| + |
PINK1 | up-regulates
phosphorylation
|
UBA52 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270342 |
Ser65 |
DYNIQKEsTLHLVLR |
Mus musculus |
MEF Cell |
| 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 |
Organism: |
Mus Musculus |
| + |
UBA52 | up-regulates activity
binding
|
PRKN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270344 |
|
|
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 |
| + |
UBA52 | form complex
binding
|
60S cytosolic large ribosomal subunit |
0.814 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262459 |
|
|
in vitro |
|
| pmid |
sentence |
| 25901680 |
Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 Å, reaching 2.9 Å resolution in the most stable regions. |The human ribosome (80S) has a molecular weight of 4.3 MDa: the large subunit (60S) consists of 28S, 5S and 5.8S rRNAs and 47 proteins, while the small subunit (40S) possesses a single 18S rRNA chain and 33 pro- teins. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SEC23B |
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