| + |
CASP8 | down-regulates activity 
cleavage
|
RIPK1 |
0.907 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71265 |
Asp324 |
RMQSLQLdCVAVPSS |
Homo sapiens |
HEK-293 Cell, MCF-7 Cell, HeLa Cell |
| pmid |
sentence |
| 10521396 |
These results suggested that the aspartic acid at position 324 is the cleavage site of ripk1. In this study we found that receptor-interacting protein (ripk1) is cleaved by casp8 when cells undergo tnf-induced apoptosis. The cleavage of ripk1 abolished its nf-kb inducing ability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, TNF-alpha Signaling |
| + |
Caspase 8 complex | down-regulates activity
cleavage
|
RIPK1 |
0.907 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256442 |
Asp324 |
RMQSLQLdCVAVPSS |
Homo sapiens |
HEK-293 Cell, MCF-7 Cell, HeLa Cell |
| pmid |
sentence |
| 10521396 |
These results suggested that the aspartic acid at position 324 is the cleavage site of ripk1. In this study we found that receptor-interacting protein (ripk1) is cleaved by casp8 when cells undergo tnf-induced apoptosis. The cleavage of ripk1 abolished its nf-kb inducing ability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRAF2 | up-regulates activity 
ubiquitination, binding
|
RIPK1 |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179456 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 18621737 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42984 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8702708 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235407 |
Lys377 |
NEPSLQSkLQDEANY |
Mus musculus |
MEF Cell, Macrophage |
| pmid |
sentence |
| 21232017 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59689 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 9712898 |
Following binding to tradd, traf2 was thought to mediate non-degradative lys-63-linked polyubiquitination of rip1 via its ring e3 ligase domain. Rip1 is known to directly interact with traf2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245032 |
|
|
Mus musculus |
MEF Cell, Macrophage |
| pmid |
sentence |
| 21232017 |
Rip1 is known to directly interact with traf2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271423 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 15175328 |
Taken together, these data suggest that Traf2 may be the E3 ubiquitin ligase that initiates TNF-α signaling, potentially by ubiquitinating Rip1. In the absence of Traf2, TNF-alpha-induced ubiquitination of Rip1 is impaired, suggesting that Traf2 may be the E3 ubiquitin ligase responsible for the TNF-alpha-dependent, ubiquitination of Rip1. Finally, recruitment of the ubiquitinated Tak1 complex is dependent on the presence of Rip1, suggesting that Rip1 ubiquitination rather than its phosphorylation is critical in signaling. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | Multiple sclerosis, NF-KB Canonical, SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
BIRC3 | up-regulates activity
ubiquitination, polyubiquitination
|
RIPK1 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145855 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 16603398 |
In this report, we show that ciap1 and ciap2 promote cancer cell survival by functioning as e3 ubiquitin ligases that maintain constitutive ubiquitination of the rip1 adaptor protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179443 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 18621737 |
In this report, we show that ciap1 and ciap2 promote cancer cell survival by functioning as e3 ubiquitin ligases that maintain constitutive ubiquitination of the rip1 adaptor protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179104 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
|
| pmid |
sentence |
| 18570872 |
In this report, we show that ciap1 and ciap2 promote cancer cell survival by functioning as e3 ubiquitin ligases that maintain constitutive ubiquitination of the rip1 adaptor protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272713 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21931591 |
CIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).Together, our results demonstrate that depleting cIAP1/2 inhibits RIP1-4 mediated NF-kB activation without affecting RIP auto-phosphorylation. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MIB2 | down-regulates activity
polyubiquitination
|
RIPK1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272662 |
Lys377 |
NEPSLQSkLQDEANY |
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 29642005 |
Here, we show that the E3 ubiquitin ligase Mind Bomb-2 (MIB2) regulates TNF-induced cell death by inactivating RIPK1 via inhibitory ubiquitylation. We find that MIB2 represses the cytotoxic potential of RIPK1 by ubiquitylating lysine residues in the C-terminal portion of RIPK1. Our data suggest that ubiquitin conjugation of RIPK1 interferes with RIPK1 oligomerization and RIPK1-FADD association. MIB2 Ubiquitylates RIPK1 at Lysines K377 and K634 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272663 |
Lys634 |
KVYQMLQkWVMREGI |
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 29642005 |
Here, we show that the E3 ubiquitin ligase Mind Bomb-2 (MIB2) regulates TNF-induced cell death by inactivating RIPK1 via inhibitory ubiquitylation. We find that MIB2 represses the cytotoxic potential of RIPK1 by ubiquitylating lysine residues in the C-terminal portion of RIPK1. Our data suggest that ubiquitin conjugation of RIPK1 interferes with RIPK1 oligomerization and RIPK1-FADD association. MIB2 Ubiquitylates RIPK1 at Lysines K377 and K634 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RIPK1 | up-regulates activity
