BAIT
PRMT8
HRMT1L3, HRMT1L4
protein arginine methyltransferase 8
GO Process (7)
GO Function (9)
GO Component (3)
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]
Homo sapiens
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
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]
Proteins Sep. 01, 2008; 72(4);1125-37 [Pubmed: 18320585]
Throughput
- Low Throughput
Curated By
- BioGRID