PML
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [ISS]
- PML body organization [IDA, IMP]
- apoptotic process [IDA]
- cell cycle arrest [IDA]
- cellular senescence [IDA]
- circadian regulation of gene expression [ISS]
- cytokine-mediated signaling pathway [TAS]
- endoplasmic reticulum calcium ion homeostasis [ISS]
- entrainment of circadian clock by photoperiod [ISS]
- innate immune response [IDA]
- interferon-gamma-mediated signaling pathway [TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [IDA]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [ISS]
- maintenance of protein location in nucleus [IDA]
- negative regulation of angiogenesis [IMP]
- negative regulation of cell growth [IDA]
- negative regulation of cell proliferation [IMP]
- negative regulation of mitotic cell cycle [IDA]
- negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IMP]
- negative regulation of telomerase activity [IMP]
- negative regulation of telomere maintenance via telomerase [IMP]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of translation in response to oxidative stress [IDA]
- negative regulation of viral release from host cell [IDA]
- positive regulation of apoptotic process involved in mammary gland involution [IDA]
- positive regulation of defense response to virus by host [IMP]
- positive regulation of extrinsic apoptotic signaling pathway [IMP]
- positive regulation of histone deacetylation [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein complex assembly [IDA]
- protein stabilization [IDA]
- protein targeting [IDA, IMP]
- regulation of calcium ion transport into cytosol [ISS]
- regulation of circadian rhythm [ISS]
- regulation of double-strand break repair [IMP]
- regulation of protein phosphorylation [ISS]
- regulation of transcription, DNA-templated [IMP]
- response to cytokine [IDA]
- response to hypoxia [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PIAS3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
The p97/VCP segregase is essential for arsenic-induced degradation of PML and PML-RARA.
Acute Promyelocytic Leukemia is caused by expression of the oncogenic Promyelocytic Leukemia (PML)-Retinoic Acid Receptor Alpha (RARA) fusion protein. Therapy with arsenic trioxide results in degradation of PML-RARA and PML and cures the disease. Modification of PML and PML-RARA with SUMO and ubiquitin precedes ubiquitin-mediated proteolysis. To identify additional components of this pathway, we performed proteomics on PML bodies. This ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PML PIAS3 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | BioGRID | 3643897 | |
| PML PIAS3 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | - |
Curated By
- BioGRID