+ |
DUSP26 | down-regulates activity
dephosphorylation
|
FADD |
0.376 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204559 |
Ser194 |
QNRSGAMsPMSWNSD |
Homo sapiens |
|
pmid |
sentence |
24548998 |
This multi-functionality of fadd may depend primarily on its subcellular location. Fadd shuttles between the cytosol and the nucleus and this signal is unclear;however, fadd trafficking requires phosphorylation of the protein on ser194dusp26 suppresses cell proliferation by fadd dephosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HIPK3 | down-regulates activity
phosphorylation
|
FADD |
0.447 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251272 |
Ser194 |
QNRSGAMsPMSWNSD |
in vitro |
|
pmid |
sentence |
11034606 |
FIST/HIPK3 causes FADD phosphorylation, thereby promoting FIST/HIPK3-FADD-Fas interaction.  Phosphorylation occurs on Ser194 close to the COOH terminus of human FADD| Fas ligand-induced activation of Jun NH(2)-terminal kinase is impaired by overexpressed active FIST/HIPK3 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAP3K1 | down-regulates activity
phosphorylation
|
FADD |
0.482 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123168 |
Ser194 |
QNRSGAMsPMSWNSD |
Homo sapiens |
|
pmid |
sentence |
15001534 |
The results clearly show that fadd phosphorylation at ser194 affects functions both upstream and downstream of the mekk1/mkk7/jnk1 pathway and is closely associated with chemosensitivity in prostate cancer cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, TNF-alpha Signaling |
+ |
PLK1 | down-regulates activity
phosphorylation
|
FADD |
0.471 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168204 |
Ser194 |
QNRSGAMsPMSWNSD |
Homo sapiens |
|
pmid |
sentence |
20890306 |
Fas-associated death domain-containing protein (FADD) was first identified as an adapter molecule involved in formation of a death-inducing signaling complex upon Fas stimulation| Plk1 phosphorylates fadd at ser-194 in response to treatment with taxol Phosphorylation by polo-like kinase 1 induces the tumor-suppressing activity of FADD |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP2K7 | down-regulates activity
phosphorylation
|
FADD |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123164 |
Ser194 |
QNRSGAMsPMSWNSD |
Homo sapiens |
|
pmid |
sentence |
15001534 |
The results clearly show that fadd phosphorylation at ser194 affects functions both upstream and downstream of the mekk1/mkk7/jnk1 pathway and is closely associated with chemosensitivity in prostate cancer cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, TNF-alpha Signaling |
+ |
CSNK1A1 | down-regulates activity
phosphorylation
|
FADD |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139307 |
Ser194 |
QNRSGAMsPMSWNSD |
Homo sapiens |
|
pmid |
sentence |
16061179 |
FADD is essential for death receptor (DR)-induced apoptosis.|Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKA | up-regulates
phosphorylation
|
FADD |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176739 |
Ser203 |
MSWNSDAsTSEAS |
Homo sapiens |
|
pmid |
sentence |
21978935 |
Here, we report that aur-a phosphorylates s203 of the fas associated with death domain protein (fadd)phosphorylation of s203 by aur-a serves to prime fadd for plk1-mediated phosphorylation at s194 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNFRSF10B | up-regulates
binding
|
FADD |
0.844 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98565 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Fadd binds to ligated trailr1 or trail-r2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRADD | up-regulates activity
binding
|
FADD |
0.774 |
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 |
+ |
FADD | up-regulates activity
binding
|
RIPK1 |
0.784 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191781 |
|
|
Homo sapiens |
|
pmid |
sentence |
22890322 |
Rip1 is required for the formation of a rip1/fadd/caspase-8 complex that drives caspase-8 activation, cleavage of bid into tbid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase-dependent apoptosis. Tweak induces assembly of a death-signaling complex containing rip1, fadd, and caspase-8 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-173429 |
|
|
Homo sapiens |
|
pmid |
sentence |
21525013 |
Rip1 is required for the formation of a rip1/fadd/caspase-8 complex that drives caspase-8 activation, cleavage of bid into tbid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase-dependent apoptosis. Tweak induces assembly of a death-signaling complex containing rip1, fadd, and caspase-8 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical, TNF-alpha Signaling |
+ |
FADD | up-regulates
binding
|
CASP10 |
0.787 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112058 |
|
|
Homo sapiens |
|
pmid |
sentence |
11717445 |
The death-effector domains ofcasp8and -10 bothinteractwith the death-effector domain offadd. Therefore, caspase-10 is recruited into the fas signaling complex and becomes activated like caspase-8 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNFRSF10A | up-regulates
binding
|
FADD |
0.825 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97869 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Fadd binds to ligated trailr1 or trail-r2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FAS | up-regulates activity
binding
|
FADD |
0.907 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176651 |
|
|
Homo sapiens |
|
pmid |
sentence |
21959933 |
Aggregation-induced conformational changes in fas lead to the formation of the death-inducing signalling complex (disc) which involves recruitment of the adaptor protein fadd/mort1 through a homotypic interaction of death domains, present in both the intracellular region of fas and the c-terminus of fadd. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical, SARS-COV APOPTOSIS |
+ |
RUNX3 | up-regulates quantity by expression
transcriptional regulation
|
FADD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255095 |
|
|
Homo sapiens |
MKN-1 Cell |
pmid |
sentence |
17956589 |
Comprehensive analysis using a cDNA microarray showed that RUNX3 upregulated 17 apoptosis-related genes (including FADD, TRAF6, caspase-2, ING1, ING4, Calpain 10, and DNase1) and downregulated 135 apoptosis-related genes (including FLIP, PEA15, TXN2, HSPD1, IKK, and TIAL1) in MKN-1 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FADD | up-regulates activity
binding
|
CASP8 |
0.929 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112061 |
|
|
Homo sapiens |
|
pmid |
sentence |
11717445 |
Fadd recruits caspase-8 through homotypic interactions of death-effector domains (deds), leading to caspase-8 activation and apoptosis. In turn, fadd recruits the zymogen form of the apoptosis-initiating protease caspase-8, through homophilic interaction of death effector domains. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |