RBMX
Gene Ontology Biological Process
- RNA splicing [TAS]
- cellular response to interleukin-1 [IDA]
- gene expression [TAS]
- mRNA splicing, via spliceosome [IC, TAS]
- membrane protein ectodomain proteolysis [IDA]
- negative regulation of mRNA splicing, via spliceosome [ISS]
- osteoblast differentiation [IDA]
- positive regulation of mRNA splicing, via spliceosome [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein homooligomerization [ISS]
- regulation of alternative mRNA splicing, via spliceosome [IDA]
- transcription from RNA polymerase II promoter [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HNRNPR
Gene Ontology Biological Process
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
Matrix-screening reveals a vast potential for direct protein-protein interactions among RNA binding proteins.
RNA-binding proteins (RBPs) are crucial factors of post-transcriptional gene regulation and their modes of action are intensely investigated. At the center of attention are RNA motifs that guide where RBPs bind. However, sequence motifs are often poor predictors of RBP-RNA interactions in vivo. It is hence believed that many RBPs recognize RNAs as complexes, to increase specificity and regulatory possibilities. ... [more]
Throughput
- High Throughput
Additional Notes
- Included protein pairs with sumIS score >= 7.1
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
RBMX HNRNPR | 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 | - | BioGRID | 3367215 | |
RBMX HNRNPR | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 0.806 | BioGRID | 743227 |
Curated By
- BioGRID