| + |
MAPK1 | down-regulates activity 
phosphorylation
|
TNFRSF1A |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249452 |
Ser274 |
LAPNPSFsPTPGFTP |
in vitro |
|
| pmid |
sentence |
| 11606045 |
Phosphorylation of murine CD120a by p42(mapk/erk2) has been shown to inhibit its ability to initiate apoptosis while preserving signaling events such as NF-kappaB activation.|Additionally, we demonstrated that (i) the p42(mapk/erk2)-dependent phosphorylation of CD120a and DR3 occurred on Ser and Thr residues, (ii) p42(mapk/erk2) phosphorylated residues located in the membrane proximal regions but not the death domains of CD120a and DR3, (iii) Ser 253 is a preferred site of phosphorylation on CD120a |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249453 |
Thr280 |
FSPTPGFtPTLGFSP |
in vitro |
|
| pmid |
sentence |
| 11606045 |
Phosphorylation of murine CD120a by p42(mapk/erk2) has been shown to inhibit its ability to initiate apoptosis while preserving signaling events such as NF-kappaB activation.|Additionally, we demonstrated that (i) the p42(mapk/erk2)-dependent phosphorylation of CD120a and DR3 occurred on Ser and Thr residues, (ii) p42(mapk/erk2) phosphorylated residues located in the membrane proximal regions but not the death domains of CD120a and DR3, (iii) Ser 253 is a preferred site of phosphorylation on CD120a |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
TNF | up-regulates activity 
binding
|
TNFRSF1A |
0.923 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199091 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23070005 |
For TNFR1, the cytokine TNFα binds to the receptor and triggers its trimerization, which leads to the assembly of the receptor complex and initiation of signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256025 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21133840 |
TNF alpha and IFN gamma exhibit a cross-talk at the level of TNFR1 to induce activation of macrophages |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253593 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14732063 |
Tumour necrosis factor (TNF) exerts two main effects: a beneficial one as an anti-infection, anti-tumour cytokine, and a detrimental one in the systemic inflammatory response syndrome (SIRS). Two receptors (TNF-R) mediate these effects. two distinct types of TNF-Rs have been identified and molecularly cloned: TNF-R55 (also referred to as TNFR1, p55 or CD120a) and TNF-R75 (also called TNFR2, p75 or CD120b) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253591 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17151142 |
TNF-α has two distinct plasma membrane receptors known as p55 and p75. These data indicate that myogenic activation of p38 requires TNF-alpha receptor-mediated signaling |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109716 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11502070 |
Binding of tnf to the extracellular domain of tnfrsf1a leads to homotrimerization. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226676 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10634209 |
TNF-induced apoptosis is mediated primarily through the activation of type I receptors |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Multiple sclerosis, NF-KB Canonical, P38 Signaling, P38 Signaling and Myogenesis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
TNFRSF1A | up-regulates activity
binding
|
TRADD |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-32739 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 7758105 |
We have identified a novel 34 kda protein, designated tradd, that specifically interacts with an intracellular domain of tnfr1 tradd interacts with the death domain of tnfrsf1a to initiate distinct signaling cascades for two of the most important biological activities of tnf, nf-kb activation and programmed cell death tradd, a novel protein that specifically interacts with the death domain of tnfr1 and activates signaling pathways for both of these activities when overexpressed. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245029 |
|
|
Mus musculus |
MEF Cell, Macrophage |
| pmid |
sentence |
| 21232017 |
TRADD and RIP1 contain a C‐terminal death domain which mediates binding to the death domain of TNFR1. Upon association with ligated TNFR1, TRADD further recruits the adapter protein TRAF2 via its N‐terminal TRAF‐binding domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109719 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11502070 |
The death domain of tnfrsf1a provides a novel molecular interface that interacts specifically with the death domain of tradd. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, NF-KB Canonical, P38 Signaling, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
KRT14 | down-regulates activity
binding
|
TNFRSF1A |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251906 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11684708 |
TRADD specifically bound K18 and K14, type I (acidic) keratins. it is possible that epidermal K14 may function as an inhibitor of TNF–TNFR1 signaling through an association with TRADD. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNFRSF1A | up-regulates 
|
MAPK14 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226637 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11672426 |
Conversely, only activation of the TNFR1 could stimulate mitogen-activated protein kinase (MAPK) or p38 MAPK activities in a time-dependent manner. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235370 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 17151142 |
These results indicate that TNF-alpha regulates myogenesis and muscle regeneration as a key activator of p38. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | P38 Signaling, P38 Signaling and Myogenesis, TNF-alpha Signaling |
| + |
GRN | down-regulates
binding
|
TNFRSF1A |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172684 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21393509 |
Collectively, these findings demonstrate that pgrn is a ligand of tnfr, an antagonist of tnf signaling, and plays a critical role in the pathogenesis of inflammatory arthritis in mice. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNFRSF1A | up-regulates
|
TRAF2 |
0.826 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256251 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10795740 |
We found that TNF-R1-mediated IKK activation requires both RIP and TRAF2 proteins. Although TRAF2 or RIP can be independently recruited to the TNF-R1 complex, neither one of them alone is capable of transducing the TNF signal that leads to IKK activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis, Multiple sclerosis, NF-KB Canonical, P38 Signaling, TNF-alpha Signaling |
| + |
TNFRSF1A | up-regulates activity
|
MAPK14 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253602 |
|
|
|
|
| pmid |
sentence |
| 20887952 |
These results indicate that TNF-a-activated p38 pathway negatively controls the expansion of PAX7-positive SCs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253600 |
|
|
|
|
| pmid |
sentence |
| 17151142 |
[...] TNF-alpha is critical for p38 activation during the early stages of myoblast differentiation |
|
| Publications: |
2 |
| Pathways: | P38 Signaling, P38 Signaling and Myogenesis, TNF-alpha Signaling |
| + |
BAG4 | down-regulates activity
binding
|
TNFRSF1A |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245022 |
|
|
Mus musculus |
Macrophage |
| pmid |
sentence |
| 12748303 |
It was suggested that the silencer of death domains (SODD) protein constitutively associates intracellularly with TNFR1 and inhibits the recruitment of cytoplasmic signaling proteins to TNFR1 to prevent spontaneous aggregation of the cytoplasmic death domains of TNFR1 molecules that are juxtaposed in the absence of ligand stimulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | TNF-alpha Signaling |
| + |
TNFRSF1A | down-regulates quantity by destabilization 
|
NFKBIA |
0.54 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235789 |
|
|
Mus musculus |
MEF Cell, Macrophage |
| pmid |
sentence |
| 21232017 |
Tnfr1-induced phosforylation and degradarionn of ikb are almost completely abolished in tradd-deficient mefs,these hallmarks of classical nf-kn signaling are only attenuated in tradd-deficient macrophage. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Multiple sclerosis, NF-KB Canonical, TNF-alpha Signaling |
3.0
TNFRSF1A
- 
- 