| + |
UBE2I | down-regulates activity 
sumoylation
|
FOS |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263013 |
Lys265 |
SISSMELkTEPFDDF |
Homo sapiens |
|
| pmid |
sentence |
| 16055711 |
We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229. Sumoylation of c-Fos preferentially occurs in the context of c-Jun/c-Fos heterodimers.|Inhibition of c-Fos and c-Jun sumoylation stimulates AP-1-dependent transcription activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SAE1/SAE2 complex | down-regulates activity
sumoylation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263014 |
Lys265 |
SISSMELkTEPFDDF |
Homo sapiens |
|
| pmid |
sentence |
| 16055711 |
We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229. Sumoylation of c-Fos preferentially occurs in the context of c-Jun/c-Fos heterodimers.|Inhibition of c-Fos and c-Jun sumoylation stimulates AP-1-dependent transcription activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | up-regulates activity 
phosphorylation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252789 |
Ser362 |
AAAHRKGsSSNEPSS |
Homo sapiens |
|
| pmid |
sentence |
| 8248197 |
We now provide evidence that two growth-regulated, nucleus- and cytoplasm-localized protein kinases, 90-kda ribosomal s6 kinase (rsk) and mitogen-activated protein kinase (map kinase), contribute to the serum-induced phosphorylation of c-fos. The major phosphopeptides derived from biosynthetically labeled c-fos correspond to phosphopeptides generated after phosphorylation of c-fos in vitro with both rsk and map kinase. The phosphorylation sites identified for rsk (ser-362) and map kinase (ser-374) are in the transrepression domain. Cooperative phosphorylation at these sites by both enzymes was observed in vitro and reflected in vivo by the predominance of the peptide phosphorylated on both sites, as opposed to singly phosphorylated peptides. This study suggests a role for nuclear rsk and map kinase in modulating newly synthesized c-fos phosphorylation and downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262998 |
Ser374 |
PSSDSLSsPTLLAL |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, |
| Pathways: | Leptin Signaling |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262995 |
Ser362 |
AAAHRKGsSSNEPSS |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251524 |
Ser374 |
PSSDSLSsPTLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251522 |
Thr325 |
TELEPLCtPVVTCTP |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263010 |
Thr325 |
TELEPLCtPVVTCTP |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251523 |
Thr331 |
CTPVVTCtPSCTAYT |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263009 |
Thr331 |
CTPVVTCtPSCTAYT |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
6 |
Organism: |
, Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, EGFR Signaling, Leptin Signaling, T cell activation |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
FOS |
0.786 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262996 |
Ser362 |
AAAHRKGsSSNEPSS |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235671 |
Ser374 |
PSSDSLSsPTLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
We have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. ERK2 phosphorylated c-Fos TADs that included Thr- 325, Thr-331, or Ser-374 as unique phospho-acceptor sites, thus indicating that these residues can serve as in vitro targets for the enzymatic activity of ERK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235877 |
Thr232 |
GGLPEVAtPESEEAF |
Homo sapiens |
1BR3.G Cell |
| pmid |
sentence |
| 7816602 |
Phosphorylation of the c-fos and c-jun hob1 motif stimulates its activation capacity here we show that the hob1-containing activation domain of c-fos is stimulated by ha-ras in vivo and phosphorylated by a map kinase family member in vitro and that mutating t232 to ala abolishes both functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263011 |
Thr325 |
TELEPLCtPVVTCTP |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236010 |
Thr325 |
TELEPLCtPVVTCTP |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
We have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. ERK2 phosphorylated c-Fos TADs that included Thr- 325, Thr-331, or Ser-374 as unique phospho-acceptor sites, thus indicating that these residues can serve as in vitro targets for the enzymatic activity of ERK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236014 |
Thr331 |
CTPVVTCtPSCTAYT |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
We have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. ERK2 phosphorylated c-Fos TADs that included Thr- 325, Thr-331, or Ser-374 as unique phospho-acceptor sites, thus indicating that these residues can serve as in vitro targets for the enzymatic activity of ERK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263007 |
Thr331 |
CTPVVTCtPSCTAYT |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
7 |
Organism: |
, Homo Sapiens |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
FOS |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262997 |
Ser362 |
AAAHRKGsSSNEPSS |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118023 |
Ser374 |
PSSDSLSsPTLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263012 |
Thr325 |
TELEPLCtPVVTCTP |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118027 |
Thr325 |
TELEPLCtPVVTCTP |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118031 |
Thr331 |
CTPVVTCtPSCTAYT |
Homo sapiens |
|
| pmid |
sentence |
| 12972619 |
In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263008 |
Thr331 |
CTPVVTCtPSCTAYT |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
6 |
Organism: |
, Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
FOS |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250356 |
Ser362 |
AAAHRKGsSSNEPSS |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 1545828 |
Human c-Fos protein is phosphorylated in vitro by PKA. phosphorylation of Fos occurs at serine residue 362. Modification of the Fos protein by phosphorylation with PKA then allows it to act as a regulator of its own synthesis by downregulating fos gene expression at a transcriptional level |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
FOS |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37154 |
Ser362 |
AAAHRKGsSSNEPSS |
Homo sapiens |
|
| pmid |
sentence |
