| + |
EGLN3 | up-regulates quantity by stabilization 
hydroxylation
|
BCL2L11 (isoform 1) |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262003 |
Pro67 |
PQGPLAPpASPGPFA |
Homo sapiens |
|
| pmid |
sentence |
| 31375625 |
EglN3 hydroxylase stabilizes BIM-EL linking VHL type 2C mutations to pheochromocytoma pathogenesis and chemotherapy resistance|EglN3 Hydroxylates BIM-EL at the Proline67/70 Residues |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262004 |
Pro70 |
PLAPPASpGPFATRS |
Homo sapiens |
|
| pmid |
sentence |
| 31375625 |
EglN3 hydroxylase stabilizes BIM-EL linking VHL type 2C mutations to pheochromocytoma pathogenesis and chemotherapy resistance|EglN3 Hydroxylates BIM-EL at the Proline67/70 Residues |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
JNK | up-regulates
phosphorylation
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98384 |
Ser104 |
FSFDTDRsPAPMSCD |
Homo sapiens |
|
| pmid |
sentence |
| 12591950 |
Biml (bim long) was induced and phosphorylated parallel to jnk activitythese data demonstrate that biml is phosphorylated in vivo on thr-56 and that jnk also phosphorylates biml on at least one serine residue (ser-44 and/or ser-58) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98388 |
Ser118 |
DKSTQTPsPPCQAFN |
Homo sapiens |
|
| pmid |
sentence |
| 12591950 |
Biml (bim long) was induced and phosphorylated parallel to jnk activitythese data demonstrate that biml is phosphorylated in vivo on thr-56 and that jnk also phosphorylates biml on at least one serine residue (ser-44 and/or ser-58) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98392 |
Thr116 |
SCDKSTQtPSPPCQA |
Homo sapiens |
|
| pmid |
sentence |
| 12591950 |
Biml (bim long) was induced and phosphorylated parallel to jnk activitythese data demonstrate that biml is phosphorylated in vivo on thr-56 and that jnk also phosphorylates biml on at least one serine residue (ser-44 and/or ser-58) |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
CDK1 | up-regulates activity
phosphorylation
|
BCL2L11 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267985 |
Ser104 |
FSFDTDRsPAPMSCD |
Homo sapiens |
|
| pmid |
sentence |
| 22071694 |
Furthermore, active recombinant Cdk1/cyclin B1 phosphorylates BimEL and BimL in vitro and Serine 44 on BimL has been identified as a Cdk1 phosphorylation site. Collectively, these results suggest that Cdk1/cyclin B1-dependent hyper-phosphorylation of Bim during prolonged mitotic arrest is an important cell death signal. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK10 | up-regulates activity
phosphorylation
|
BCL2L11 |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250130 |
Ser59 |
GDSCPHGsPQGPLAP |
Mus musculus |
|
| pmid |
sentence |
| 12818176 |
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250131 |
Ser77 |
PGPFATRsPLFIFMR |
Mus musculus |
|
| pmid |
sentence |
| 12818176 |
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
MAPK9 | up-regulates activity
phosphorylation
|
BCL2L11 |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250134 |
Ser59 |
GDSCPHGsPQGPLAP |
|
|
| pmid |
sentence |
| 12818176 |
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250135 |
Ser77 |
PGPFATRsPLFIFMR |
|
|
| pmid |
sentence |
| 12818176 |
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity. |
|
| Publications: |
2 |
| + |
MAPK8 | down-regulates quantity by destabilization 
phosphorylation
|
BCL2L11 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160323 |
Ser69 |
GPLAPPAsPGPFATR |
Homo sapiens |
|
| pmid |
sentence |
| 18174237 |
Constitutive activation of the c-jun n-terminal kinase (jnk) pathway in sup-t1 cells promoted phosphorylation and degradation of bimel via the proteosome. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250132 |
Ser69 |
GPLAPPAsPGPFATR |
Mus musculus |
|
| pmid |
sentence |
| 15486195 |
Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | COVID-19 Causal Network, SAPK/JNK Signaling |
| + |
MAPK1 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.705 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129874 |
Ser69 |
GPLAPPAsPGPFATR |
Homo sapiens |
|
| pmid |
sentence |
| 15486195 |
In vitro, bimel was phosphorylated by extracellular signal-regulated kinase on ser(69), which resides in the bimel-specific insert region. Using phosphospecific antibody against this site, we show that this residue is actually phosphorylated in cells. We also show that phosphorylation of ser(69) promotes ubiquitination of bimel. We conclude that mek inhibitors sensitize mda-mb231 and hbc4 cells to anoikis by blocking phosphorylation and hence degradation of bimel |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141584 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16282323 |
Erk phosphorylation serves as a signal for bim ubiquitination and proteasomal degradation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK10 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250080 |
Ser69 |
GPLAPPAsPGPFATR |
in vitro |
|
| pmid |
sentence |
| 15486195 |
Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPK14 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260442 |
Ser69 |
GPLAPPAsPGPFATR |
Rattus norvegicus |
|
| pmid |
sentence |
| 15486195 |
Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
MAPK9 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250136 |
Ser69 |
GPLAPPAsPGPFATR |
|
|
| pmid |
sentence |
| 18174237 |
Constitutive activation of the c-jun n-terminal kinase (jnk) pathway in sup-t1 cells promoted phosphorylation and degradation of bimel via the proteosome. |