phosphorylation
|
RIPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276161 |
Ser14 |
LNVIKMKsSDFLESA |
in vitro |
|
| pmid |
sentence |
| 18408713 |
These data suggest that Ser14/15, Ser20, Ser161 and Ser166 represent autophosphorylation sites in vitro, detected in the RIP1 kinase assay (Fig. 1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276162 |
Ser15 |
NVIKMKSsDFLESAE |
in vitro |
|
| pmid |
sentence |
| 18408713 |
These data suggest that Ser14/15, Ser20, Ser161 and Ser166 represent autophosphorylation sites in vitro, detected in the RIP1 kinase assay (Fig. 1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276158 |
Ser161 |
IADLGLAsFKMWSKL |
in vitro |
|
| pmid |
sentence |
| 18408713 |
These data suggest that Ser14/15, Ser20, Ser161 and Ser166 represent autophosphorylation sites in vitro, detected in the RIP1 kinase assay (Fig. 1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276159 |
Ser166 |
LASFKMWsKLNNEEH |
in vitro |
|
| pmid |
sentence |
| 18408713 |
These data suggest that Ser14/15, Ser20, Ser161 and Ser166 represent autophosphorylation sites in vitro, detected in the RIP1 kinase assay (Fig. 1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276160 |
Ser20 |
KSSDFLEsAELDSGG |
in vitro |
|
| pmid |
sentence |
| 18408713 |
These data suggest that Ser14/15, Ser20, Ser161 and Ser166 represent autophosphorylation sites in vitro, detected in the RIP1 kinase assay (Fig. 1) |
|
| Publications: |
5 |
Organism: |
In Vitro |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Innate Immune Response, Inflammosome Activation, Macrophage polarization, Mitochondrial Control of Apoptosis, Multiple sclerosis, NF-KB Canonical, P38 Signaling and Myogenesis, SAPK/JNK Signaling, SARS-CoV INFLAMMATORY RESPONSE, SARS-CoV INNATE RESPONSE TO dsRNA, TNF-alpha Signaling |
| + |
RIPK1 | up-regulates activity
phosphorylation
|
DAB2IP |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254763 |
Ser728 |
PSPARSSsYSEANEP |
Homo sapiens |
|
| pmid |
sentence |
| 27858941 |
Upon TNF stimulation, RIP1 phosphorylates DAB2IP on Serine 604, inducing a conformational switch that allows formation of the complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259976 |
Ser728 |
PSPARSSsYSEANEP |
Bos taurus |
|
| pmid |
sentence |
| 17389591 |
We further show that RIP1 (the Ser/Thr protein kinase receptor-interacting protein) associates with the GAP domain of AIP1 and mediates TNF-induced AIP1 phosphorylation at Ser-604 and JNK/p38 activation as demonstrated by both overexpression and small interfering RNA knockdown of RIP1 in EC. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Bos Taurus |
| + |
RIPK1 | up-regulates activity
phosphorylation
|
MAP3K1 |
0.431 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108257 |
Ser970 |
HSQCLNSsPLSHHSQ |
Homo sapiens |
|
| pmid |
sentence |
| 11369754 |
These findings strongly suggest that rip phosphorylates mekk1 at ser-957 and ser-994. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Macrophage polarization, SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
RIPK1 | up-regulates activity
binding
|
CASP8 |
0.907 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173432 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21525013 |
Degradation of ciaps triggers the release of receptor interacting protein kinase (ripk1) from tnf receptor i (tnfr1) to form a caspase-8 activating complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104255 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12887920 |
Tradd and rip1 associate with fadd and caspase-8, forming a cytoplasmic complex |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, TNF-alpha Signaling |
| + |
RIPK1 | up-regulates activity
binding
|
IKBKG |
0.912 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145858 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16603398 |
Interestingly, polyubiquitinated rip1 recruits ikk through the binding between the polyubiquitin chains and nemo, a regulatory subunit of the ikk complex. Mutations of nemo that disrupt its polyubiquitin binding also abolish ikk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Canonical |
| + |
BIRC2 | down-regulates quantity by destabilization
polyubiquitination
|
RIPK1 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272638 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 18570872 |
In this report, we show that cIAP1 and cIAP2 promote cancer cell survival by functioning as E3 ubiquitin ligases that maintain constitutive ubiquitination of the RIP1 adaptor protein. We demonstrate that AEG40730, a compound modeled on BIR-binding tetrapeptides, binds to cIAP1 and cIAP2, facilitates their autoubiquitination and proteosomal degradation, and causes a dramatic reduction in RIP1 ubiquitination. We show that cIAP1 and cIAP2 directly ubiquitinate RIP1 and induce constitutive RIP1 ubiquitination in cancer cells and demonstrate that constitutively ubiquitinated RIP1 associates with the prosurvival kinase TAK1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BIRC2 | up-regulates activity
ubiquitination, polyubiquitination
|
RIPK1 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18570872 |
