TRIM37
Gene Ontology Biological Process
- aggresome assembly [IDA]
- negative regulation of NF-kappaB transcription factor activity [IDA]
- negative regulation of centriole replication [IMP]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- protein autoubiquitination [IDA]
Gene Ontology Molecular Function
HIST1H2AB
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
TRIM37 Mediates Chemoresistance and Maintenance of Stemness in Pancreatic Cancer Cells via Ubiquitination of PTEN and Activation of the AKT-GSK-3?-?-Catenin Signaling Pathway.
The tripartite motif-containing family member TRIM37 is involved in a number of important biological and pathological processes, and it has recently been shown to be an essential regulator of protein ubiquitination and a contributor to tumorigenesis. We previously showed that TRIM37 is overexpressed in and promotes the proliferation and invasion of pancreatic cancer (PC).Sphere formation, flow cytometric, qRT-PCR, western blot, ... [more]
Throughput
- High Throughput
Additional Notes
- High confidence interaction
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM37 HIST1H2AB | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 2489566 |
Curated By
- BioGRID