| + |
ATM | up-regulates activity 
phosphorylation
|
PEX5 |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262792 |
Ser141 |
DYNETDWsQEFISEV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26344566 |
Specificity for autophagy of peroxisomes (pexophagy) is provided by ATM phosphorylation of PEX5 at Ser 141, which promotes PEX5 monoubiquitylation at Lys 209, and recognition of ubiquitylated PEX5 by the autophagy adaptor protein p62, directing the autophagosome to peroxisomes to induce pexophagy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PEX1 | up-regulates activity
binding
|
PEX5 |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253618 |
|
|
Cricetulus griseus |
|
| pmid |
sentence |
| 16314507 |
Pex1, Pex6, and Pex26 are involved in Pex5 export from peroxisomes., we found that Pex1 and Pex6 bind to Pex5 (Fig. (Fig.6). Therefore, it is conceivable that Pex1 and Pex6 pull out Pex5 from peroxisome membranes in an ATP-dependent manner. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
PEX6 | up-regulates activity
binding
|
PEX5 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253619 |
|
|
Cricetulus griseus |
|
| pmid |
sentence |
| 16314507 |
Pex1, Pex6, and Pex26 are involved in Pex5 export from peroxisomes., we found that Pex1 and Pex6 bind to Pex5 (Fig. (Fig.6). Therefore, it is conceivable that Pex1 and Pex6 pull out Pex5 from peroxisome membranes in an ATP-dependent manner. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
PEX12 | up-regulates activity
ubiquitination
|
PEX5 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253020 |
|
|
in vitro |
|
| pmid |
sentence |
| 19687296 |
Here we report on the identification of the protein-ubiquitin ligases that are responsible for the ubiquitination of the peroxisomal protein import receptor Pex5. It is demonstrated that each of the three RING peroxins Pex2, Pex10, and Pex12 exhibits ubiquitin-protein isopeptide ligase activity. Our results show that Pex2 mediates the Ubc4-dependent polyubiquitination whereas Pex12 facilitates the Pex4-dependent monoubiquitination of Pex5.While polyubiquitinated Pex5 is degraded by the proteasome, monoubiquitinated Pex5 is destined for a new round of the receptor cycle. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PEX2 | down-regulates quantity by destabilization 
ubiquitination
|
PEX5 |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253021 |
|
|
in vitro |
|
| pmid |
sentence |
| 19687296 |
Here we report on the identification of the protein-ubiquitin ligases that are responsible for the ubiquitination of the peroxisomal protein import receptor Pex5. It is demonstrated that each of the three RING peroxins Pex2, Pex10, and Pex12 exhibits ubiquitin-protein isopeptide ligase activity. Our results show that Pex2 mediates the Ubc4-dependent polyubiquitination whereas Pex12 facilitates the Pex4-dependent monoubiquitination of Pex5.While polyubiquitinated Pex5 is degraded by the proteasome, monoubiquitinated Pex5 is destined for a new round of the receptor cycle. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PEX14 | up-regulates activity
binding
|
PEX5 |
0.931 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253027 |
|
|
in vitro |
|
| pmid |
sentence |
| 15798189 |
The peroxisomal docking complex is a key component of the import machinery for matrix proteins. The core protein of this complex, Pex14, is thought to represent the initial docking site for the import receptors Pex5 and Pex7. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PEX5 | up-regulates activity
binding
|
SQSTM1 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262793 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26344566 |
Specificity for autophagy of peroxisomes (pexophagy) is provided by ATM phosphorylation of PEX5 at Ser 141, which promotes PEX5 monoubiquitylation at Lys 209, and recognition of ubiquitylated PEX5 by the autophagy adaptor protein p62, directing the autophagosome to peroxisomes to induce pexophagy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2D2 | down-regulates quantity by destabilization
ubiquitination
|
PEX5 |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253023 |
|
|
in vitro |
|
| pmid |
sentence |
| 19687296 |
Here we report on the identification of the protein-ubiquitin ligases that are responsible for the ubiquitination of the peroxisomal protein import receptor Pex5. It is demonstrated that each of the three RING peroxins Pex2, Pex10, and Pex12 exhibits ubiquitin-protein isopeptide ligase activity. Our results show that Pex2 mediates the Ubc4-dependent polyubiquitination whereas Pex12 facilitates the Pex4-dependent monoubiquitination of Pex5.While polyubiquitinated Pex5 is degraded by the proteasome, monoubiquitinated Pex5 is destined for a new round of the receptor cycle. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UBE2D1 | up-regulates activity
ubiquitination
|
PEX5 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253022 |
|
|
in vitro |
|
| pmid |
sentence |
| 19687296 |
Here we report on the identification of the protein-ubiquitin ligases that are responsible for the ubiquitination of the peroxisomal protein import receptor Pex5. It is demonstrated that each of the three RING peroxins Pex2, Pex10, and Pex12 exhibits ubiquitin-protein isopeptide ligase activity. Our results show that Pex2 mediates the Ubc4-dependent polyubiquitination whereas Pex12 facilitates the Pex4-dependent monoubiquitination of Pex5.While polyubiquitinated Pex5 is degraded by the proteasome, monoubiquitinated Pex5 is destined for a new round of the receptor cycle. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PEX5
- 
- 