| + |
PINK1 | up-regulates 
phosphorylation
|
Ubiquitin |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270341 |
Ser65 |
DYNIQKEsTLHLVLR |
|
|
| pmid |
sentence |
| 24784582 |
Here we report that ubiquitin is the genuine substrate of PINK1. PINK1 phosphorylated ubiquitin at Ser 65 both in vitro and in cells, and a Ser 65 phosphopeptide derived from endogenous ubiquitin was only detected in cells in the presence of PINK1 and following a decrease in mitochondrial membrane potential. |
|
| Publications: |
1 |
| + |
OTULIN | up-regulates quantity
cleavage
|
Ubiquitin |
0.704 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270829 |
|
|
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 |
| + |
Ubiquitin | form complex 
binding
|
Ub:RBR_E3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271381 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner to form a thioester-linked E1‒Ub conjugate. The activated Ub is then delivered to an E2 enzyme via a transthiolation reaction. Finally, an E3 enzyme, which can bind both a substrate and an E2‒Ub conjugate, mediates the covalent linkage of Ub to the target protein as a tag. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
Ubiquitin | form complex
binding
|
Ub:E1 (UBA1 substrate) |
0.756 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270834 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24816100 |
The activation of ubiquitin by the ubiquitin-activating enzyme Uba1 (E1) constitutes the first step in the covalent modification of target proteins with ubiquitin. This activation is a three-step process in which ubiquitin is adenylated at its C-terminal glycine, followed by the covalent attachment of ubiquitin to a catalytic cysteine residue of Uba1 and the subsequent adenylation of a second ubiquitin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
USP9X | up-regulates quantity
cleavage
|
Ubiquitin |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270831 |
|
|
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 |
| + |
Ubiquitin | form complex
ubiquitination
|
Ub:E2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270839 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
Ubiquitin | form complex
binding
|
Ub:RING_E3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271380 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner to form a thioester-linked E1‒Ub conjugate. The activated Ub is then delivered to an E2 enzyme via a transthiolation reaction. Finally, an E3 enzyme, which can bind both a substrate and an E2‒Ub conjugate, mediates the covalent linkage of Ub to the target protein as a tag. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
Ubiquitin | up-regulates activity
binding
|
PRKN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270343 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 24784582 |
The phosphorylation-dependent interaction between ubiquitin and parkin suggests that phosphorylated ubiquitin unlocks autoinhibition of the catalytic cysteine. 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: |
Mus Musculus |
| + |
USP5 | up-regulates quantity
cleavage
|
Ubiquitin |
0.84 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270830 |
|
|
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 |
| + |
Ubiquitin | form complex
binding
|
Ub:E1 (UBA6 substrate) |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270836 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24816100 |
The activation of ubiquitin by the ubiquitin-activating enzyme Uba1 (E1) constitutes the first step in the covalent modification of target proteins with ubiquitin. This activation is a three-step process in which ubiquitin is adenylated at its C-terminal glycine, followed by the covalent attachment of ubiquitin to a catalytic cysteine residue of Uba1 and the subsequent adenylation of a second ubiquitin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
| + |
USP7 | up-regulates quantity
cleavage
|
Ubiquitin |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270837 |
|
|
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 |
| + |
Ubiquitin | form complex
binding
|
Ubiquitinated-Viral_Protein |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25688236 |
MHC class I antigen presentation pathway. Proteins with ubiquitin tags (red spheres) are degraded by proteasomes and the resulting peptides are transported into the endoplasmic reticulum (ER) by TAP|Many viruses have mechanisms of interfering with MHC class I processing, including direct interaction of viral proteins with immunoproteasome subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UCHL3 | up-regulates quantity
cleavage
|
Ubiquitin |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270832 |
|
|
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 |
| + |
Ubiquitin | form complex
binding
|
Ub:HECT_E3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271379 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner to form a thioester-linked E1‒Ub conjugate. The activated Ub is then delivered to an E2 enzyme via a transthiolation reaction. Finally, an E3 enzyme, which can bind both a substrate and an E2‒Ub conjugate, mediates the covalent linkage of Ub to the target protein as a tag. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Ubiquitin activation |
3.0
Ubiquitin