+ |
MLKL | down-regulates quantity by destabilization
phosphorylation
|
CNR2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274121 |
Ser352 |
KITPWPDsRDLDLSD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10400664; 36448459 |
Under hyperglycemic conditions, high glucose induced CB2R internalization in a β-arrestin 2-dependent manner; thereafter, MLKL (mixed lineage kinase domain-like), but not receptor-interacting protein kinase 1 or 3, phosphorylated CB2R at serine 352 and promoted CB2R degradation by ubiquitin modification. CB2R transcriptionally repressed necroptosis through interaction with BACH2; in turn, MLKL formed a negative feedback to phosphorylate CB2R. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RIPK3 | up-regulates activity
phosphorylation
|
MLKL |
0.742 |
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-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-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-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 |
|
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 |
|
Publications: |
6 |
Organism: |
Mus Musculus, In Vitro |
+ |
MERTK | up-regulates quantity by stabilization
phosphorylation
|
MLKL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274118 |
Tyr376 |
DRVKSTAyLSPQELE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
31230815 |
TAM kinases phosphorylate MLKL to promote necroptosis. MLKL is then recruited to the plasma membrane, where TAM kinases phosphorylate MLKL at Tyr376 (Figure 5G, step 5), promoting its oligomerization and formation of membrane-rupturing pores that result in necrotic cell death (Figure 5G, step 6). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TYRO3 | up-regulates quantity by stabilization
phosphorylation
|
MLKL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274120 |
Tyr376 |
DRVKSTAyLSPQELE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
31230815 |
TAM kinases phosphorylate MLKL to promote necroptosis. MLKL is then recruited to the plasma membrane, where TAM kinases phosphorylate MLKL at Tyr376 (Figure 5G, step 5), promoting its oligomerization and formation of membrane-rupturing pores that result in necrotic cell death (Figure 5G, step 6). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXL | up-regulates quantity by stabilization
phosphorylation
|
MLKL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274119 |
Tyr376 |
DRVKSTAyLSPQELE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
31230815 |
TAM kinases phosphorylate MLKL to promote necroptosis. MLKL is then recruited to the plasma membrane, where TAM kinases phosphorylate MLKL at Tyr376 (Figure 5G, step 5), promoting its oligomerization and formation of membrane-rupturing pores that result in necrotic cell death (Figure 5G, step 6). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MLKL | up-regulates activity
|
Necroptosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266431 |
|
|
Homo sapiens |
|
pmid |
sentence |
24316671 |
Here, we report that MLKL forms a homotrimer through its amino-terminal coiled-coil domain and locates to the cell plasma membrane during TNF-induced necroptosis. By generating different MLKL mutants, we demonstrated that the plasma membrane localization of trimerized MLKL is critical for mediating necroptosis. Importantly, we found that the membrane localization of MLKL is essential for Ca(2+) influx, which is an early event of TNF-induced necroptosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |