PSMA1
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [TAS]
- G1/S transition of mitotic cell cycle [TAS]
- RNA metabolic process [TAS]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- apoptotic process [TAS]
- cellular nitrogen compound metabolic process [TAS]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- mitotic cell cycle [TAS]
- negative regulation of apoptotic process [TAS]
- negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- protein polyubiquitination [TAS]
- regulation of apoptotic process [TAS]
- regulation of cellular amino acid metabolic process [TAS]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- small molecule metabolic process [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GLTSCR2
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Proteolytic Processing)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Nucleolar stress induces ubiquitination-independent proteasomal degradation of PICT1.
A nucleolar protein, PICT1, regulates the tumor suppressor p53 by tethering ribosomal protein L11 within the nucleolus to repress the binding of L11 to the E3 ligase MDM2. PICT1 depletion results in the release of L11 to the nucleoplasm to inhibit MDM2, leading to p53 activation. Here, we demonstrate that nucleolar stress induces proteasome-mediated degradation of PICT1 in a ubiquitin-independent ... [more]
Throughput
- Low Throughput
Additional Notes
- 20S proteasome core degraded PICT1 in vitro
Curated By
- BioGRID