CIAP1 and cIAP2 directly ubiquitinate RIP1 and induce constitutive RIP1 ubiquitination in cancer cells and demonstrate that constitutively ubiquitinated RIP1 associates with the prosurvival kinase TAK1. In this way RIP1 functions as a prosurvival scaffold molecule instead of a proapoptotic adaptor protein |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272710 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21931591 |
CIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).Together, our results demonstrate that depleting cIAP1/2 inhibits RIP1-4 mediated NF-kB activation without affecting RIP auto-phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179439 |
|
|
Homo sapiens |
Fibrosarcoma Cell |
| pmid |
sentence |
| 18621737 |
c-IAPs are ubiquitin ligases capable of promoting polymerization of non-degradative Lys-63-linked polyubiquitin chains on the critical adapter in the canonical NF-_B signaling pathway, RIP1. c-IAPs are E3 ligases and RIP1 ubiquitination is critical for propagation of TNF_-induced NF-_B activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145036 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16603398 |
In this report, we show that ciap1 and ciap2 promote cancer cell survival by functioning as e3 ubiquitin ligases that maintain constitutive ubiquitination of the rip1 adaptor protein. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
RNF216 | down-regulates quantity by destabilization
ubiquitination
|
RIPK1 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271608 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16968706 |
Triad3A promotes proteolytic degradation of adapter proteins. Triad3A promotes down-regulation of TIRAP, TRIF, and RIP1 proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIPK1 | up-regulates 
|
Necrosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121901 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14965271 |
Fas-induced necrosis requires rip |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FADD | up-regulates activity
binding
|
RIPK1 |
0.784 |
| 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 |
|
| 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 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical, TNF-alpha Signaling |
| + |
RIPK1 | up-regulates activity
binding
|
TAB2 |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128406 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15327770 |
TNF_ induced the polyubiquitination of RIP and the association of polyubiquitinated RIP with TAB2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145861 |
|
|
Homo sapiens |
HEK-293 Cell, JURKAT Cell |
| pmid |
sentence |
| 16603398 |
Taken together, these results indicate that polyubiquitination of RIP1 mediates the independent re- cruitment of TAB2 and NEMO, which in turn recruits TAK1 and IKK, respectively, to TNF-R1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Canonical, P38 Signaling and Myogenesis |
| + |
RIPK1 | up-regulates
phosphorylation
|
MAP3K1 |
0.431 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108260 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11369754 |
These findings strongly suggest that rip phosphorylates mekk1 at ser-957 and ser-994. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Macrophage polarization, SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
TRAF2 | up-regulates
|
RIPK1 |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256252 |
|
|
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: | Multiple sclerosis, NF-KB Canonical, SAPK/JNK Signaling, TNF-alpha Signaling |
| + |
ponatinib | down-regulates activity
chemical inhibition
|
RIPK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261082 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25801024 |
Discovery of ponatinib as the first-in-class dual inhibitor of RIPK1 and RIPK3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RFFL | down-regulates quantity by destabilization
ubiquitination
|
RIPK1 |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271482 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18450452 |
We report that CARP-2, a RING domain-containing ubiquitin protein ligase (E3), is a negative regulator of TNF-induced NF-kappaB activation. By virtue of its phospholipid-binding FYVE domain, CARP-2 localized to endocytic vesicles, where it interacted with internalized TNF-receptor complex, resulting in RIP ubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OTUD7B | down-regulates activity
deubiquitination
|
RIPK1 |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268411 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18178551 |
NF-kappaB Suppression by the Deubiquitinating Enzyme Cezanne|Our study provides several lines of evidence to suggest that Cezanne suppresses TNFR signaling to NF-κB by targeting RIP1 for deubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OTUD7A | down-regulates activity
deubiquitination
|
RIPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268410 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18178551 |
NF-kappaB Suppression by the Deubiquitinating Enzyme Cezanne|Our study provides several lines of evidence to suggest that Cezanne suppresses TNFR signaling to NF-κB by targeting RIP1 for deubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FAS | up-regulates activity
binding
|
RIPK1 |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235430 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 7538908 |
Fas associates with rip. Rip is a novel form of apoptosis-inducing protein |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical |
| + |
TNFAIP3 | down-regulates quantity
ubiquitination
|