|
| Publications: |
1 |
| + |
p38 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260443 |
Ser69 |
GPLAPPAsPGPFATR |
Rattus norvegicus |
|
| pmid |
sentence |
| 15486195 |
Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS |
| + |
MAPK3 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129878 |
Ser69 |
GPLAPPAsPGPFATR |
Homo sapiens |
|
| pmid |
sentence |
| 15486195 |
In vitro, bimel was phosphorylated by extracellular signal-regulated kinase on ser(69), which resides in the bimel-specific insert region. Using phosphospecific antibody against this site, we show that this residue is actually phosphorylated in cells. We also show that phosphorylation of ser(69) promotes ubiquitination of bimel. We conclude that mek inhibitors sensitize mda-mb231 and hbc4 cells to anoikis by blocking phosphorylation and hence degradation of bimel |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | up-regulates activity
phosphorylation
|
BCL2L11 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250133 |
Ser77 |
PGPFATRsPLFIFMR |
Mus musculus |
|
| pmid |
sentence |
| 12818176 |
Mitochondrially localized JNKs but not their upstream activators MLKs or MKKs phosphorylated BIMEL at Ser65, potentiating its cytotoxicity without altering its subcellular distribution or integration into mitochondrial membranes. JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, SAPK/JNK Signaling |
| + |
AKT1 | down-regulates activity
phosphorylation
|
BCL2L11 |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252487 |
Ser87 |
FIFMRRSsLLSRSSS |
Homo sapiens |
|
| pmid |
sentence |
| 16282323 |
Recombinant Akt could directly phosphorylate a GST-Bim(EL) fusion protein and identified the Akt phosphorylation site in the Bim(EL) domain as Ser(87). Further, we demonstrated that cytokine stimulation promotes Bim(EL) binding to 14-3-3 proteins. Finally, we show that mutation of Ser(87) dramatically increases the apoptotic potency of Bim(EL). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT | down-regulates activity
phosphorylation
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141581 |
Ser87 |
FIFMRRSsLLSRSSS |
Homo sapiens |
|
| pmid |
sentence |
| 16282323 |
Recombinant Akt could directly phosphorylate a GST-Bim(EL) fusion protein and identified the Akt phosphorylation site in the Bim(EL) domain as Ser(87). Further, we demonstrated that cytokine stimulation promotes Bim(EL) binding to 14-3-3 proteins. Finally, we show that mutation of Ser(87) dramatically increases the apoptotic potency of Bim(EL). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, SARS-COV APOPTOSIS |
| + |
AURKA | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276247 |
Ser93 |
SSLLSRSsSGYFSFD |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23912711 |
We observed that BimEL is phosphorylated by Aurora A early in mitosis and reversed by PP2A after mitotic exit. Aurora A phosphorylation stimulated binding of BimEL to the F-box protein beta-transducin repeat containing E3 ubiquitin protein ligase and promoted ubiquitination and degradation of BimEL. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276248 |
Ser94 |
SLLSRSSsGYFSFDT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23912711 |
We observed that BimEL is phosphorylated by Aurora A early in mitosis and reversed by PP2A after mitotic exit. Aurora A phosphorylation stimulated binding of BimEL to the F-box protein beta-transducin repeat containing E3 ubiquitin protein ligase and promoted ubiquitination and degradation of BimEL. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276246 |
Ser98 |
RSSSGYFsFDTDRSP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23912711 |
We observed that BimEL is phosphorylated by Aurora A early in mitosis and reversed by PP2A after mitotic exit. Aurora A phosphorylation stimulated binding of BimEL to the F-box protein beta-transducin repeat containing E3 ubiquitin protein ligase and promoted ubiquitination and degradation of BimEL. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | up-regulates
phosphorylation
|
BCL2L11 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98396 |
Thr116 |
SCDKSTQtPSPPCQA |
Homo sapiens |
|
| pmid |
sentence |
| 12591950 |
Here, we demonstrate that jnk phosphorylates two members of the bh3-only subgroup of bcl2-related proteins (bim and bmf) that are normally sequestered by binding to dynein and myosin v motor complexes. Phosphorylation by jnk causes release from the motor complexes |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178686 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18498746 |
Jnk phosphorylates two members of the bh3-only sub of bcl2-related proteins (bim and bmf). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98399 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12591950 |
Jnk phosphorylates two members of the bh3-only sub of bcl2-related proteins (bim and bmf). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SAPK/JNK Signaling |
| + |
MAPK10 | up-regulates
phosphorylation
|
BCL2L11 |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178683 |
Thr116 |
SCDKSTQtPSPPCQA |
Homo sapiens |
|
| pmid |
sentence |
| 18498746 |
Jnk is the physiogically relevant uv-stimulated kinase that phosphorylates bimel on thr-112/jnk-induced bim apoptotic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXO3 | down-regulates quantity by repression 
transcriptional regulation
|
