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
UBE2E2
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Functional interactions between ubiquitin E2 enzymes and TRIM proteins.
The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite motif module, composed of a RING domain, one or two B-box domains and a coiled-coil region. TRIM proteins are involved in many cellular processes and represent the largest subfamily of RING-containing putative ubiquitin E3 ligases. Whereas their role as E3 ubiquitin ligases has been presumed, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| UBE2E2 TRIM37 | Two-hybrid 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. | Low | - | BioGRID | - |
Curated By
- BioGRID