009629; P:response to gravity; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0030431; P:sleep; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029816; c-Fos/v-Fos.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF31; PTHR23351:SF31; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; DNA-binding;
Endoplasmic reticulum; Isopeptide bond; Nucleus; Phosphoprotein;
Proto-oncogene; Reference proteome; Ubl conjugation.
CHAIN 1 380 Proto-oncogene c-Fos.
/FTId=PRO_0000076467.
DOMAIN 137 200 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 139 159 Basic motif; required for the activation
of phospholipid synthesis, but not for
CDS1-binding.
REGION 165 193 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 10 10 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 30 30 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 232 232 Phosphothreonine.
{ECO:0000269|PubMed:12972619}.
MOD_RES 325 325 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
MOD_RES 331 331 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
MOD_RES 362 362 Phosphoserine; by MAPK1, MAPK3 and
RPS6KA3. {ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619,
ECO:0000269|PubMed:15719069}.
MOD_RES 374 374 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01100}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01100}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01100}.
MUTAGEN 139 139 K->N: No effect on activation of
phospholipid synthesis.
{ECO:0000269|PubMed:22105363}.
MUTAGEN 144 144 R->N: No effect on activation of
phospholipid synthesis, nor on CDS1-
binding. {ECO:0000269|PubMed:22105363}.
MUTAGEN 146 146 R->N: Complete loss of activation of
phospholipid synthesis. No effect on
CDS1-binding.
{ECO:0000269|PubMed:22105363}.
MUTAGEN 232 232 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. {ECO:0000269|PubMed:12972619}.
MUTAGEN 325 325 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.
{ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
MUTAGEN 331 331 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.
{ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
MUTAGEN 343 343 F->A: Reduced phosphorylation by ERK.
Reduced AP1 activity by 65%.
{ECO:0000269|PubMed:12134156}.
MUTAGEN 345 345 Y->A: Reduced phosphorylation by ERK.
{ECO:0000269|PubMed:12134156}.
MUTAGEN 362 362 S->D: Enhanced EGF- and RSK-mediated
tranformation; when associated with D-
374. {ECO:0000269|PubMed:12134156}.
MUTAGEN 362 362 S->E: Increased enhancement of EGF- and
RSK-mediated tranformation; when
associated with E-374.
{ECO:0000269|PubMed:12134156}.
MUTAGEN 374 374 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. {ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
MUTAGEN 374 374 S->D: Enhanced EGF- and RSK-mediated
tranformation; when associated with D-
362. {ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
MUTAGEN 374 374 S->E: Enhanced EGF- and RSK-mediated
tranformation; when associated with E-
362. {ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:12972619}.
HELIX 139 199 {ECO:0000244|PDB:2WT7}.
SEQUENCE 380 AA; 40838 MW; 475966265952B624 CRC64;
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNTQDFC ADLSVSSANF
IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGLPT QSAGAYARAG MVKTVSGGRA
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLTGGLPEA STPESEEAFT
LPLLNDPEPK PSLEPVKSIS NVELKAEPFD DFLFPASSRP SGSETSRSVP DVDLSGSFYA
ADWEPLHSNS LGMGPMVTEL EPLCTPVVTC TPGCTTYTSS FVFTYPEADS FPSCAAAHRK
GSSSNEPSSD SLSSPTLLAL


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