YWHAZ
Gene Ontology Biological Process
- Golgi reassembly [IMP]
- RNA metabolic process [TAS]
- apoptotic process [TAS]
- blood coagulation [TAS]
- establishment of Golgi localization [IMP]
- gene expression [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- mRNA metabolic process [TAS]
- membrane organization [TAS]
- negative regulation of apoptotic process [TAS]
- platelet activation [TAS]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TRIM21
Gene Ontology Biological Process
- innate immune response [IDA, TAS]
- negative regulation of NF-kappaB transcription factor activity [IDA]
- negative regulation of protein deubiquitination [IMP]
- negative regulation of viral release from host cell [IDA]
- negative regulation of viral transcription [IDA]
- positive regulation of cell cycle [IMP]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of type I interferon production [TAS]
- protein autoubiquitination [IDA]
- protein destabilization [IMP]
- protein monoubiquitination [IDA]
- protein polyubiquitination [IDA]
- protein trimerization [IDA]
- protein ubiquitination [IDA]
- regulation of type I interferon production [TAS]
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
Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.
BACKGROUND: 14-3-3 proteins are abundant and conserved polypeptides that mediate the cellular effects of basophilic protein kinases through their ability to bind specific peptide motifs phosphorylated on serine or threonine. RESULTS: We have used mass spectrometry to analyze proteins that associate with 14-3-3 isoforms in HEK293 cells. This identified 170 unique 14-3-3-associated proteins, which show only modest overlap with previous ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM21 YWHAZ | 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 | - | |
| TRIM21 YWHAZ | 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. | Low | - | BioGRID | - | |
| TRIM21 YWHAZ | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| YWHAZ TRIM21 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - |
Curated By
- BioGRID