| + |
CHEK2 | up-regulates activity 
phosphorylation
|
SOD1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262794 |
Ser60 |
DNTAGCTsAGPHFNP |
Saccharomyces cerevisiae |
|
| pmid |
sentence |
| 24647101 |
ROS signaling is mediated by Mec1/ATM and its effector Dun1/Cds1 kinase, through Dun1 interaction with Sod1 and regulation of Sod1 by phosphorylation at S60, 99. In the nucleus, Sod1 binds to the promoters and regulates the expression of oxidative resistance and repair genes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262795 |
Ser99 |
KDGVADVsIEDSVIS |
Saccharomyces cerevisiae |
|
| pmid |
sentence |
| 24647101 |
ROS signaling is mediated by Mec1/ATM and its effector Dun1/Cds1 kinase, through Dun1 interaction with Sod1 and regulation of Sod1 by phosphorylation at S60, 99. In the nucleus, Sod1 binds to the promoters and regulates the expression of oxidative resistance and repair genes. |
|
| Publications: |
2 |
Organism: |
Saccharomyces Cerevisiae |
| + |
BTG2 | up-regulates quantity by expression 
transcriptional regulation
|
SOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254650 |
|
|
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 |
| + |
WT1 | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253898 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9867871 |
The human copper-zinc superoxide dismutase gene (SOD1) proximal promoter is regulated by Sp1, Egr-1, and WT1 via non-canonical binding sites. Egr-1 and two splicing variants of the Egr-related protein WT1 were able to transactivate the SOD1 promoter in co-transfection experiments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEBPD | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253774 |
|
|
Homo sapiens |
Urinary Bladder Cancer Cell Line |
| pmid |
sentence |
| 20385105 |
Expression of CEBPD reduced cisplatin-induced reactive oxygen species (ROS) and apoptosis in NTUB1 cells by inducing the expression of Cu/Zn-superoxide dismutase (SOD1) via direct promoter transactivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARCHF5 | down-regulates quantity by destabilization 
ubiquitination
|
SOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272982 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 19741096 |
Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
MIF | down-regulates quantity by destabilization
relocalization
|
SOD1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262797 |
|
|
Mus musculus |
NSC-34 Cell |
| pmid |
sentence |
| 29371591 |
Here, we show that MIF inhibits mutant SOD1 nuclear clearance when overexpressed in motor neuron-like NSC-34 cells|SOD1WT is evenly distributed between the cytoplasm and the nucleus while mutant SOD1G93A shows predominantly cytoplasmic distribution (Fig. 1a, b). Expression of MIF in cells expressing SOD1WT had no effect on the distribution of the SOD1WT–EGFP protein. However, expression of MIF together with the mutant SOD1G93A–EGFP, inhibited the nuclear clearance of misfolded SOD1 resulting in a more wild-type-like distribution of the mutant SOD1 protein |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MARCHF5 | down-regulates quantity
ubiquitination
|
SOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278654 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19741096 |
Cycloheximide-chase assay in the Neuro2a cells indicated that MITOL overexpression promoted mSOD1 degradation and suppressed both the mitochondrial accumulation of mSOD1 and mSOD1-induced reactive oxygen species generation.|In vitro ubiquitination assay revealed that MITOL directly ubiquitinates mSOD1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD1 | up-regulates
|
MAP3K5 |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262789 |
|
|
Mus musculus |
NSC-34 Cell |
| pmid |
sentence |
| 18519638 |
To investigate the role of ASK1 in the motor neurotoxicity by SOD1mut, we examined whether SOD1mut activates ASK1 as assessed by in vitro kinase assay. Expression of SOD1mut, but not SOD1wt, activated endogenous ASK1 (Fig. 4A, top panel). We next examined whether SOD1mut-induced ASK1 activation is mediated by ER stress. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SOD1 | down-regulates quantity by destabilization
binding
|
KARS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262800 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 18715867 |
In the presence of mutant SOD1, mitoKARS displays a high propensity to misfold and aggregate prior to its import into mitochondria, becoming a target for proteasome degradation. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SOD1 | up-regulates quantity
|
