+ |
AKT2 | up-regulates
phosphorylation
|
XIAP |
0.43 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119492 |
Ser87 |
VGRHRKVsPNCRFIN |
Homo sapiens |
|
pmid |
sentence |
14645242 |
Here, we demonstrate that akt, including akt1 and akt2, interacts with and phosphorylates x-linked inhibitor of apoptosis protein (xiap) at residue serine-87 in vitro and in vivo. Phosphorylation of xiap by akt protects xiap from ubiquitination and degradation in response to cisplatin. Moreover, autoubiquitination of xiap is also inhibited by akt. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT | up-regulates quantity by stabilization
phosphorylation
|
XIAP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244377 |
Ser87 |
VGRHRKVsPNCRFIN |
Homo sapiens |
|
pmid |
sentence |
14645242 |
Akt, including akt1 and akt2, interacts with and phosphorylates x-linked inhibitor of apoptosis protein (xiap) at residue serine-87 in vitro and in vivo. Phosphorylation of xiap by akt protects xiap from ubiquitination and degradation in response to cisplatin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Ovary Cancer Cell |
Pathways: | Inhibition of Apoptosis |
+ |
AKT1 | up-regulates quantity by stabilization
phosphorylation
|
XIAP |
0.638 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119488 |
Ser87 |
VGRHRKVsPNCRFIN |
Homo sapiens |
|
pmid |
sentence |
14645242 |
Akt, including akt1 and akt2, interacts with and phosphorylates x-linked inhibitor of apoptosis protein (xiap) at residue serine-87 in vitro and in vivo. Phosphorylation of xiap by akt protects xiap from ubiquitination and degradation in response to cisplatin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Ovary Cancer Cell |
Pathways: | Parkinson |
+ |
GSK3B | up-regulates activity
phosphorylation
|
XIAP |
0.403 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277390 |
Thr180 |
WPDYAHLtPRELASA |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
29678905 |
We now demonstrate that XIAP is phosphorylated by GSK3 at threonine 180, and that an alanine mutant (XIAPT180A) exhibits decreased Wnt activity compared to wild-type XIAP in cultured human cells and in Xenopus embryos. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BIRC5 | up-regulates
binding
|
XIAP |
0.509 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-126367 |
|
|
Homo sapiens |
|
pmid |
sentence |
15218035 |
Formation of a survivin-xiap complex promotes increased xiap stability against ubiquitination/proteasomal destruction and synergistic apoptosis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HTRA2 | down-regulates
binding
|
XIAP |
0.702 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110834 |
|
|
Homo sapiens |
|
pmid |
sentence |
11583623 |
Here we report that a serine protease called htra2/omi is released from mitochondria and inhibits the function of xiap by direct binding in a similar way to diablo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Parkinson |
+ |
XIAP | down-regulates activity
binding
|
CASP3 |
0.938 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110837 |
|
|
Homo sapiens |
|
pmid |
sentence |
11583623 |
Xiap is an endogenous inhibitor of caspase-3 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71954 |
|
|
Homo sapiens |
|
pmid |
sentence |
10548111 |
The linker region located adjacent to the bir2 domain also participates in the binding of xiap to the effector caspases (-3 and -7). |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling, Inhibition of Apoptosis, Parkinson |
+ |
XIAP | down-regulates quantity by destabilization
binding
|
CASP9 |
0.92 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98988 |
|
|
in vitro |
|
pmid |
sentence |
12620238 |
This paper reports the crystal structure of caspase-9 in an inhibitory complex with the third baculoviral iap repeat (bir3) of xiap at 2.4 a resolution. X-linked inhibitor-of-apoptosis protein (xiap) interacts with caspase-9 and inhibits its activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-56484 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
9545235 |
IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspasesThese findings demonstrate that IAPs can suppress different apoptotic pathways by inhibiting distinct caspases and identify pro-caspase-9 as a new target for IAP-mediated inhibition of apoptosis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105702 |
|
|
Homo sapiens |
|
pmid |
sentence |
11242052 |
A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis |
|
Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
Pathways: | Death Receptor Signaling, Inhibition of Apoptosis, Parkinson |
+ |
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 |
+ |
embelin | down-regulates activity
chemical inhibition
|
XIAP |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262013 |
|
|
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
28704451 |
Targeting of X-linked inhibitor of apoptosis protein and PI3-kinase/AKT signaling by embelin suppresses growth of leukemic cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
XIAP | up-regulates activity
polyubiquitination
|
RIPK4 |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272716 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21931591 |
In this study, we report that in addition to RIP1 and RIP2, also RIP3 and RIP4 directly interact with XIAP, cIAP1 and cIAP2. When comparing the ability of these IAPs to directly conjugate RIP1–RIP4 with ubiquitin chains, we found that cIAP1 was the most effective E3 and was capable of ubiquitinating all four RIPs in the presence of the E2 component UbcH5a. On the contrary, XIAP was only capable of inducing weak ubiquitination of RIP4. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |
+ |
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 |
+ |
XAF1 | down-regulates
binding
|
XIAP |
0.576 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155637 |
|
|
Homo sapiens |
|
pmid |
sentence |
17613533 |
Immunoprecipitation studies indicate that xaf1 binds to xiap,birc2,birc3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
XIAP | down-regulates quantity by destabilization
binding
|
CASP7 |
0.854 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110840 |
|
|
in vitro |
|
pmid |
sentence |
11583623 |
Xiap is an endogenous inhibitor of caspase-7 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105732 |
|
|
in vitro |
|
pmid |
sentence |
11257231 |
Our crystal structure of the complex between xiap (linker-bir2) and caspase-7 surprisingly revealed that the linker is the major determinant of binding and inhibition for the caspase. |
|
Publications: |
2 |
Organism: |
In Vitro |
Pathways: | Inhibition of Apoptosis |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
XIAP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271045 |
|
|
Homo sapiens |
|
pmid |
sentence |
34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
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 |
+ |
XIAP | down-regulates quantity by destabilization
ubiquitination
|
CASP3 |
0.938 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109243 |
|
|
Homo sapiens |
|
pmid |
sentence |
11447297 |
Xiap promotes the degradation of active-form caspase-3, but not procaspase-3, in living cells. Both the association of XIAP with caspase-3 and the RING finger domain of XIAP were essential for ubiquitination. XIAP promotes the degradation of caspase-3, which enhances its anti-apoptotic effect. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling, Inhibition of Apoptosis, Parkinson |
+ |
SEPTIN4 | down-regulates quantity
binding
|
XIAP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267671 |
|
|
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
15029247 |
The mitochondrial ARTS protein promotes apoptosis through targeting XIAP.|Binding of ARTS to XIAP is direct, as recombinant ARTS and XIAP proteins can bind to each other in vitro. ARTS binding to XIAP is specific and related to its pro-apoptotic function, as mutant forms of ARTS (or related septins) that fail to bind XIAP failed to induce apoptosis. ARTS leads to decreased XIAP protein levels and caspase activation. Our data suggest that ARTS induces apoptosis by antagonizing IAPs. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |