RING1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HIST1H2AB
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Ubiquitination)
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
De novo mutation in RING1 with epigenetic effects on neurodevelopment.
RING1 is an E3-ubiquitin ligase that is involved in epigenetic control of transcription during development. It is a component of the polycomb repressive complex 1, and its role in that complex is to ubiquitylate histone H2A. In a 13-year-old girl with syndromic neurodevelopmental disabilities, we identified a de novo mutation, RING1 p.R95Q, which alters a conserved arginine residue in the ... [more]
Throughput
- Low Throughput
Additional Notes
- in vitro mono-ubiquitination of histone H2A as substrate, with UBA1 as E1, UBE2D3 as E2, and RING1 and either BMI1 or PCGF1 as E3
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RING1 HIST1H2AB | Co-crystal Structure 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. | Low | - | BioGRID | - |
Curated By
- BioGRID