SREK1
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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
Regulation of alternative splicing by SRrp86 and its interacting proteins.
SRrp86 is a unique member of the SR protein superfamily containing one RNA recognition motif and two serine-arginine (SR)-rich domains separated by an unusual glutamic acid-lysine (EK)-rich region. Previously, we showed that SRrp86 could regulate alternative splicing by both positively and negatively modulating the activity of other SR proteins and that the unique EK domain could inhibit both constitutive and ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
SREK1 RBMX | 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