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Proto-oncogene c-Fos (Cellular oncogene fos)

 FOS_PHORO               Reviewed;         381 AA.
Q56TN0;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
28-MAR-2018, entry version 65.
RecName: Full=Proto-oncogene c-Fos;
AltName: Full=Cellular oncogene fos;
Name=FOS;
Phodopus roborovskii (Roborovski's desert hamster) (Cricetulus
roborovskii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Phodopus.
NCBI_TaxID=109678;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Weiler E.;
"Expression of c-FOS in dwarf desert hamster Phodopus roborovskii
(Satunin 1903).";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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. 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 (By similarity). 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}.
-!- SUBUNIT: Heterodimer; with JUN (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 DSIPI; this interaction inhibits the binding of
active AP1 to its target DNA. Interacts with MAFB (By similarity).
Interacts with CDS1 and PI4K2A (By similarity). {ECO:0000250}.
-!- 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-363 and Ser-375 by MAPK1/2 and RSK1/2 leads to protein
stabilization with phosphorylation on Ser-375 being the major site
for protein stabilization on NGF stimulation. Phosphorylation on
Ser-363 and Ser-375 primes further phosphorylations on Thr-326 and
Thr-332 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-363 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
{ECO:0000305}.
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EMBL; AY593962; AAU00057.1; -; Genomic_DNA.
ProteinModelPortal; Q56TN0; -.
SMR; Q56TN0; -.
HOVERGEN; HBG005743; -.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029816; c-Fos/v-Fos.
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.
3: Inferred from homology;
Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond;
Nucleus; Phosphoprotein; Proto-oncogene; Ubl conjugation.
CHAIN 1 381 Proto-oncogene c-Fos.
/FTId=PRO_0000254958.
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. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
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:0000250|UniProtKB:P01101}.
MOD_RES 326 326 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 332 332 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 363 363 Phosphoserine; by MAPK1, MAPK3 and
RPS6KA3. {ECO:0000250|UniProtKB:P01100}.
MOD_RES 375 375 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000250|UniProtKB:P01100}.
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}.
SEQUENCE 381 AA; 40920 MW; 68E1F8C6C150E2E9 CRC64;
MMFSGFNTDY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC ADLSVSSANF
IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPT PSTGAYSRAG MVKTVSGGRA
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEDMSVAS LDLTGGLPEA ATPESEEAFS
LPLLNEPEPK TSLESVKSIS SMELKAEPFD DFLFSASSRP SGSETTARSV PDMDLSGSFY
AADWEPLHSS SLGMGPMATE LEPLCTPVVT CTPSCTTYTS SFVFTYPETD SFPSCAAAHR
KGSSSNEPSS DSLSSPTLLA L


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