| 8248197 |
We now provide evidence that two growth-regulated, nucleus- and cytoplasm-localized protein kinases, 90-kda ribosomal s6 kinase (rsk) and mitogen-activated protein kinase (map kinase), contribute to the serum-induced phosphorylation of c-fos. The major phosphopeptides derived from biosynthetically labeled c-fos correspond to phosphopeptides generated after phosphorylation of c-fos in vitro with both rsk and map kinase. The phosphorylation sites identified for rsk (ser-362) and map kinase (ser-374) are in the transrepression domain. Cooperative phosphorylation at these sites by both enzymes was observed in vitro and reflected in vivo by the predominance of the peptide phosphorylated on both sites, as opposed to singly phosphorylated peptides. This study suggests a role for nuclear rsk and map kinase in modulating newly synthesized c-fos phosphorylation and downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262999 |
Ser374 |
PSSDSLSsPTLLAL |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, |
| + |
RPS6KA4 | up-regulates activity
phosphorylation
|
FOS |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191678 |
Ser362 |
AAAHRKGsSSNEPSS |
Homo sapiens |
|
| pmid |
sentence |
| 22187936 |
Rsk1/2 stabilize c-fos and increases its activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37216 |
Ser362 |
AAAHRKGsSSNEPSS |
Homo sapiens |
|
| pmid |
sentence |
| 8248197 |
Rsk1/2 phosphorylates the transcription factor c-fos on s362 and increases its activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263000 |
Ser374 |
PSSDSLSsPTLLAL |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, |
| + |
ERK1/2 | up-regulates
phosphorylation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251525 |
Thr232 |
GGLPEVAtPESEEAF |
Homo sapiens |
|
| pmid |
sentence |
| 7816602 |
Phosphorylation of the c-fos and c-jun hob1 motif stimulates its activation capacity here we show that the hob1-containing activation domain of c-fos is stimulated by ha-ras in vivo and phosphorylated by a map kinase family member in vitro and that mutating t232 to ala abolishes both functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260762 |
|
|
Homo sapiens |
HuH-7 Cell |
| pmid |
sentence |
| 21561061 |
3b Augments c-Fos Levels by Activating the ERK Pathway. | Higher c-Fos levels were observed in 3b-expressing cells than in GFP-expressing control cells |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, EGFR Signaling, Leptin Signaling, T cell activation |
| + |
MAPK3 | up-regulates
phosphorylation
|
FOS |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33909 |
Thr232 |
GGLPEVAtPESEEAF |
Homo sapiens |
|
| pmid |
sentence |
| 7816602 |
Phosphorylation of the c-fos and c-jun hob1 motif stimulates its activation capacity here we show that the hob1-containing activation domain of c-fos is stimulated by ha-ras in vivo and phosphorylated by a map kinase family member in vitro and that mutating t232 to ala abolishes both functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N | up-regulates quantity by expression
transcriptional regulation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260726 |
|
|
in vitro |
|
| pmid |
sentence |
| 14623261 |
The transcription factors c-Fos, FosB, CREB-1, and ATF2 were all activated by the addition of SARS-CoV N protein to the sample well |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MIR9-1HG | up-regulates quantity by expression
transcriptional regulation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261569 |
|
|
Rattus norvegicus |
Rat-2 Cell |
| pmid |
sentence |
| 10995546 |
CROC-4: a novel brain specific transcriptional activator of c-fos expressed from proliferation through to maturation of multiple neuronal cell types. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FOS | up-regulates quantity by expression
transcriptional regulation
|
STAR |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254878 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19022561 |
We found that both SF1 and LRH1 can transcriptionally cooperate with the AP-1 family members c-JUN and c-FOS, known to be associated with enhanced proliferation of endometrial carcinoma cells, to further enhance activation of the STAR, HSD3B2, and CYP19A1 PII promoters. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSDE1 | down-regulates quantity
post transcriptional regulation
|
FOS |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261145 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15314026 |
By testing different classes of mammalian poly(A) nucleases, we identified CCR4 as a poly(A) nuclease involved in the mCRD-mediated rapid deadenylation in viv |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
miR-155 | up-regulates quantity by expression
post transcriptional regulation
|
FOS |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24708856 |
We found overexpression of miR-155 led to increase in cJUN, FOS and TRIB2, and decrease in MEIS1, GFI1, cMYC and JARID2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML |
| + |
Gbeta | up-regulates
phosphorylation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270105 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7816602 |
Phosphorylation of the c-fos and c-jun hob1 motif stimulates its activation capacity here we show that the hob1-containing activation domain of c-fos is stimulated by ha-ras in vivo and phosphorylated by a map kinase family member in vitro and that mutating t232 to ala abolishes both functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YY2 | up-regulates quantity by expression
transcriptional regulation
|
FOS |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266212 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15087442 |
YY2 activated the p53 promoter. However, in contrast to YY1, which represses the activity of c-Fos, YY2 increased the activity of the c-Fos promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOS | form complex 
binding
|
AP1 |
0.952 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256366 |
|
|
in vitro |
|
| pmid |
sentence |
| 3142692 |
The c-Jun and c-fos proto-oncogenes encode proteins that form a complex which regulates transcription from promoters containing AP-1 activation elements. c-Jun has specific DNA binding activity, while c-Fos has homology to the putative DNA binding domain of c-Jun. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256368 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25875593 |
