| + |
FUS | up-regulates activity 
sumoylation
|
PA2G4 |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249657 |
Lys298 |
MGVVECAkHELLQPF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19946338 |
Here, we show that Ebp1 p42 isoform can be sumoylated on both K93 and K298 residues, which mediate its nuclear translocation and are required for its anti-proliferative activity .. Hence, TLS-mediated sumoylation is required for Ebp1 transcriptional repressive activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236904 |
Lys93 |
VCHFSPLkSDQDYIL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19946338 |
Here, we show that Ebp1 p42 isoform can be sumoylated on both K93 and K298 residues, which mediate its nuclear translocation and are required for its anti-proliferative activity .. Hence, TLS-mediated sumoylation is required for Ebp1 transcriptional repressive activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SAFB | up-regulates activity
relocalization
|
FUS |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262821 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27731383 |
SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription| In addition, depletion of SAFB1 reduced FUS's localization to chromatin-bound fraction and splicing activity, suggesting SAFB1 could tether FUS to chromatin compartment thorough N-terminal DNA-binding motif. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates quantity
post transcriptional regulation
|
DLG4 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262103 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 32118033 |
These results point toward a novel mechanism by which FUS targets neuronal mRNA and given that these PSD-95 and Shank1 3'-UTR G quadruplex structures are also targeted by the fragile X mental retardation protein (FMRP), they raise the possibility that FUS and FMRP might work together to regulate the translation of these neuronal mRNA targets.|As seen in Figure 7 (top panel), both PSD-95 Q1-Q2 and Shank1a GQ probes pulled down endogenous FUS, whereas their M2 mutants did not, indicating that the GQ structure is sufficient for recognition. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
TNPO1 | up-regulates activity
relocalization
|
FUS |
0.661 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262101 |
|
|
in vitro |
|
| pmid |
sentence |
| 23056579 |
The C-terminal nuclear localization sequence of FUsed in Sarcoma (FUS-NLS) is critical for its nuclear import mediated by transportin (Trn1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FUS | up-regulates activity
relocalization
|
MATR3 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262822 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27731383 |
Moreover, FUS interacts with another nuclear matrix-associated protein Matrin3, which is muted in a subset of familial ALS cases and reportedly interacts with TDP-43. Interestingly, ectopic ALS-linked FUS mutant sequestered endogenous Matrin3 and SAFB1 in the cytoplasmic aggregates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates quantity
post transcriptional regulation
|
SHANK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262104 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 32118033 |
These results point toward a novel mechanism by which FUS targets neuronal mRNA and given that these PSD-95 and Shank1 3'-UTR G quadruplex structures are also targeted by the fragile X mental retardation protein (FMRP), they raise the possibility that FUS and FMRP might work together to regulate the translation of these neuronal mRNA targets.|As seen in Figure 7 (top panel), both PSD-95 Q1-Q2 and Shank1a GQ probes pulled down endogenous FUS, whereas their M2 mutants did not, indicating that the GQ structure is sufficient for recognition. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
Exosome_Complex | up-regulates activity
relocalization
|
FUS |
0.234 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262812 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 27460707 |
We hypothesized that FUS could be secreted via the exosome pathway. We tested and confirmed that FUS was indeed present in exosomes in both SH-SY5Y and N2A cells (Fig. 6 and Supplemental Fig. 2). It is also noted that the level of the R495X mutant in exosomes was significantly higher than that of WT or the R521G mutant. |It raises the possibility that the exosome-mediated secretion of FUS may contribute to the cell-to-cell propagation of FUS pathology. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates activity
binding
|
SNRNP70 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262823 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26124092 |
FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SF1 | down-regulates 
binding
|
FUS |
0.54 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9660765 |
We speculate that zfm1 may inhibit transcription driven by the ntds of tls |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | down-regulates activity 
|
FUS |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262819 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33082139 |
When mTORC2 is inhibited, FUS is recruited to polyribosomes to promote translation inhibition and polyribosome stalling. Panel iv, ALS-FUS R521G and P525L mutants that localize more prominently to the cytoplasm also associate more abundantly with polyribosomes to inhibit translation and protein synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates quantity 
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262277 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 22051914 |
Similarly, cytoplasmic inclu- sions containing mutant fused in sarcoma (FUS) protein have been observed in some patients with FUS-related FALS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | down-regulates
|
Protein_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262820 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33082139 |
When mTORC2 is inhibited, FUS is recruited to polyribosomes to promote translation inhibition and polyribosome stalling. Panel iv, ALS-FUS R521G and P525L mutants that localize more prominently to the cytoplasm also associate more abundantly with polyribosomes to inhibit translation and protein synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
D-glucitol | down-regulates activity
relocalization
|
FUS |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262813 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 33172210 |