BCL2L11 |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261528 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 14981546 |
Induction of Foxo3a phosphorylation by FLT3-ITD receptors in Ba/F3 cells correlates with the suppression of Foxo-target genes p27Kip1 and the proapoptotic Bcl-2 family member Bim |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Inhibition of Apoptosis |
| + |
ER stress | up-regulates 
|
BCL2L11 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196941 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22492984 |
Exposure to stress results in the induction of bh3-only proteins, which neutralise the pro-survival proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
BCL2L11 | up-regulates activity
binding
|
BAX |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152986 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Contrary to the direct-activation model, we show that Bax and Bak can mediate apoptosis without discernable association with the putative BH3-only activators (Bim, Bid, and Puma), even in cells with no Bim or Bid and reduced Puma. Our results indicate that BH3-only proteins induce apoptosis at least primarily by engaging the multiple pro-survival relatives guarding Bax and Bak |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92939 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12242151 |
We find short peptides representing the alpha-helical BH3 domains of BID or BIM are capable of inducing oligomerization of BAK and BAX to release cytochrome c. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87280 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11997495 |
We have shown that the interaction of the bims and bimad isoforms with bax leads to a conformational change in this protein analogous to that triggered by the bh3-only protein bid.We find short peptides representing the alpha-helical bh3 domains of bid or bim are capable of inducing oligomerization of bak and bax to release cytochrome. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196935 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22492984 |
Bim, and puma bind with high affinity to all pro-survival proteins |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SAPK/JNK Signaling, SARS-COV APOPTOSIS |
| + |
BCL2L11 | down-regulates activity
binding
|
BCL2 |
0.811 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178676 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18498746 |
We show that mutation of the phosphorylation site Thr-112 causes decreased binding of Bim to the antiapoptotic protein Bcl2 and can increase cell survival. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133820 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15694340 |
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove on the Bcl-2-like proteins. These interactions have been considered promiscuous, but our analysis of the affinity of eight BH3 peptides for five Bcl-2-like proteins has revealed that the interactions vary over 10,000-fold in affinity, and accordingly, only certain protein pairs associate inside cells. Bim and Puma potently engaged all the prosurvival proteins comparably. Bad, however, bound tightly to Bcl-2, Bcl-xL, and Bcl-w but only weakly to A1 and not to Mcl-1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
FOXO3 | up-regulates quantity by expression
transcriptional regulation
|
BCL2L11 |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209657 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12913110 |
In addition, we find that FKHRL1 (FOXO3a) directly activates the bim promoter via two conserved FOXO binding sites and that mutation of these sites abolishes bim promoter activation after NGF withdrawal. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis |
| + |
BCL2L11 | down-regulates activity
binding
|
BCL2L1 |
0.955 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178679 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18498746 |
Bim can induce apoptosis by interacting with anti-apoptotic members of the bcl2 family, including bcl2, bcl-xl and mcl-1.Bim binds bcl-2, bcl2l1, bcl2l2, mcl1 and a1 tightly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
BCL2L11 | down-regulates
binding
|
BCL2 |
0.811 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133823 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15694340 |
Bim can induce apoptosis by interacting with anti-apoptotic members of the bcl2 family, including bcl2, bcl-xl and mcl-1.. Bim binds prosurvival proteins comparably. The members that promote cell survival, including mammalian bcl-2, bcl-xl,bcl-w, mcl-1, and a1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
Gbeta | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270031 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15486195 |
In vitro, bimel was phosphorylated by extracellular signal-regulated kinase on ser(69), which resides in the bimel-specific insert region. Using phosphospecific antibody against this site, we show that this residue is actually phosphorylated in cells. We also show that phosphorylation of ser(69) promotes ubiquitination of bimel. We conclude that mek inhibitors sensitize mda-mb231 and hbc4 cells to anoikis by blocking phosphorylation and hence degradation of bimel |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL2L11 | down-regulates
binding
|
BCL2L2 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133832 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15694340 |
