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Proto-oncogene c-Fos (Cellular oncogene fos) (G0/G1 switch regulatory protein 7)

 FOS_HUMAN               Reviewed;         380 AA.
P01100; A8K4E2; B4DQ65; P18849;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 208.
RecName: Full=Proto-oncogene c-Fos;
AltName: Full=Cellular oncogene fos;
AltName: Full=G0/G1 switch regulatory protein 7;
Name=FOS; Synonyms=G0S7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6574479; DOI=10.1073/pnas.80.11.3183;
van Straaten F., Mueller R., Curran T., Van Beveren C., Verma I.M.;
"Complete nucleotide sequence of a human c-onc gene: deduced amino
acid sequence of the human c-fos protein.";
Proc. Natl. Acad. Sci. U.S.A. 80:3183-3187(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-6 (ISOFORM 1/2).
PubMed=1658710;
Roux P., Verrier B., Klein B., Niccolino M., Marty L., Alexandre C.,
Piechaczyk M.;
"Retrovirus-mediated gene transfer of a human c-fos cDNA into mouse
bone marrow stromal cells.";
Oncogene 6:2155-2160(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 133-200 (ISOFORM 1), DNA-BINDING, AND
SUBUNIT.
PubMed=2516827; DOI=10.1101/gad.3.12b.2083;
Hai T., Liu F., Coukos W.J., Green M.R.;
"Transcription factor ATF cDNA clones: an extensive family of leucine
zipper proteins able to selectively form DNA-binding heterodimers.";
Genes Dev. 3:2083-2090(1989).
[9]
ERRATUM.
Hai T., Liu F., Coukos W.J., Green M.R.;
Genes Dev. 4:682-682(1990).
[10]
DNA-BINDING.
PubMed=2511004;
Nakabeppu Y., Nathans D.;
"The basic region of Fos mediates specific DNA binding.";
EMBO J. 8:3833-3841(1989).
[11]
PHOSPHORYLATION AT SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF
SER-362 AND SER-374.
PubMed=7588633;
Okazaki K., Sagata N.;
"The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and
augments its transforming activity in NIH 3T3 cells.";
EMBO J. 14:5048-5059(1995).
[12]
IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX,
FUNCTION, AND INTERACTION WITH SMAD3.
PubMed=9732876; DOI=10.1038/29814;
Zhang Y., Feng X.H., Derynck R.;
"Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-
induced transcription.";
Nature 394:909-913(1998).
[13]
PHOSPHORYLATION AT THR-325; THR-331 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).
[14]
SUMOYLATION AT LYS-265, SUBCELLULAR LOCATION, FUNCTION, AND
MUTAGENESIS OF LYS-128; LYS-192; LYS-265; THR-325; THR-331; SER-362
AND SER-374.
PubMed=16055710; DOI=10.1128/MCB.25.16.6964-6979.2005;
Bossis G., Malnou C.E., Farras R., Andermarcher E., Hipskind R.,
Rodriguez M., Schmidt D., Muller S., Jariel-Encontre I.,
Piechaczyk M.;
"Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.";
Mol. Cell. Biol. 25:6964-6979(2005).
[15]
SUMOYLATION.
PubMed=17709345; DOI=10.1093/nar/gkm617;
Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
"Ubc9 fusion-directed SUMOylation identifies constitutive and
inducible SUMOylation.";
Nucleic Acids Res. 35:E109-E109(2007).
[16]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION
AT TYR-10 AND TYR-30, AND MUTAGENESIS OF TYR-10; TYR-30; TYR-106 AND
TYR-337.
PubMed=17160021; DOI=10.1038/sj.onc.1210137;
Portal M.M., Ferrero G.O., Caputto B.L.;
"N-Terminal c-Fos tyrosine phosphorylation regulates c-Fos/ER
association and c-Fos-dependent phospholipid synthesis activation.";
Oncogene 26:3551-3558(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-10 AND TYR-30,
AND MUTAGENESIS OF TYR-10 AND TYR-30.
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).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128 AND LYS-265, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113; LYS-128 AND LYS-265,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[22]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 139-198 OF COMPLEX WITH JUN.
PubMed=7816143; DOI=10.1038/373257a0;
Glover J.N., Harrison S.C.;
"Crystal structure of the heterodimeric bZIP transcription factor c-
Fos-c-Jun bound to DNA.";
Nature 373:257-261(1995).
-!- 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}.
-!- SUBUNIT: Heterodimer; with JUN (By similarity). Interacts with
MAFB (By similarity). 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. Interacts with
DSIPI; this interaction inhibits the binding of active AP1 to its
target DNA. Interacts with CDS1 and PI4K2A (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P05067:APP; NbExp=3; IntAct=EBI-852851, EBI-77613;
P15336:ATF2; NbExp=9; IntAct=EBI-852851, EBI-1170906;
P18848:ATF4; NbExp=3; IntAct=EBI-852851, EBI-492498;
P17544:ATF7; NbExp=4; IntAct=EBI-852851, EBI-765623;
P10909:CLU; NbExp=2; IntAct=EBI-852851, EBI-1104674;
Q9BT78:COPS4; NbExp=2; IntAct=EBI-852851, EBI-742413;
P05412:JUN; NbExp=36; IntAct=EBI-852851, EBI-852823;
P17275:JUNB; NbExp=8; IntAct=EBI-852851, EBI-748062;
P17535:JUND; NbExp=9; IntAct=EBI-852851, EBI-2682803;
P56671:Maz (xeno); NbExp=2; IntAct=EBI-852851, EBI-1809712;
Q03112:MECOM; NbExp=4; IntAct=EBI-852851, EBI-1384862;
O14974:PPP1R12A; NbExp=2; IntAct=EBI-852851, EBI-351726;
P42224:STAT1; NbExp=6; IntAct=EBI-852851, EBI-1057697;
P56279:TCL1A; NbExp=4; IntAct=EBI-852851, EBI-749995;
P52736:ZNF133; NbExp=4; IntAct=EBI-852851, EBI-2687350;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P01100-1; Sequence=Displayed;
Name=2;
IsoId=P01100-2; Sequence=VSP_055560;
Note=No experimental confirmation available.;
Name=3;
IsoId=P01100-3; Sequence=VSP_055561;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Expressed at very low levels in quiescent
cells. When cells are stimulated to reenter growth, they undergo 2
waves of expression, the first one peaks 7.5 minutes following FBS
induction. At this stage, the protein is localized endoplasmic
reticulum. The second wave of expression occurs at about 20
minutes after induction and peaks at 1 hour. At this stage, the
protein becomes nuclear. {ECO:0000269|PubMed:17160021}.
-!- 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}.
-!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fos/";
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EMBL; V01512; CAA24756.1; -; Genomic_DNA.
EMBL; K00650; AAA52471.1; -; Genomic_DNA.
EMBL; AY212879; AAO21129.1; -; Genomic_DNA.
EMBL; AK097379; BAG53458.1; -; mRNA.
EMBL; AK290907; BAF83596.1; -; mRNA.
EMBL; AK298659; BAG60827.1; -; mRNA.
EMBL; AF111167; AAC98315.1; -; Genomic_DNA.
EMBL; CH471061; EAW81229.1; -; Genomic_DNA.
EMBL; BC004490; AAH04490.1; -; mRNA.
EMBL; S65138; AAB20306.1; -; mRNA.
CCDS; CCDS9841.1; -. [P01100-1]
PIR; A01342; TVHUF1.
PIR; E34223; E34223.
RefSeq; NP_005243.1; NM_005252.3. [P01100-1]
UniGene; Hs.25647; -.
PDB; 1A02; X-ray; 2.70 A; F=138-193.
PDB; 1FOS; X-ray; 3.05 A; E/G=139-200.
PDB; 1S9K; X-ray; 3.10 A; D=140-192.
PDBsum; 1A02; -.
PDBsum; 1FOS; -.
PDBsum; 1S9K; -.
DisProt; DP00078; -.
ProteinModelPortal; P01100; -.
SMR; P01100; -.
BioGrid; 108636; 134.
CORUM; P01100; -.
DIP; DIP-1047N; -.
ELM; P01100; -.
IntAct; P01100; 143.
MINT; MINT-105814; -.
STRING; 9606.ENSP00000306245; -.
BindingDB; P01100; -.
ChEMBL; CHEMBL2111421; -.
DrugBank; DB08813; Nadroparin.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; P01100; -.
PhosphoSitePlus; P01100; -.
BioMuta; FOS; -.
DMDM; 120470; -.
EPD; P01100; -.
PaxDb; P01100; -.
PeptideAtlas; P01100; -.
PRIDE; P01100; -.
DNASU; 2353; -.
Ensembl; ENST00000303562; ENSP00000306245; ENSG00000170345. [P01100-1]
Ensembl; ENST00000535987; ENSP00000442268; ENSG00000170345. [P01100-3]
Ensembl; ENST00000555686; ENSP00000452590; ENSG00000170345. [P01100-2]
GeneID; 2353; -.
KEGG; hsa:2353; -.
UCSC; uc010asi.4; human. [P01100-1]
CTD; 2353; -.
DisGeNET; 2353; -.
EuPathDB; HostDB:ENSG00000170345.9; -.
GeneCards; FOS; -.
HGNC; HGNC:3796; FOS.
HPA; HPA018531; -.
MIM; 164810; gene.
neXtProt; NX_P01100; -.
OpenTargets; ENSG00000170345; -.
Orphanet; 528; Berardinelli-Seip congenital lipodystrophy.
PharmGKB; PA28212; -.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00730000110541; -.
HOGENOM; HOG000234334; -.
HOVERGEN; HBG005743; -.
InParanoid; P01100; -.
KO; K04379; -.
OMA; HRPACKM; -.
OrthoDB; EOG091G0GGW; -.
PhylomeDB; P01100; -.
TreeFam; TF326301; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
SignaLink; P01100; -.
SIGNOR; P01100; -.
ChiTaRS; FOS; human.
EvolutionaryTrace; P01100; -.
