| + |
FBXO32 | up-regulates 
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255342 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11717410 |
Atrogin-1 is one of the few examples of an F-box protein or Ub-protein ligase (E3) expressed in a tissue-specific manner and appears to be a critical component in the enhanced proteolysis leading to muscle atrophy in diverse diseases |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255341 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 20871233 |
Atrogin-1, but not MuRF-1, was induced at both the gene and protein level as ApcMin/+ mice aged from 3 to 6 months of age, going from a pre-cachectic to a cachectic state. Atrogin-1 mRNA and protein levels were also elevated in ApcMin/+ mice when we over-expressed IL-6 in the circulation. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
UBXN1 | up-regulates
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261059 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15362974 |
Our working hypothesis is that SAKS1 acts as scaffolding protein to enhance the unfolding and proteolytic destruction of a subset of proteins. PNGase removes high-mannose-containing oligosaccharides from MGPs [30], and our results suggest this may be facilitated by the formation of a complex between PNGase, VCP, SAKS1 and ubiquitinated MGPs, as illustrated schematically in Figure 7(B). PNGase has been reported to bind to the S4 component of the proteasome [30], so that the deglycosylation of MGPs by PNGase, followed by VCP-catalysed unfolding, may facilitate their destruction by the proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
26S Proteasome | up-regulates
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263375 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29636472 |
The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Caspase 3 complex | up-regulates
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256476 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25787076 |
The UPS by itself degrades actomyosin and myofibrillar proteins slowly, but when caspase-3 is activated, it cleaves actomyosin and the myofibrillar proteins to provide substrates for degradation in the UPS . Caspase-3 also can cleave specific subunits of the 19 S proteasome particle, which stimulates the proteolytic activity of the 26S proteasome[...] These results indicate that caspase-3 participates in the muscle proteolysis that is present in tumor-bearing mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CASP3 | up-regulates
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255337 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25787076 |
The UPS by itself degrades actomyosin and myofibrillar proteins slowly, but when caspase-3 is activated, it cleaves actomyosin and the myofibrillar proteins to provide substrates for degradation in the UPS . Caspase-3 also can cleave specific subunits of the 19 S proteasome particle, which stimulates the proteolytic activity of the 26S proteasome[...] These results indicate that caspase-3 participates in the muscle proteolysis that is present in tumor-bearing mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RAD23B | up-regulates
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261062 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16401726 |
The XPCB domain of Rad23 binds Png1, which in turn facilitates the substrate recognition of Rad23. Through interactions with Ub chains and the proteasome mediated by the UBA and UBL domains in Rad23, Rad23 facilitates substrate transfer to the proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Protein_degradation