S100A4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262784 |
|
|
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 31623154 |
We demonstrated the increased expression of S100A4 also in fibroblasts derived from amyotrophic lateral sclerosis (ALS) patients carrying SOD1 pathogenic variants. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262783 |
|
|
Rattus norvegicus |
Fibroblast, Astrocyte |
| pmid |
sentence |
| 31623154 |
We found that S100A4 was significantly up-regulated in astrocytes and microglia in the spinal cord of a transgenic rat SOD1-G93A model of amyotrophic lateral sclerosis |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Rattus Norvegicus |
| Tissue: |
Spinal Cord |
| + |
SOD1 | up-regulates
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262796 |
|
|
Mus musculus |
NSC-34 Cell |
| pmid |
sentence |
| 29371591 |
Incubating SOD1G93A or SOD1G85R, another well-established misfolded SOD1 mutant, in the absence of recombinant MIF resulted in an exponential increase in thioflavin T (ThT) fluorescence (which correlates with amyloid aggregate formation) |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SOD1 | up-regulates activity
binding
|
EIF2AK3 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262787 |
|
|
Mus musculus |
NSC-34 Cell |
| pmid |
sentence |
| 18519638 |
SOD1mut-induced ER stress |we first examined whether SOD1mut induces ER stress in NSC34 motor neurons, as assessed by band-shift analyses of the ER transmembrane kinase receptors IRE1 and PERK. Adenovirus (Ad)-mediated expression of ALS-linked SOD1mut (SOD1G93A) was detectable within 48 h of infection (Supplemental Fig. S1A). SOD1mut (SOD1A4V, SOD1G85R, and SOD1G93A) but not wild-type SOD1 (SOD1wt) activated IRE1 and PERK |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
copper(1+) | up-regulates activity
chemical activation
|
SOD1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272299 |
|
|
|
|
| pmid |
sentence |
| 1542024 |
Copper as a cofactor and regulator of copper,zinc superoxide dismutase |
|
| Publications: |
1 |
| + |
SOD1 | up-regulates quantity
chemical modification
|
dioxygen |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272286 |
|
|
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 |
| + |
SOD1 | up-regulates quantity
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262279 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 22051914 |
SOD1 inclusions are found in motor neurons of patients with FALS, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SP1 | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253899 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8921911 |
Studies using two mutant versions of this promoter, in which the Sp1 and C/EBP-related factor binding sites were deleted, respectively, revealed that Sp1 and C/EBP-related factors activate the transcription of SOD1 gene. the binding of Sp1 to the proximal upstream region of the Cu/Zn SOD might explain the expression of Cu/Zn SOD in a wide variety of cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGR1 | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253897 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9867871 |
The human copper-zinc superoxide dismutase gene (SOD1) proximal promoter is regulated by Sp1, Egr-1, and WT1 via non-canonical binding sites. Egr-1 and two splicing variants of the Egr-related protein WT1 were able to transactivate the SOD1 promoter in co-transfection experiments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SQSTM1 | down-regulates quantity by destabilization
binding
|
SOD1 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262801 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 19765191 |
This study provides a novel molecular mechanism by which mutant SOD1 can be recognized by p62 in an ubiquitin-independent fashion and targeted for the autophagy-lysosome degradation pathway. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Autophagy |
| + |
SOD1 | up-regulates
|
ER stress |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262788 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18519638 |
SOD1mut-induced ER stress |we first examined whether SOD1mut induces ER stress in NSC34 motor neurons, as assessed by band-shift analyses of the ER transmembrane kinase receptors IRE1 and PERK. Adenovirus (Ad)-mediated expression of ALS-linked SOD1mut (SOD1G93A) was detectable within 48 h of infection (Supplemental Fig. S1A). SOD1mut (SOD1A4V, SOD1G85R, and SOD1G93A) but not wild-type SOD1 (SOD1wt) activated IRE1 and PERK |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPARD | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255053 |
