PRMT8
Gene Ontology Biological Process
Gene Ontology Molecular Function- S-adenosylmethionine-dependent methyltransferase activity [IDA]
- histone methyltransferase activity (H4-R3 specific) [IBA]
- histone-arginine N-methyltransferase activity [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [IDA]
- protein-arginine omega-N asymmetric methyltransferase activity [IDA]
- protein-arginine omega-N monomethyltransferase activity [IDA]
- S-adenosylmethionine-dependent methyltransferase activity [IDA]
- histone methyltransferase activity (H4-R3 specific) [IBA]
- histone-arginine N-methyltransferase activity [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [IDA]
- protein-arginine omega-N asymmetric methyltransferase activity [IDA]
- protein-arginine omega-N monomethyltransferase activity [IDA]
EWSR1
Gene Ontology Molecular Function
Biochemical Activity (Methylation)
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
Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state.
Protein arginine methylation is a eukaryotic posttranslational modification that plays a role in transcription, mRNA splicing and transport, in protein-protein interaction, and cell signaling. The type I protein arginine methyltransferase (PRMT) 8 is the only member of the human PRMT family that is localized at the cell membrane and its endogenous substrates have remained unknown as yet. Although PRMT8 was ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PRMT8 EWSR1 | Affinity Capture-MS 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. | High | 0.851 | BioGRID | 1186068 | |
| PRMT8 EWSR1 | Affinity Capture-MS 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. | High | 0.9418 | BioGRID | 2253231 | |
| PRMT8 EWSR1 | Affinity Capture-MS 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. | High | 0.8376 | BioGRID | 3115372 | |
| PRMT8 EWSR1 | Affinity Capture-MS 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. | Low | - | BioGRID | - | |
| PRMT8 EWSR1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID