UFL1
Gene Ontology Biological Process
- negative regulation of NF-kappaB transcription factor activity [IMP]
- negative regulation of protein ubiquitination [IDA]
- osteoblast differentiation [IDA]
- protein ufmylation [IDA, IMP]
- regulation of proteasomal ubiquitin-dependent protein catabolic process [IMP]
- response to endoplasmic reticulum stress [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RPN1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
UFMylation maintains tumour suppressor p53 stability by antagonizing its ubiquitination.
p53 is the most intensively studied tumour suppressor1. The regulation of p53 homeostasis is essential for its tumour-suppressive function2,3. Although p53 is regulated by an array of post-translational modifications, both during normal homeostasis and in stress-induced responses2-4, how p53 maintains its homeostasis remains unclear. UFMylation is a recently identified ubiquitin-like modification with essential biological functions5-7. Deficiency in this modification leads ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RPN1 UFL1 | 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 | 17.5 | BioGRID | 3005047 |
Curated By
- BioGRID