| + |
TRADD | up-regulates activity 
binding
|
CASP8 |
0.906 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118591 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Tradd recruits caspase-8 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
KRT14 | down-regulates activity 
binding
|
TRADD |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251907 |
|
|
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 |
| + |
TRADD | up-regulates activity
binding
|
FADD |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177958 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18545270 |
Tradd recruits fadd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39951 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8565075 |
The strong interaction between tradd and fadd occurs via their death domains. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical, 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 |
| + |
TRADD | up-regulates activity
binding
|
TRAF2 |
0.864 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179446 |
|
|
Mus musculus |
Fibrosarcoma Cell |
| pmid |
sentence |
| 18621737 |
The high affinity of the tradd-traf2 interaction is required for efficient suppression of apoptosis upon stimulation of the tumor necrosis factor receptor1 (tnfr1), tnf-receptor-associated death domain (tradd) provides a scaffold for the assembly of complex i at the plasma membrane by binding receptor interacting protein 1 (rip1), tnfreceptor- associated factor 2 ,traf2 these results provide evidence that tradd can serve as an adaptor protein and recruit traf1, traf2, or both to tnfrsf1a. The demonstration that tradd interacts with traf2 and fadd, and can recruit both to tnfrsf1a, suggested that traf2 and fadd may be involved in tnfrsf1a tradd-mediated signaling. That these interactions define two distinct signaling pathways emanating from tradd (figure 9) is supported by the ability of traf2 and fadd to activate nf-kb and induce apoptosis, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42980 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27383048 |
Upon stimulation with TNFα, TNFR1 recruits TRADD, which provides a scaffold for the assembly of complex I at the plasma membrane by binding with RIP1, TRAF2 and cIAP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118770 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 14585074 |
Tradd mediates recruitment of the traf2 adaptor protein |
|
| Publications: |
3 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | Inhibition of Apoptosis, NF-KB Canonical, P38 Signaling, TNF-alpha Signaling |
| + |
TRADD | up-regulates activity
binding
|
RIPK1 |
0.935 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40043 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8612133 |
We show that tradd interacts strongly with rip;rip is a serinethreonine kinase that is recruited by tradd to tnfr1 in a tnf-dependent process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical, TNF-alpha Signaling |
| + |
TRADD | up-regulates
binding
|
TRAF1 |
0.681 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73913 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10629108 |
Tradd mediates recruitment of traf1/2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNFRSF21 | up-regulates
binding
|
TRADD |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100184 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Dr6 interacts with tradd |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRADD | up-regulates
binding
|
TRAF5 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187058 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19632174 |
Upon stimulation of the tumor necrosis factor receptor1 (tnfr1), tnf-receptor-associated death domain (tradd) provides a scaffold for the assembly of complex i at the plasma membrane by binding receptor interacting protein 1 (rip1), tnfreceptor-associated factor 2 ,traf2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNFRSF25 | up-regulates
binding
|
TRADD |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100480 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Dr3 induces apoptosis by tradd-mediated recruitment of fadd and caspase-8 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRADD | up-regulates activity
binding
|
BIRC2 |
0.686 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45134 |
|
|
Homo sapiens |
HEK-293 Cell, U-937 Cell, HeLa Cell |
| pmid |
sentence |
| 8943045 |
The recruitment of TRAF2 and c-IAP1 to TNF-R1 is TNF-dependent, is mediated by TRADD. N-terminal domain of tradd may become accessible to traf2, thereby permitting recruitment of the traf2/ciap1 heterocomplex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TRADD
- 
- 