| + |
PTPN5 | up-regulates activity 
dephosphorylation
|
BAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248542 |
Tyr108 |
QPTAENAyEYFTKIA |
Homo sapiens |
|
| pmid |
sentence |
| 20959805 |
In this study, we report that on apoptotic stimulation Bak undergoes dephosphorylation at tyrosine residue 108 (Y108), a critical event that is necessary but not sufficient for Bak activation, but is required both for early exposure of the occluded N-terminal domain and multimerisation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAK1 | up-regulates
relocalization
|
AIFM1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23003569 |
First, bax/bak-mediated momp leads to the release of a significant part of the cyt c, smac/diablo and htra2/omi proteins. in a third step, cyt c, smac/diablo and htra2/omi, which were released into the cytosol, trigger caspase activation. This is necessary to alter the physical association of aif and endog with the im to enable their relocation to the cytosol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAK1 | up-regulates 
|
DIABLO |
0.519 |
| 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 |
| + |
BAK1 | up-regulates
|
ENDOG |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86406 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12941691 |
We show that the mitochondrial outer-membrane permeabilization induced by bax-, tbid- or bax/bak-dependent pro-apoptotic drugs results in the release of cytochrome c, smac/diablo and htra2/omi, but that subsequent caspase activation is required to induce the translocation of endog in addition to aif into the cytosol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL2 | down-regulates 
binding
|
BAK1 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152980 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Bax is held in check by mcl1, bcl-2, and either bcl2l1 or bcl2l2, or by all four. They bind a primed conformer of bak or bax bax/bak are kept in check by the pro-survival bcl-2 family members and also proposes that for apoptotic death to occur, all pro-survival bcl-2-like proteins present within a given cell need to be neutralised by bh3-only proteins, thereby derepressing bax/bak |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9463381 |
Bcl-2 bind to bax or five other pro-apoptotic relatives (bak, bad, bik, bid or bim) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML, Malignant Melanoma, Non-small-cell lung cancer (NSCLC) |
| + |
BCL2L11 | up-regulates
binding
|
BAK1 |
0.836 |
| 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 |
| + |
SH3GLB1 | up-regulates
|
BAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141163 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16227588 |
Here, we provide evidence that bif-1 plays a regulatory role in apoptotic activation of not only bax but also bak and appears to be involved in suppression of tumorigenesis. while bif-1 did not directly interact with bak, it heterodimerized with bax on mitochondria in intact cells, and this interaction was enhanced by apoptosis induction and preceded the bax conformational change. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WWTR1 | up-regulates quantity by expression
transcriptional regulation
|
BAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255605 |
|
|
Homo sapiens |
Colorectal Cancer Cell |
| pmid |
sentence |
| 22470139 |
Efficient knockdown of WWTR1, demonstrated by quantitative real-time PCR, led to upregulation of ASNS and downregulation of SMAD3, LTBR, BAX and BAK1 in WWTR1 knockdown cells, suggesting that these genes may be involved in the repression of cell proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL2L1 | down-regulates
binding
|
BAK1 |
0.744 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152983 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Bax is held in check by mcl1, bcl-2, and either bcl2l1 or bcl2l2, or by all four. They bind a primed conformer of bak or bax |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55549 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9463381 |
Bcl-xl bind to bax or five other pro-apoptotic relatives (bak, bad, bik, bid or bim) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Malignant Melanoma |
| + |
TP53 | up-regulates
binding
|
BAK1 |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124122 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15077116 |
P53 interacts with the pro-apoptotic mitochondrial membrane protein bak |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Malignant Melanoma, Non-small-cell lung cancer (NSCLC) |
| + |
BAK1 | up-regulates
binding
|
BAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105203 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11175253 |
Allosteric activation of bak induces its intramembranous oligomerization into a proposed pore for cytochrome c efflux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML, Malignant Melanoma, Non-small-cell lung cancer (NSCLC) |
| + |
BID | up-regulates
binding
|
BAK1 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105210 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11175253 |
Activated tbid results in an allosteric activation of bak |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152992 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
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. these data support a two-class model for bh3 domains: bid-like domains that activate bax, bak and bad-like domains that sensitize by occupying the pocket of antiapoptotic members. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92942 |
|
|
Homo sapiens |
|
| 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. these data support a two-class model for bh3 domains: bid-like domains that activate bax, bak and bad-like domains that sensitize by occupying the pocket of antiapoptotic members. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
BAK1 | up-regulates
relocalization
|
HTRA2 |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118908 |
|
|
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 |
| + |
BAK1 | up-regulates
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261493 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23567751 |
The mitochondrial pathway of apoptosis proceeds when the outer mitochondrial membrane (OMM) is compromised by the pro-apoptotic BCL-2 family members, BAK and BAX. Once activated, BAK and BAX form proteolipid pores in the OMM leading to mitochondrial outer membrane permeabilization (MOMP), and the release of inner membrane space proteins, such as cytochrome c, which promotes caspase activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML, Malignant Melanoma |
| + |
BAK1 | up-regulates
|
HTRA2 |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170966 |
|
|
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 |
| + |
MCL1 | down-regulates
binding
|
BAK1 |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149774 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Bax is held in check by mcl1, bcl-2, and either bcl2l1 or bcl2l2, or by all four. They bind a primed conformer of bak or bax |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
BAK1 | up-regulates
relocalization
|
CYCS |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105206 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11175253 |
Allosteric activation of bak induces its intramembranous oligomerization into a proposed pore for cytochrome c efflux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAK1 | up-regulates
relocalization
|
DIABLO |
0.519 |
| 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 |
| + |
BAK1 | up-regulates
|
CYCS |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160036 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18097445 |
This process of mitochondrial outer membrane permeabilization (momp) results in the release of cycs. It is commonly thought that bax and bak form pores in membranes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BBC3 | up-regulates
binding
|
BAK1 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196929 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22492984 |
Bim, and puma bind with high affinity to all pro-survival proteins |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152974 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Bh3-only proteins induce apoptosis at least primarily by engaging the multiple pro-survival relatives guarding bax and bak enabler bh3-only proteins such as puma promote momp more indirectly. They activate bax and bak by forming inhibitory complexes with the anti-apoptotic bh1-4 proteins such as bcl2, bclxl and mcl1 that normally stabilize the outer membrane. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BCL2L2 | down-regulates
binding
|
BAK1 |
0.465 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152989 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Bax is held in check by mcl1, bcl-2, and either bcl2l1 or bcl2l2, or by all four. They bind a primed conformer of bak or bax. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BAK1
- 
- 