RANBP9
Gene Ontology Biological Process
Gene Ontology Molecular Function
MARK2
Gene Ontology Biological Process
- activation of protein kinase activity [TAS]
- establishment of cell polarity [IDA, TAS]
- establishment or maintenance of epithelial cell apical/basal polarity [IDA]
- intracellular signal transduction [IDA]
- mitochondrion degradation [NAS]
- mitochondrion localization [NAS]
- neuron migration [ISS]
- peptidyl-threonine phosphorylation [TAS]
- positive regulation of neuron projection development [IDA]
- protein autophosphorylation [ISS]
- protein phosphorylation [IDA, NAS]
- regulation of axonogenesis [IMP]
- regulation of cytoskeleton organization [ISS]
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 analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis.
Ubiquitination is an essential post-translational modification that regulates protein stability or function. Its substrate specificity is dictated by various E3 ligases. The human C-terminal to LisH (CTLH) complex is a newly discovered multi-subunit really interesting new gene (RING) E3 ligase with only a few known ubiquitination targets. Here, we used mass spectrometry-based proteomic techniques to gain insight into CTLH complex ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RANBP9 MARK2 | 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 | - |
Curated By
- BioGRID