We found that osmotic stress robustly induced nuclear loss of TDP-43, SPFQ, FUS, hnRNPA1 and hnRNPK, with characteristic changes in nucleocytoplasmic localisation in an RBP-dependent manne |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | down-regulates activity
relocalization
|
DDX3X |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262811 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27460707 |
We found that ALS mutants of FUS co-localized with Caprin-1, DDX3X, and DHX9 in cytoplasmic inclusions that could lead to the mis-regulation of their respective pathways, providing further clues to the mechanism of ALS pathogenesis.|FUS interacting proteins were sequestered into the cytoplasmic mutant FUS inclusions that could lead to their mis-regulation or loss of function, contributing to ALS pathogenesis. | We also demonstrated the co-localization of DHX9, DDX3X and Caprin-1 with cytoplasmic EGFP-P525L mutant FUS inclusions in primary cortical neurons |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
DUSP22 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262803 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
GRIA4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262806 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
ATXN2 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262809 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
MPHOSPH9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262804 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
AMPA |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270231 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events inhFUS+/+;Smn+/‚àímice. As shown in Fig.6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected inhFUS+/+mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
VPS16 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262808 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
FUS | up-regulates activity
relocalization
|
GEMIN6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262106 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 23022481 |
Here, we report that FUS associates with the SMN complex, mediated by U1 snRNP and by direct interactions between FUS and SMN.|The FUS IP and pulldown revealed that FUS also associates with components of the SMN complex, including SMN and Gemins 4 and 6 |Remarkably, the number of SMN-stained nuclear bodies was dramatically reduced in the FUS knockdown cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates quantity by stabilization
post transcriptional regulation
|
CSDE1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262110 |
|
|
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 32808651 |
These findings demonstrated that LINC00205 facilitates malignant phenotypes in LC by recruiting FUS to stabilize CSDE1, suggesting LINC00205 as a potential target for LC therapy.|Subsequent RIP assay con- firmed such prediction, as CSDE1 mRNA was evidently precipitated by anti-FUS (Figure 3A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
HNRNPA2B1 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262802 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FUS | down-regulates activity
relocalization
|
DHX9 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262810 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 27460707 |
We found that ALS mutants of FUS co-localized with Caprin-1, DDX3X, and DHX9 in cytoplasmic inclusions that could lead to the mis-regulation of their respective pathways, providing further clues to the mechanism of ALS pathogenesis.|FUS interacting proteins were sequestered into the cytoplasmic mutant FUS inclusions that could lead to their mis-regulation or loss of function, contributing to ALS pathogenesis. | We also demonstrated the co-localization of DHX9, DDX3X and Caprin-1 with cytoplasmic EGFP-P525L mutant FUS inclusions in primary cortical neurons |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates activity
relocalization
|
GEMIN4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262105 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 23022481 |
Here, we report that FUS associates with the SMN complex, mediated by U1 snRNP and by direct interactions between FUS and SMN.|The FUS IP and pulldown revealed that FUS also associates with components of the SMN complex, including SMN and Gemins 4 and 6 |Remarkably, the number of SMN-stained nuclear bodies was dramatically reduced in the FUS knockdown cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates activity
relocalization
|
SMN1 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262107 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 23022481 |
Here, we report that FUS associates with the SMN complex, mediated by U1 snRNP and by direct interactions between FUS and SMN.|The FUS IP and pulldown revealed that FUS also associates with components of the SMN complex, including SMN and Gemins 4 and 6 |Remarkably, the number of SMN-stained nuclear bodies was dramatically reduced in the FUS knockdown cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRMT1 | down-regulates activity
methylation
|
FUS |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262274 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 30354839 |
PRMT1 catalyzes the arginine methylation of Fused in Sarcoma (FUS), an RNA-binding protein that interacts with RALY. We demonstrate that RALY down-regulation decreases protein arginine N-methyltransferase 1 levels, thus reducing FUS methylation. It is known that mutations in the FUS nuclear localization signal (NLS) retain the protein to the cytosol, promote aggregate formation, and are associated with amyotrophic lateral sclerosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
ADARB1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262805 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
AGRN |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262807 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Osmotic_stress | down-regulates activity
relocalization
|
FUS |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262815 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 33172210 |
We found that osmotic stress robustly induced nuclear loss of TDP-43, SPFQ, FUS, hnRNPA1 and hnRNPK, with characteristic changes in nucleocytoplasmic localisation in an RBP-dependent manne |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FUS
- 
- 