| + |
SP1 | up-regulates quantity by expression 
transcriptional regulation
|
SOD2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271693 |
|
|
|
|
| pmid |
sentence |
| 10669635 |
These results suggest that PMA stimulates transcription of the Mn-SOD gene through an increase in Sp1 expression and thus implicate Sp1 as an effector mediating the PKC-signaling pathway elicited by extracellular signals. |
|
| Publications: |
1 |
| + |
NFE2L2 | up-regulates quantity by expression 
transcriptional regulation
|
SOD2 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254652 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22493435 |
BTG2 was found to up-regulate expression of antioxidant enzymes known to be regulated by NFE2L2, including catalase, SOD1, and SOD2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP36 | up-regulates quantity by stabilization
deubiquitination
|
SOD2 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272280 |
|
|
|
|
| pmid |
sentence |
| 21268071 |
Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36|Finally, USP36 was shown to be a specific deubiquitinating enzyme that reduces the ubiquitination level of SOD2 and was involved in SOD2 protein stability by extending its half-life. |
|
| Publications: |
1 |
| + |
FARP2 | up-regulates quantity by expression
transcriptional regulation
|
SOD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251761 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19276662 |
FIR induced the expression of IAP1, IAP2, XIAP Survivin, MnSOD, TNFalpha, pAKT and IL-1alpha |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SIRT1 | up-regulates quantity by expression
transcriptional regulation
|
SOD2 |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251763 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20089851 |
SIRT1 deacetylates and activates the FOXOs under oxidative stress, thereby inducing Mn-SOD expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARGC1A | up-regulates quantity by expression
transcriptional regulation
|
SOD2 |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251762 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20089851 |
PGC-1α has been reported to induce Mn-SOD expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
copper(1+) | up-regulates activity
chemical activation
|
SOD2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272300 |
|
|
|
|
| pmid |
sentence |
| 1542024 |
Copper as a cofactor and regulator of copper,zinc superoxide dismutase |
|
| Publications: |
1 |
| + |
BTG2 | up-regulates quantity by expression
transcriptional regulation
|
SOD2 |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254649 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 22493435 |
BTG2 was found to up-regulate expression of antioxidant enzymes known to be regulated by NFE2L2, including catalase, SOD1, and SOD2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SIRT3 | up-regulates activity
deacetylation
|
SOD2 |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267646 |
|
|
|
|
| pmid |
sentence |
| 34929314 |
SOD2 is the key substrate of SIRT3 in mitochondria. The combination of SIRT3 and SOD2 leads to the deacetylation and activation of SOD2 |
|
| Publications: |
1 |
| + |
superoxide | up-regulates activity
precursor of
|
SOD2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272284 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD2 | up-regulates quantity
chemical modification
|
dioxygen |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272282 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD2 | up-regulates quantity
chemical modification
|
hydrogen peroxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272283 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARGC1A | up-regulates
|
SOD2 |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253395 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18074631 |
In fact, experiments with either genetic knockouts or RNAi for the PGC1s show that the ability of ROS to induce a ROS scavenging programme depends entirely on the PGC1s. This includes genes encoding mitochondrial proteins like SOD2, but also includes cytoplasmic proteins such as catalase and GPX1. Cells lacking PGC1alpha are hypersensitive to death from oxidative stress caused by H2O2 or paraquat. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DIP2A | up-regulates activity
binding
|
SOD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266592 |
|
|
Mus musculus |
Brain |
| pmid |
sentence |
| 33781892 |
DIP2a is associated with SOD in the mitochondria of mouse brain. DIP2a knockout inhibited SOD activity. In this paper, we analyzed the interacting proteins of DIP2A by mass spectrum analysis and found that DIP2A was correlated with superoxide dismutase (SOD), SOD1 and SOD2. Knockout of DIP2A decreased SOD activity and increased the level of ROS in the mouse brain. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NfKb-p65/p50 | up-regulates quantity by expression
transcriptional regulation
|
SOD2 |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172392 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21357467 |
The nfkb p65/p50 heterodimer increases sod2, and p50/p50 suppresses it nf-kb p65/p50 binds to the enhancer and is important for cytokine-induced sod2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD2 | down-regulates quantity 
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272281 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29301787 |
Oxidative stress contributes to diabetes mellitus (DM)–induced endothelial dysfunction, which is one of the most common causes of cardiovascular morbidity and mortality.1,2 The major cellular defense against superoxide (O2•−) is SODs (superoxide dismutases), which consists of the SOD1 (cytoplasmic copper zinc SOD [Cu/ZnSOD]), the SOD2 (mitochondrial MnSOD), and the SOD3 (extracellular Cu/ZnSOD). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SOD2
- 
- 