PREY
TRIM28
KAP1, PPP1R157, RNF96, TF1B, TIF1B
tripartite motif containing 28
GO Process (13)
GO Function (11)
GO Component (2)
Gene Ontology Biological Process
- DNA repair [IDA]
- epithelial to mesenchymal transition [ISS]
- gene expression [TAS]
- innate immune response [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of viral release from host cell [IDA]
- positive regulation of DNA repair [IDA]
- positive regulation of transcription factor import into nucleus [IDA]
- positive regulation of transcription, DNA-templated [ISS]
- protein oligomerization [IDA]
- protein sumoylation [IDA]
- protein ubiquitination [IDA]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- DNA binding [IDA]
- Krueppel-associated box domain binding [IDA]
- chromo shadow domain binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- sequence-specific DNA binding transcription factor activity [ISS]
- transcription corepressor activity [IDA]
- ubiquitin protein ligase binding [IDA]
- ubiquitin-protein transferase activity [IDA]
- zinc ion binding [IDA]
- DNA binding [IDA]
- Krueppel-associated box domain binding [IDA]
- chromo shadow domain binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- sequence-specific DNA binding transcription factor activity [ISS]
- transcription corepressor activity [IDA]
- ubiquitin protein ligase binding [IDA]
- ubiquitin-protein transferase activity [IDA]
- zinc ion binding [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
Interactome analyses revealed that the U1 snRNP machinery overlaps extensively with the RNAP II machinery and contains multiple ALS/SMA-causative proteins.
Mutations in multiple RNA/DNA binding proteins cause Amyotrophic Lateral Sclerosis (ALS). Included among these are the three members of the FET family (FUS, EWSR1 and TAF15) and the structurally similar MATR3. Here, we characterized the interactomes of these four proteins, revealing that they largely have unique interactors, but share in common an association with U1 snRNP. The latter observation led ... [more]
Sci Rep Dec. 08, 2017; 8(1);8755 [Pubmed: 29884807]
Throughput
- High Throughput
Curated By
- BioGRID