|
|
Homo sapiens |
HOS-TE85 Cell |
| pmid |
sentence |
| 18048767 |
Activation of PPAR-delta upregulated the expression of antioxidant genes superoxide dismutase 1, catalase, and thioredoxin and decreased reactive oxygen species production in ECs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLF4 | down-regulates quantity by repression 
transcriptional regulation
|
SOD1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254545 |
|
|
Homo sapiens |
BE(2)-M17 Cell |
| pmid |
sentence |
| 23370975 |
The expression of superoxide dismutase (SOD) 1 in both mRNA and protein levels was found to be decreased by overexpressing KLF4, while increased by knockdown of KLF4 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD1 | up-regulates activity
binding
|
ERN1 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262786 |
|
|
Mus musculus |
NSC-34 Cell |
| pmid |
sentence |
| 18519638 |
SOD1mut-induced ER stress |we first examined whether SOD1mut induces ER stress in NSC34 motor neurons, as assessed by band-shift analyses of the ER transmembrane kinase receptors IRE1 and PERK. Adenovirus (Ad)-mediated expression of ALS-linked SOD1mut (SOD1G93A) was detectable within 48 h of infection (Supplemental Fig. S1A). SOD1mut (SOD1A4V, SOD1G85R, and SOD1G93A) but not wild-type SOD1 (SOD1wt) activated IRE1 and PERK |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SOD1 | up-regulates activity
binding
|
BCL2 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262799 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15233914 |
Familial amyotrophic lateral sclerosis (ALS)-linked mutations in the copper-zinc superoxide dismutase (SOD1) gene cause motor neuron death in about 3% of ALS cases. While the wild-type (wt) protein is anti-apoptotic, mutant SOD1 promotes apoptosis.|We now demonstrate that both wt and mutant SOD1 bind the anti-apoptotic protein Bcl-2, providing evidence of a direct link between SOD1 and an apoptotic pathway. This interaction is evident in vitro and in vivo in mouse and human spinal cord.|These findings provide new insights into the anti-apoptotic function of SOD1 and suggest that entrapment of Bcl-2 by large SOD1 aggregates may deplete motor neurons of this anti-apoptotic protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Spinal Cord |
| Pathways: | Autophagy |
| + |
SOD1 | up-regulates quantity
chemical modification
|
hydrogen peroxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272287 |
|
|
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 |
| + |
SOD1 | down-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272285 |
|
|
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 |
| + |
MTF1 | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254601 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15378601 |
MRE-binding transcription factor-1 (MTF-1) is a highly conserved heavy metal-induced transcriptional activator. MTF-1 also activates transcription in response to oxidative stress and regulates the expression of several cytoprotective factor genes, including MT, gamma-glutamylcysteine synthetase, and Cu/Zn-superoxide dismutase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD1 | down-regulates activity
binding
|
VDAC1 |
0.426 |
| 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 |
| + |
NFE2L2 | up-regulates quantity by expression
transcriptional regulation
|
SOD1 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254653 |
|
|
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 |
| + |
DIP2A | up-regulates activity
binding
|
SOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266591 |
|
|
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 |
| + |
superoxide | up-regulates activity
precursor of
|
SOD1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272288 |
|
|
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 |
| + |
SOD1 | down-regulates activity
binding
|
DERL1 |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262785 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18519638 |
Various proteins involved in ERAD have been identified recently (Meusser et al. 2005). Among them, components of the retro-translocation machinery including ATPase p97, its cofactors Ufd1 and Npl4, and the ER membrane proteins Derlin-1 and VIMP are of key importance to ERAD function |Here we show that SOD1(mut) specifically interacted with Derlin-1, a component of endoplasmic reticulum (ER)-associated degradation (ERAD) machinery and triggered ER stress through dysfunction of ERAD. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SOD1
- 
- 