DNM1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
SUMO1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular protein metabolic process [TAS]
- cytokine-mediated signaling pathway [TAS]
- interferon-gamma-mediated signaling pathway [TAS]
- negative regulation of DNA binding [IMP]
- negative regulation of sequence-specific DNA binding transcription factor activity [IMP]
- negative regulation of transcription, DNA-templated [IDA, IMP]
- palate development [ISS]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein complex assembly [IDA]
- post-translational protein modification [TAS]
- protein sumoylation [IDA, TAS]
- regulation of interferon-gamma-mediated signaling pathway [TAS]
- regulation of protein localization [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Dynamin interacts with members of the sumoylation machinery.
Dynamin is a GTP-binding protein whose oligomerization-dependent assembly around the necks of lipid vesicles mediates their scission from parent membranes. Dynamin is thus directly involved in the regulation of endocytosis. Sumoylation is a post-translational protein modification whereby the ubiquitin-like modifier Sumo is covalently attached to lysine residues on target proteins by a process requiring the concerted action of an activating ... [more]
Throughput
- High Throughput|Low Throughput
Additional Notes
- #LPPI
- Likely protein-protein interaction
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DNM1 SUMO1 | 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 | 1059918 |
Curated By
- BioGRID