+ |
AREL1 | down-regulates quantity by destabilization
ubiquitination
|
DIABLO |
0.386 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267672 |
Lys191 |
RNHIQLVkLQVEEVH |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
31732561 |
AREL1 ubiquitinated SMAC, primarily on Lys62 and Lys191 |E701A substitution in the AREL1 HECT domain substantially increased its autopolyubiquitination and SMAC ubiquitination activity, whereas deletion of the last three amino acids at the C terminus completely abrogated AREL1 autoubiquitination and reduced SMAC ubiquitination. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267673 |
Lys62 |
CAVPIAQkSEPHSLS |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
31732561 |
AREL1 ubiquitinated SMAC, primarily on Lys62 and Lys191 |E701A substitution in the AREL1 HECT domain substantially increased its autopolyubiquitination and SMAC ubiquitination activity, whereas deletion of the last three amino acids at the C terminus completely abrogated AREL1 autoubiquitination and reduced SMAC ubiquitination. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267668 |
|
|
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
23479728 |
Furthermore, the ubiquitination and degradation of SMAC, HtrA2, and ARTS were significantly enhanced in AREL1-expressing cells following apoptotic stimulation, indicating that AREL1 binds to and ubiquitinates cytosolic but not mitochondria-associated forms of IAP antagonists| |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
BAK1 | up-regulates
relocalization
|
DIABLO |
0.502 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118905 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Bax and/or bak-mediated release of pro-apoptotic mediators including smac/diablo and omi |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DIABLO | down-regulates
binding
|
XIAP |
0.912 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171770 |
|
|
Homo sapiens |
|
pmid |
sentence |
10929711 |
Smac promotes caspase-9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
HSPB1 | down-regulates
|
DIABLO |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-103539 |
|
|
Homo sapiens |
|
pmid |
sentence |
12855565 |
These data demonstrate that hsp27 inhibits the release of smac |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BCL2 | down-regulates
|
DIABLO |
0.471 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-88885 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Bcl- confers protection to apoptosis by interference with bax/bak-mediated release of the pro-apoptotic mitochodrial factors smac/diablo and htra2/omi |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
MAPK10 | down-regulates
phosphorylation
|
DIABLO |
0.349 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157280 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17686459 |
Here we demonstrate that jnk3 can phosphorylate smac. Phosphorylation of smac by jnk3 attenuates its interaction with xiap. These results suggest that jnk3 activity can attenuate the progression of apoptosis through a novel mechanism of action, the down-regulation of interaction between smac and xiap. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BIRC2 | down-regulates quantity by destabilization
ubiquitination
|
DIABLO |
0.891 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271392 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12525502 |
Here we show that cIAP1 and cIAP2 are E3 ubiquitin-protein isopeptide ligases (ubiquitin ligases) for Smac. cIAPs stimulate Smac ubiquitination both in vivo and in vitro, leading to Smac degradation. cIAP1 and cIAP2 associate with overlapping but distinct subsets of E2 (ubiquitin carrier protein) ubiquitin-conjugating enzymes. The substrate-dependent E3 activity of cIAPs is mediated by their RING domains and is dependent on the specific interactions between cIAPs and Smac. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BAX | up-regulates
|
DIABLO |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170969 |
|
|
Homo sapiens |
|
pmid |
sentence |
21210296 |
Permeabilization of the outer mitochondrial membrane allows the leakage of at least five apoptotic mediators from the mitochondrial intermembrane space, such as cyt c,(diablo/diablo), htra2/omi, apoptosis-inducing factors (aif), and endonuclease g. Such modifications result in their activation and translocation to outer mitochondrial membrane (omm) which helps it to interact with multidomain pro-apototic members, bax/baklike proteins, leading to their oligomerization and formation of pore. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
DIABLO | down-regulates activity
binding
|
BIRC3 |
0.785 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80225 |
|
|
Homo sapiens |
HEK-293 Cell, NTERA-2 Cell |
pmid |
sentence |
10929712 |
Diablo may promote apoptosis by binding to iaps and preventing them from inhibiting caspases. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80209 |
|
|
Homo sapiens |
HEK-293 Cell, NTERA-2 Cell |
pmid |
sentence |
10929711 |
Smac promotes caspase-9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
XIAP | down-regulates quantity by destabilization
ubiquitination
|
DIABLO |
0.912 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134504 |
|
|
in vitro |
|
pmid |
sentence |
15749826 |
Xiap functions as ubiquitin ligase toward smac to inhibit apoptosis. |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | Death Receptor Signaling |
+ |
BIRC3 | down-regulates quantity by destabilization
ubiquitination
|
DIABLO |
0.785 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271391 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12525502 |
