+ |
NEK1 | down-regulates
phosphorylation
|
VDAC1 |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164222 |
Ser193 |
DGTEFGGsIYQKVNK |
Homo sapiens |
|
pmid |
sentence |
20230784 |
Nek1 phosphorylates vdac1 on ser193. Wild-type vdac1 assumes an open configuration, but closes and prevents cytochrome c efflux when phosphorylated by nek1. A vdac1-ser193ala mutant, which cannot be phosphorylated by nek1 under identical conditions, remains open and constitutively allows cytochrome c efflux. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BCL2L1 | down-regulates activity
binding
|
VDAC1 |
0.584 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249614 |
|
|
|
|
pmid |
sentence |
10365962 |
The anti-apoptotic protein Bcl-x(L) closes VDAC by binding to it directly |
|
Publications: |
1 |
+ |
BAX | up-regulates activity
binding
|
VDAC1 |
0.574 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249613 |
|
|
|
|
pmid |
sentence |
10365962 |
The recombinant pro-apoptotic proteins Bax and Bak accelerate the opening of VDAC |
|
Publications: |
1 |
+ |
SOD1 | down-regulates activity
binding
|
VDAC1 |
0.437 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262798 |
|
|
Mus musculus |
|
pmid |
sentence |
20797535 |
Misfolded Mutant SOD1 Directly Inhibits VDAC1 Conductance in a Mouse Model of Inherited ALS|With conformation-specific antibodies, we now demonstrate that misfolded mutant SOD1 binds directly to the voltage-dependent anion channel (VDAC1), an integral membrane protein imbedded in the outer mitochondrial membrane. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Spinal Cord |
+ |
FAM162A | up-regulates activity
binding
|
VDAC1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260293 |
|
|
Homo sapiens |
PC-3 Cell |
pmid |
sentence |
15082785 |
HGTD-P was coprecipitated with VDAC but not with ANT or cyclophilin D (Fig. 7A, left upper panel).|However, it is not clear at present whether HGTD-P participates directly in channel formation in association with VDAC or modulates its channel-forming activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TSPO2 | up-regulates activity
binding
|
VDAC1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261826 |
|
|
Homo sapiens |
Erythrocyte |
pmid |
sentence |
30061676 |
Our results demonstrate the existence of a VDAC-TSPO2-ANT complex that mediates ATP release from RBCs. We previously demonstrated that the translocase protein TSPO2 together with the voltage-dependent anion channel (VDAC) and adenine nucleotide transporter (ANT) were involved in a membrane transport complex in human red blood cells (RBCs). . The present results show that TSPO ligands induce polymerization of VDAC, coupled to activation of ATP release by a supramolecular complex involving VDAC, TSPO2 and ANT. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VDAC1 | up-regulates
|
Apoptosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249615 |
|
|
|
|
pmid |
sentence |
10365962 |
Our results indicate that the Bcl-2 family of proteins bind to the VDAC in order to regulate the mitochondrial membrane potential and the release of cytochrome c during apoptosis. |
|
Publications: |
1 |