C-Fos dimerizes with c-Jun to form the transcription activator protein-1 (AP-1) which binds to the specific recognition site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256364 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1904542 |
The proteins encoded by the proto-oncogenes c-fos and c-jun (Fos and Jun, respectively) form a heterodimeric complex that regulates transcription by interacting with the DNA-regulatory element known as the activator protein 1 (AP-1) binding site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256362 |
|
|
in vitro |
|
| pmid |
sentence |
| 2467839 |
The protein products of the fos (Fos) and jun (Jun) proto-oncogenes have been shown to associate with a DNA element known as the transcription factor activator protein-1 (AP-1) binding site. Jun (previously known as the Fos-binding protein p39) and Fos form a protein complex in the nucleus. These data demonstrate a cooperative interaction between the protein products of two proto-oncogenes with a DNA element involved in transcriptional regulation. |
|
| Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML, Leptin Signaling, T cell activation |
| + |
ETS1 | up-regulates quantity
transcriptional regulation
|
FOS |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256495 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1722028 |
Furthermore, the possible involvement of an Ets protein in the control of c-fos has interesting implications for proto-oncogene cooperation in cellular growth control. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
(-)-anisomycin | up-regulates
chemical activation
|
FOS |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189626 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TWIST1 | up-regulates quantity by expression 
transcriptional regulation
|
FOS |
0.492 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255526 |
|
|
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 19051271 |
we performed microarray analysis to compare the gene expression profiles in HGC-27 cells, with or without small interfering RNA (siRNA)-mediated depletion of TWIST. Our results showed that NF1, RAP1A, SRPX, RBL2, PFDN4, ILK, F2R, ERBB3, and MYB were up-regulated, whereas AKR1C2, FOS, GDF15, NR2F1, ATM, and CTPS were down-regulated after TWIST depletion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML |
| + |
ARNT | down-regulates quantity by repression 
transcriptional regulation
|
FOS |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253696 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21544813 |
Screening by quantitative reverse-transcription PCR and PCR arrays revealed that cyclin E1, CDK2, Fos and Jun were negatively regulated by ARNT, whereas CDKN1C, CNKN2A, CDKN2B, MAPK11 and MAPK14 were positively regulated in HCC |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
arachidonic acid | up-regulates
|
FOS |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255392 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15878913 |
AA increases PC-3 prostate tumor cell growth, total DNA content and endogenous PGE 2 levels via induction of c-fos , cPLA 2 and cox-2 mRNA transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CREB1 | up-regulates quantity by expression
transcriptional regulation
|
FOS |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157151 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 17668895 |
Phosphorylation of creb by msk has been linked to the of nur77, nor1 and c-fos downstream of mapkin various cell types |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOS | up-regulates activity
binding
|
JUN |
0.952 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252087 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 2516828 |
The cFos proto-oncoprotein associates with cJun to form a heterodimer with increased DNA binding and transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, EGFR Signaling |
| + |
TWIST2 | up-regulates quantity by expression
transcriptional regulation
|
FOS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255503 |
|
|
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 19051271 |
we performed microarray analysis to compare the gene expression profiles in HGC-27 cells, with or without small interfering RNA (siRNA)-mediated depletion of TWIST. Our results showed that NF1, RAP1A, SRPX, RBL2, PFDN4, ILK, F2R, ERBB3, and MYB were up-regulated, whereas AKR1C2, FOS, GDF15, NR2F1, ATM, and CTPS were down-regulated after TWIST depletion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOS | up-regulates quantity by expression
transcriptional regulation
|
CYP19A1 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254879 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19022561 |
We found that both SF1 and LRH1 can transcriptionally cooperate with the AP-1 family members c-JUN and c-FOS, known to be associated with enhanced proliferation of endometrial carcinoma cells, to further enhance activation of the STAR, HSD3B2, and CYP19A1 PII promoters. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOS | up-regulates quantity by expression
transcriptional regulation
|
HSD3B2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254877 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19022561 |
We found that both SF1 and LRH1 can transcriptionally cooperate with the AP-1 family members c-JUN and c-FOS, known to be associated with enhanced proliferation of endometrial carcinoma cells, to further enhance activation of the STAR, HSD3B2, and CYP19A1 PII promoters. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GTF2I | up-regulates quantity by expression
transcriptional regulation
|
FOS |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268535 |
|
|
|
|
| pmid |
sentence |
| 16611241 |
For example, TFII-I binds to the Inr element of the T cell receptor Vbeta gene and activates its transcription in reporter gene assays (Cheriyath et al. 1998). TFII-I also activates transcription of c-fos and Goosecoid through binding to the serum response element and the distal element, respectively (Grueneberg et al. 1997; Ku et al. 2005). |
|
| Publications: |
1 |
3.0
FOS
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- 