Bim binds prosurvival proteins comparably. The members that promote cell survival, including mammalian bcl-2, bcl-xl,bcl-w, mcl-1, and a1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | up-regulates activity
dephosphorylation
|
BCL2L11 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21984578 |
Moreover, it indicates that PTPN2 modulates the apoptotic activity of Bim via regulation of the protein kinase JNK1.|PTPN2 inhibition increased Bim phosphorylation at residue 65 in untreated INS-1E cells, and this effect was prolonged until 4 h of treatment with IFNalpha or 8 h after treatment with IFNgamma (XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
14-3-3 | down-regulates
binding
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141577 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16282323 |
Cytokine stimulation promotes bim(el) binding to 14-3-3 proteins. Akt could directly phosphorylate a gst-bim(el) fusion protein and identified the akt phosphorylation site in the bim(el) domain as ser(87). we propose that ser87 of bimel is an important regulatory site that is targeted byakt to attenuate thepro-apoptotic function of bim el, thereby promoting cell survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL2L11 | down-regulates
binding
|
BCL2L1 |
0.955 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133829 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15694340 |
Bim can induce apoptosis by interacting with anti-apoptotic members of the bcl2 family, including bcl2, bcl-xl and mcl-1.Bim binds bcl-2, bcl2l1, bcl2l2, mcl1 and a1 tightly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
BCL2L11 | up-regulates
binding
|
BAK1 |
0.83 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196932 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22492984 |
Bim, and puma bind with high affinity to all pro-survival proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD3/SMAD4 | up-regulates quantity by expression
transcriptional regulation
|
BCL2L11 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260425 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17960585 |
Transforming growth factor-beta (TGF-beta) signaling is known to depend on the formation of Smad2/3-Smad4 transcription regulatory complexes. Functional analysis revealed that Smad3 and Smad4 were the predominant mediators of TGF-beta-induced apoptosis in Hep3B cells. We provide evidence that up-regulation of Bcl-2-interacting mediator of cell death (Bim), under the transcriptional control of Smad3-Smad4 signaling, is crucial to TGF-beta-induced apoptosis in Hep3B cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS |
| + |
BCL2L11 | up-regulates
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260426 |
|
|
Homo sapiens |
HEP-3B Cell |
| pmid |
sentence |
| 17960585 |
Transforming growth factor-beta (TGF-beta) signaling is known to depend on the formation of Smad2/3-Smad4 transcription regulatory complexes. Functional analysis revealed that Smad3 and Smad4 were the predominant mediators of TGF-beta-induced apoptosis in Hep3B cells. We provide evidence that up-regulation of Bcl-2-interacting mediator of cell death (Bim), under the transcriptional control of Smad3-Smad4 signaling, is crucial to TGF-beta-induced apoptosis in Hep3B cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Fibrosis, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, SARS-CoV FIBROSIS |
| + |
ERK1/2 | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270152 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15486195 |
In vitro, bimel was phosphorylated by extracellular signal-regulated kinase on ser(69), which resides in the bimel-specific insert region. Using phosphospecific antibody against this site, we show that this residue is actually phosphorylated in cells. We also show that phosphorylation of ser(69) promotes ubiquitination of bimel. We conclude that mek inhibitors sensitize mda-mb231 and hbc4 cells to anoikis by blocking phosphorylation and hence degradation of bimel |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis |
| + |
MAPK8 | down-regulates
phosphorylation
|
BCL2L11 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160326 |
|
|
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 18174237 |
Constitutive activation of the c-jun n-terminal kinase (jnk) pathway in sup-t1 cells promoted phosphorylation and degradation of bimel via the proteosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SAPK/JNK Signaling |
| + |
FLT3 | down-regulates quantity by repression
transcriptional regulation
|
BCL2L11 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261525 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 14981546 |
FLT3-ITD signaling contributes to transcriptional inhibition of p27Kip1 and Bim gene expression |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
BCL2L11 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209654 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12913110 |
FOXO transcription factors directly activate bim gene expression and promote apoptosis in sympathetic neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis |
| + |
FOXO | up-regulates quantity by expression
transcriptional regulation
|
BCL2L11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252914 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12913110 |
FOXO transcription factors directly activate bim gene expression and promote apoptosis in sympathetic neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BCL2L11
- 
- 