RNF4
Gene Ontology Biological Process
- cellular response to gamma radiation [ISO]
- cellular response to hydroxyurea [ISO]
- negative regulation of cell death [ISO]
- positive regulation of transcription from RNA polymerase II promoter [IDA, ISO]
- positive regulation of transcription, DNA-templated [ISO]
- proteasome-mediated ubiquitin-dependent protein catabolic process [ISO]
- protein K11-linked ubiquitination [ISO]
- protein K48-linked ubiquitination [ISO]
- protein K6-linked ubiquitination [ISO]
- protein K63-linked ubiquitination [ISO]
- protein autoubiquitination [ISO]
- protein ubiquitination [ISO]
- regulation of kinetochore assembly [ISO]
- regulation of spindle assembly [ISO]
- response to arsenic-containing substance [ISO]
Gene Ontology Molecular Function
SUMO3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.
The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) ... [more]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- Likely protein-protein interaction
- NMR structure
Curated By
- BioGRID