| + |
RIPK3 | up-regulates activity 
phosphorylation
|
MLKL |
0.742 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266439 |
Ser358 |
ELRKTQTsMSLGTTR |
in vitro |
|
| pmid |
sentence |
| 24012422 |
MLKL comprises a four-helical bundle tethered to the pseudokinase domain, which contains an unusual pseudoactive site. Although the pseudokinase domain binds ATP, it is catalytically inactive and its essential nonenzymatic role in necroptotic signaling is induced by receptor-interacting serine-threonine kinase 3 (RIPK3)-mediated phosphorylation.[...]S345, S347, and T349 in the MLKL activation loop were phosphorylated by RIPK3 in in vitro kinase assays |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266427 |
Ser358 |
ELRKTQTsMSLGTTR |
Mus musculus |
|
| pmid |
sentence |
| 24012422 |
MLKL comprises a four-helical bundle tethered to the pseudokinase domain, which contains an unusual pseudoactive site. Although the pseudokinase domain binds ATP, it is catalytically inactive and its essential nonenzymatic role in necroptotic signaling is induced by receptor-interacting serine-threonine kinase 3 (RIPK3)-mediated phosphorylation.[...]S345, S347, and T349 in the MLKL activation loop were phosphorylated by RIPK3 in in vitro kinase assays |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266428 |
Ser360 |
RKTQTSMsLGTTREK |
Mus musculus |
|
| pmid |
sentence |
| 24012422 |
MLKL comprises a four-helical bundle tethered to the pseudokinase domain, which contains an unusual pseudoactive site. Although the pseudokinase domain binds ATP, it is catalytically inactive and its essential nonenzymatic role in necroptotic signaling is induced by receptor-interacting serine-threonine kinase 3 (RIPK3)-mediated phosphorylation.[...]S345, S347, and T349 in the MLKL activation loop were phosphorylated by RIPK3 in in vitro kinase assays |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266440 |
Ser360 |
RKTQTSMsLGTTREK |
in vitro |
|
| pmid |
sentence |
| 24012422 |
MLKL comprises a four-helical bundle tethered to the pseudokinase domain, which contains an unusual pseudoactive site. Although the pseudokinase domain binds ATP, it is catalytically inactive and its essential nonenzymatic role in necroptotic signaling is induced by receptor-interacting serine-threonine kinase 3 (RIPK3)-mediated phosphorylation.[...]S345, S347, and T349 in the MLKL activation loop were phosphorylated by RIPK3 in in vitro kinase assays |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266429 |
Thr357 |
FELRKTQtSMSLGTT |
Mus musculus |
|
| pmid |
sentence |
| 24012422 |
MLKL comprises a four-helical bundle tethered to the pseudokinase domain, which contains an unusual pseudoactive site. Although the pseudokinase domain binds ATP, it is catalytically inactive and its essential nonenzymatic role in necroptotic signaling is induced by receptor-interacting serine-threonine kinase 3 (RIPK3)-mediated phosphorylation.[...]S345, S347, and T349 in the MLKL activation loop were phosphorylated by RIPK3 in in vitro kinase assays |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266438 |
Thr357 |
FELRKTQtSMSLGTT |
in vitro |
|
| pmid |
sentence |
| 24012422 |
MLKL comprises a four-helical bundle tethered to the pseudokinase domain, which contains an unusual pseudoactive site. Although the pseudokinase domain binds ATP, it is catalytically inactive and its essential nonenzymatic role in necroptotic signaling is induced by receptor-interacting serine-threonine kinase 3 (RIPK3)-mediated phosphorylation.[...]S345, S347, and T349 in the MLKL activation loop were phosphorylated by RIPK3 in in vitro kinase assays |
|
| Publications: |
6 |
Organism: |
In Vitro, Mus Musculus |
| + |
RIPK3 | up-regulates activity
phosphorylation
|
DLD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266372 |
Thr135 |
STAVKALtGGIAHLF |
in vitro |
|
| pmid |
sentence |
| 29358703 |
Here, we show that RIP3 activates the pyruvate dehydrogenase complex (PDC, also known as PDH), the rate-limiting enzyme linking glycolysis to aerobic respiration, by directly phosphorylating the PDC E3 subunit (PDC-E3) on T135. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RIPK3 | up-regulates activity
phosphorylation
|
RIPK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277396 |
Thr182 |
GSGEPGGtLGYLAPE |
in vitro |
|
| pmid |
sentence |
| 29883609 |
This suggests that Thr182 is a likely auto-phosphorylation target and may be involved in RIP3 activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Death Receptor Signaling |
| + |
BIRC3 | up-regulates activity
polyubiquitination
|
RIPK3 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272714 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |
| + |
RIPK3 | up-regulates activity
phosphorylation
|
PDH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268065 |
|
|
in vitro |
|
| pmid |
sentence |
| 29358703 |
Here, we show that RIP3 activates the pyruvate dehydrogenase complex (PDC, also known as PDH), the rate-limiting enzyme linking glycolysis to aerobic respiration, by directly phosphorylating the PDC E3 subunit (PDC-E3) on T135. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RIPK3 | up-regulates
binding
|
PYGL |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186939 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19632174 |
Rip3 directly interacts with glycogen phosphorylase (pygl), glutamate ammonia ligase (glul), and glutamate dehydrogenase 1 (glud1). Rip kinase activity is required to enhance the activities of all three enzymes both in vivo and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIPK3 | up-regulates
binding
|
GLUD1 |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19632174 |
Rip3 directly interacts with glycogen phosphorylase (pygl), glutamate ammonia ligase (glul), and glutamate dehydrogenase 1 (glud1). Rip kinase activity is required to enhance the activities of all three enzymes both in vivo and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ponatinib | down-regulates activity 
chemical inhibition
|
RIPK3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261083 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 25801024 |
Discovery of ponatinib as the first-in-class dual inhibitor of RIPK1 and RIPK3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BIRC2 | up-regulates activity
polyubiquitination
|
RIPK3 |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272711 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |
| + |
ZBP1 | up-regulates activity
binding
|
RIPK3 |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266430 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 32200799 |
ZBP1 initiates RIPK3-driven cell death by sensing IAV RNA and activating RIPK3. Here, we show that replicating IAV generates Z-RNAs, which activate ZBP1 in the nucleus of infected cells. ZBP1 then initiates RIPK3-mediated MLKL activation in the nucleus, resulting in nuclear envelope disruption, leakage of DNA into the cytosol, and eventual necroptosis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RIPK3 | up-regulates activity
phosphorylation
|
OGDC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268066 |
|
|
in vitro |
|
| pmid |
sentence |
| 29358703 |
Here, we show that RIP3 activates the pyruvate dehydrogenase complex (PDC, also known as PDH), the rate-limiting enzyme linking glycolysis to aerobic respiration, by directly phosphorylating the PDC E3 subunit (PDC-E3) on T135. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
RIPK3
- 
- 