Here we show that cIAP1 and cIAP2 are E3 ubiquitin-protein isopeptide ligases (ubiquitin ligases) for Smac. cIAPs stimulate Smac ubiquitination both in vivo and in vitro, leading to Smac degradation. cIAP1 and cIAP2 associate with overlapping but distinct subsets of E2 (ubiquitin carrier protein) ubiquitin-conjugating enzymes. The substrate-dependent E3 activity of cIAPs is mediated by their RING domains and is dependent on the specific interactions between cIAPs and Smac. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DIABLO | down-regulates
binding
|
BIRC5 |
0.586 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80212 |
|
|
Homo sapiens |
|
pmid |
sentence |
10929711 |
Diablo seem to function as a general iaps neutralizer by binding to these protein. Diablo promotes casp9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. mitochondrial survivin associated with smac/diablo, delaying its release. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155364 |
|
|
Homo sapiens |
|
pmid |
sentence |
17546047 |
Diablo seem to function as a general iaps neutralizer by binding to these protein. Diablo promotes casp9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. mitochondrial survivin associated with smac/diablo, delaying its release. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
DIABLO | down-regulates quantity
binding
|
BIRC3 |
0.785 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-121886 |
|
|
Homo sapiens |
|
pmid |
sentence |
14960576 |
Smac/diablo selectively causes the rapid degradation of c-iap1 and c-iap2 in hela cells. Smac binding to c-iap via its n-terminal iap-binding motif is the prerequisite for this effect |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DIABLO | down-regulates quantity
binding
|
BIRC2 |
0.891 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-121883 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14960576 |
Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80206 |
|
|
in vitro |
|
pmid |
sentence |
10929711 |
Smac promotes caspase-9 activation by binding to inhibitor of apoptosis proteins, IAPs, and removing their inhibitory activity. Smac is normally a mitochondrial protein but is released into the cytosol when cells undergo apoptosis. |
|
Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
+ |
BIRC7 | down-regulates
binding
|
DIABLO |
0.688 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129869 |
|
|
Homo sapiens |
Melanoma Cell |
pmid |
sentence |
15485396 |
These results suggest that ml-iap might regulate apoptosis by sequestering smac and preventing it from antagonizing xiap-mediated caspases, rather than by direct caspases. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DIABLO | up-regulates
|
CASP9 |
0.726 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80215 |
|
|
Homo sapiens |
|
pmid |
sentence |
10929711 |
Smac promotes caspase-9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
DIABLO | down-regulates activity
binding
|
XIAP |
0.912 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80218 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10929711 |
Smac promotes caspase-9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110831 |
|
|
Homo sapiens |
HEK-293 Cell, HeLa Cell |
pmid |
sentence |
11583623 |
Smac/diablo, an inhibitor of xiap, is released from mitochondria upon receiving apoptotic stimuli and binds to the bir2 and bir3 domains of xiap, thereby inhibiting its caspase-inhibitory activity |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
BAX | up-regulates
relocalization
|
DIABLO |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87109 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Bax and/or bak-mediated release of pro-apoptotic mediators including smac/diablo and omi |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
DIABLO | down-regulates quantity
binding
|
XIAP |
0.912 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118411 |
|
|
Homo sapiens |
HEK-293 Cell, HeLa Cell |
pmid |
sentence |
14523016 |
Smac3, a novel Smac/DIABLO splicing variant, accelerates XIAP auto-ubiquitination and destruction |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
BIRC5 | down-regulates
binding
|
DIABLO |
0.586 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155361 |
|
|
Homo sapiens |
|
pmid |
sentence |
17546047 |
Mitochondrial survivin associated with smac/diablo, delaying its release. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BAK1 | up-regulates
|
DIABLO |
0.502 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170963 |
|
|
Homo sapiens |
|
pmid |
sentence |
21210296 |
Permeabilization of the outer mitochondrial membrane allows the leakage of at least five apoptotic mediators from the mitochondrial intermembrane space, such as cyt c, (diablo/diablo), htra2/omi, apoptosis-inducing factors (aif), and endonuclease g. Such modifications result in their activation and translocation to outer mitochondrial membrane (omm) which helps it to interact with multidomain pro-apototic members, bax/baklike proteins, leading to their oligomerization and formation of pore. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DIABLO | down-regulates activity
binding
|
BIRC2 |
0.891 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-80222 |
|
|
Homo sapiens |
HEK-293 Cell, NTERA-2 Cell |
pmid |
sentence |
10929712 |
Diablo seem to function as a general iaps neutralizer by binding to these protein. Diablo promotes casp9 activation by binding to inhibitor of apoptosis proteins, iaps, and removing their inhibitory activity. ciap1 and ciap2 undergo autoubiquitination and degradation upon binding to the iap antagonist second mitochondrial activator of caspases (smac)/direct iap-binding protein with low pi (diablo), which is released from the mitochondria. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |