DAXX
Gene Ontology Biological Process
- activation of JUN kinase activity [TAS]
- androgen receptor signaling pathway [IDA]
- apoptotic process [TAS]
- chromatin remodeling [IDA]
- extrinsic apoptotic signaling pathway via death domain receptors [TAS]
- negative regulation of transcription, DNA-templated [IDA]
- nucleosome assembly [IDA]
- positive regulation of neuron death [IGI]
- positive regulation of protein kinase activity [IGI]
- positive regulation of protein phosphorylation [IGI]
- regulation of protein ubiquitination [IDA]
- regulation of transcription, DNA-templated [IDA]
Gene Ontology Molecular Function- androgen receptor binding [IPI]
- enzyme binding [IPI]
- heat shock protein binding [TAS]
- histone binding [IDA]
- p53 binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- protein kinase activator activity [IGI]
- protein kinase binding [IPI]
- receptor signaling protein activity [TAS]
- transcription corepressor activity [IDA]
- transcription factor binding [IDA]
- ubiquitin protein ligase binding [IPI]
- androgen receptor binding [IPI]
- enzyme binding [IPI]
- heat shock protein binding [TAS]
- histone binding [IDA]
- p53 binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- protein kinase activator activity [IGI]
- protein kinase binding [IPI]
- receptor signaling protein activity [TAS]
- transcription corepressor activity [IDA]
- transcription factor binding [IDA]
- ubiquitin protein ligase binding [IPI]
SUMO2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Characterizing the N- and C-terminal Small ubiquitin-like modifier (SUMO)-interacting motifs of the scaffold protein DAXX.
DAXX is a scaffold protein with diverse roles that often depend upon binding SUMO via its N- and/or C-terminal SUMO-interacting motifs (SIM-N and SIM-C). Using NMR spectroscopy, we characterized the in vitro binding properties of peptide models of SIM-N and SIM-C to SUMO-1 and SUMO-2. In each case, binding was mediated by hydrophobic and electrostatic interactions and weakened with increasing ... [more]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- Likely protein-protein interaction
- interaction detected by NMR
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DAXX SUMO2 | 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 | 685659 | |
| SUMO2 DAXX | 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 | 1101142 | |
| SUMO2 DAXX | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | High | - | BioGRID | 2878203 | |
| DAXX SUMO2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 610801 | |
| SUMO2 DAXX | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | High | - | BioGRID | 1101192 | |
| DAXX SUMO2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 1101148 | |
| DAXX SUMO2 | 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 | 685654 | |
| DAXX SUMO2 | 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 | - | |
| DAXX SUMO2 | 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 | 1101158 |
Curated By
- BioGRID