| + |
PINK1 | up-regulates activity 
phosphorylation
|
UBC |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249691 |
Ser65 |
DYNIQKEsTLHLVLR |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24784582 |
Ubiquitin is phosphorylated by PINK1 to activate parkin|PINK1 phosphorylated ubiquitin at Ser65 both in vitro and in cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
| + |
USP5 | up-regulates quantity
cleavage
|
UBC |
0.846 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270822 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26235645 |
Here we provide data suggesting that two of the four mammalian ubiquitin precursors, UBA52 and UBA80, are processed mostly post-translationally whereas the other two, UBB and UBC, probably undergo a combination of co- and post-translational processing. Using an unbiased biochemical approach we found that UCHL3, USP9X, USP7, USP5 and Otulin/Gumby/FAM105b are by far the most active DUBs acting on these precursors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
OTULIN | up-regulates quantity
cleavage
|
UBC |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270820 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26235645 |
Here we provide data suggesting that two of the four mammalian ubiquitin precursors, UBA52 and UBA80, are processed mostly post-translationally whereas the other two, UBB and UBC, probably undergo a combination of co- and post-translational processing. Using an unbiased biochemical approach we found that UCHL3, USP9X, USP7, USP5 and Otulin/Gumby/FAM105b are by far the most active DUBs acting on these precursors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
UBC | up-regulates activity
binding
|
PRKN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249692 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26161729 |
Mechanism of phospho-ubiquitin-induced PARKIN activation|PhosphoUb binding leads to straightening of a helix in the RING1 domain, and the resulting conformational changes release the Ubl domain from the PARKIN core; this activates PARKIN|Our results show that PINK1-dependent phosphorylation of both parkin and ubiquitin is sufficient for full activation of parkin E3 activity. These findings demonstrate that phosphorylated ubiquitin is a parkin activator. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
| + |
UCHL1 | up-regulates quantity
cleavage
|
UBC |
0.864 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249693 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9521656 |
These data suggest that the physiological role of UCH is to hydrolyze small adducts of ubiquitin and to generate free monomeric ubiquitin from ubiquitin proproteins, but not to deubiquitinate ubiquitin-protein conjugates or disassemble polyubiquitin chains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Parkinson |
4.0
UBC
- 
- 