RIPK1 |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259977 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15258597 |
A20The carboxy-terminal domain of A20, composed of seven C2/C2 zinc fingers, then functions as a ubiquitin ligase by polyubiquitinating RIP with K48-linked ubiquitin chains, thereby targeting RIP for proteasomal degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259978 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15258597 |
The amino-terminal domain of A20, which is a de-ubiquitinating (DUB) enzyme of the OTU (ovarian tumour) family, removes lysine-63 (K63)-linked ubiquitin chains from receptor interacting protein (RIP), an essential mediator of the proximal TNF receptor 1 (TNFR1) signalling complex. The carboxy-terminal domain of A20, composed of seven C2/C2 zinc fingers, then functions as a ubiquitin ligase by polyubiquitinating RIP with K48-linked ubiquitin chains, thereby targeting RIP for proteasomal degradation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Canonical |
| + |
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 |
| + |
RIPK1 | up-regulates
|
TNFRSF10A |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177952 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18545270 |
The death domain of the rip1 kinase binds to death receptors such as tumor necrosis factor-related apoptosis-inducing ligand receptor 1,trailr1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIPK1 | up-regulates activity
binding
|
IKK-complex |
0.662 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245026 |
|
|
Mus musculus |
Fibroblast |
| 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: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Innate Immune Response, Inflammosome Activation, Macrophage polarization, Multiple sclerosis, NF-KB Canonical, SARS-CoV INFLAMMATORY RESPONSE, SARS-CoV INNATE RESPONSE TO dsRNA, TNF-alpha Signaling |
| + |
RIPK1 | up-regulates activity
binding
|
TRAF6 |
0.647 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216325 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20404851 |
Collectively, TRIF forms a multiprotein signaling complex along with TRAF6, TRADD, Pellino-1 and RIP1 for the activation of TAK1, which in turn activates the NF-_B and MAPK pathways. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Innate Immune Response, Inflammosome Activation, NF-KB Canonical, SARS-CoV INFLAMMATORY RESPONSE |
| + |
RIPK1 | up-regulates activity
binding
|
TAB3 |
0.557 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161787 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19927120 |
Tab2 and tab3 activate the jun n-terminal kinase and nuclear factor-kappab pathways through the specific recognition of lys 63-linked polyubiquitin chains by its npl4 zinc-finger (nzf) domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NF-KB Canonical |
| + |
TICAM1 | up-regulates activity
binding
|
RIPK1 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20404851 |
TRIF also recruits the adaptor RIP1 through the distinct RIP homotypic interaction motif. RIP1 undergoes K63-linked polyubiquitination after stimulation by TLR3 agonists, and this modification is required for NF-_B activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Innate Immune Response, Inflammosome Activation, Macrophage polarization, SARS-CoV INFLAMMATORY RESPONSE, SARS-CoV INNATE RESPONSE TO dsRNA |
| + |
RIPK1 | up-regulates activity
binding
|
MAP3K7 |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256022 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21133840 |
RIP-1 recruitment of MEKK-3 and transforming growth factor-beta (TGFbeta)-activated kinase (TAK1) subsequently activates the IKK (inhibitor of κB kinase) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inflammosome Activation, NF-KB Canonical, P38 Signaling and Myogenesis, SAPK/JNK Signaling, SARS-CoV INFLAMMATORY RESPONSE |
| + |
BIRC3 | down-regulates quantity by destabilization
polyubiquitination
|
RIPK1 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272637 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 18570872 |
In this report, we show that cIAP1 and cIAP2 promote cancer cell survival by functioning as E3 ubiquitin ligases that maintain constitutive ubiquitination of the RIP1 adaptor protein. We demonstrate that AEG40730, a compound modeled on BIR-binding tetrapeptides, binds to cIAP1 and cIAP2, facilitates their autoubiquitination and proteosomal degradation, and causes a dramatic reduction in RIP1 ubiquitination. We show that cIAP1 and cIAP2 directly ubiquitinate RIP1 and induce constitutive RIP1 ubiquitination in cancer cells and demonstrate that constitutively ubiquitinated RIP1 associates with the prosurvival kinase TAK1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIPK1 | up-regulates activity
binding
|
FAS |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177949 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18545270 |
The death domain of the rip1 kinase binds to death receptors such as fas that is required for caspase 8 activation and apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, NF-KB Canonical |
| + |
5-(1H-indol-3-ylmethyl)-3-methyl-2-sulfanylidene-4-imidazolidinone | down-regulates
chemical inhibition
|
RIPK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186075 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19524513 |
The interaction between rip1 and rip3 is abolished by the rip1 kinase inhibitor necrostatin-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RIPK1
- 
- 