GeneWiki; C-Fos; -.
GenomeRNAi; 2353; -.
PRO; PR:P01100; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000170345; -.
CleanEx; HS_FOS; -.
ExpressionAtlas; P01100; baseline and differential.
Genevisible; P01100; HS.
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; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
GO; GO:0035976; C:transcription factor AP-1 complex; IDA:CAFA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IMP:CAFA.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IMP:CAFA.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:BHF-UCL.
GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl.
GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0030431; P:sleep; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:BHF-UCL.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029816; c-Fos/v-Fos.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF4; PTHR23351:SF4; 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; Alternative splicing; 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_0000076465.
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:0000269|PubMed:17160021,
ECO:0000269|PubMed:22105363}.
MOD_RES 30 30 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:17160021,
ECO:0000269|PubMed:22105363}.
MOD_RES 232 232 Phosphothreonine.
{ECO:0000250|UniProtKB:P01101}.
MOD_RES 325 325 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:12134156}.
MOD_RES 331 331 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:12134156}.
MOD_RES 362 362 Phosphoserine; by MAPK1, MAPK3 and
RPS6KA3. {ECO:0000269|PubMed:7588633}.
MOD_RES 374 374 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:12134156,
ECO:0000269|PubMed:7588633}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 114 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055560.
VAR_SEQ 132 167 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055561.
MUTAGEN 10 10 Y->E: Loss of activation of phospholipid
synthesis; when associated with E-30.
{ECO:0000269|PubMed:17160021,
ECO:0000269|PubMed:22105363}.
MUTAGEN 10 10 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.
{ECO:0000269|PubMed:17160021,
ECO:0000269|PubMed:22105363}.
MUTAGEN 30 30 Y->E: Loss of activation of phospholipid
synthesis; when associated with E-10.
{ECO:0000269|PubMed:17160021,
ECO:0000269|PubMed:22105363}.
MUTAGEN 30 30 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.
{ECO:0000269|PubMed:17160021,
ECO:0000269|PubMed:22105363}.
MUTAGEN 106 106 Y->F: No effect on Tyr-phosphorylation.
Loss of endoplasmic reticulum
localization in quiescent cells.
{ECO:0000269|PubMed:17160021}.
MUTAGEN 128 128 K->R: No change in sumoylation.
{ECO:0000269|PubMed:16055710}.
MUTAGEN 192 192 K->R: No change in sumoylation.
{ECO:0000269|PubMed:16055710}.
MUTAGEN 232 232 T->D: Decreased sumoylation levels.
MUTAGEN 265 265 K->R: Abolishes sumoylation. No change in
nuclear location nor on protein
stability. Increased AP1 transactivation
activity when heterodimerized with cJUN.
{ECO:0000269|PubMed:16055710}.
MUTAGEN 325 325 T->D: No change in sumoylation levels.
{ECO:0000269|PubMed:16055710}.
MUTAGEN 331 331 T->D: No change in sumoylation levels.
{ECO:0000269|PubMed:16055710}.
MUTAGEN 337 337 Y->F: No effect on Tyr-phosphorylation.
Loss of endoplasmic reticulum
localization in quiescent cells.
{ECO:0000269|PubMed:17160021}.
MUTAGEN 362 362 S->A: Loss of protein stability. Reduced
MOS/MAPK-mediated transforming ability;
when associated with A-374.
{ECO:0000269|PubMed:16055710,
ECO:0000269|PubMed:7588633}.
MUTAGEN 362 362 S->D: Increased protein stability.
Increased MOS/MAPK-mediated transforming
ability and no change in sumoylation
levels; when associated with D-374.
{ECO:0000269|PubMed:16055710,
ECO:0000269|PubMed:7588633}.
MUTAGEN 374 374 S->A: No change in sumoylation levels.
Loss of protein stability. Reduced
MOS/MAPK-mediated transforming ability;
when associated with A-362.
{ECO:0000269|PubMed:16055710,
ECO:0000269|PubMed:7588633}.
MUTAGEN 374 374 S->D: Increased protein stability.
Increased MOS/MAPK-mediated transforming
ability and no change in sumoylation
levels; when associated with D-362.
{ECO:0000269|PubMed:16055710,
ECO:0000269|PubMed:7588633}.
CONFLICT 133 144 SPEEEEKRRIRR -> ISRRRREKENPK (in Ref. 6;
no nucleotide entry). {ECO:0000305}.
HELIX 141 191 {ECO:0000244|PDB:1A02}.
SEQUENCE 380 AA; 40695 MW; 9E3B2969347C90C8 CRC64;
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC TDLAVSSANF
IPTVTAISTS PDLQWLVQPA LVSSVAPSQT RAPHPFGVPA PSAGAYSRAG VVKTMTGGRA
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLTGGLPEV ATPESEEAFT
LPLLNDPEPK PSVEPVKSIS SMELKTEPFD DFLFPASSRP SGSETARSVP DMDLSGSFYA
ADWEPLHSGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS FPSCAAAHRK
GSSSNEPSSD SLSSPTLLAL


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