PARD6A
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PRKCZ
Gene Ontology Biological Process
- blood coagulation [TAS]
- establishment of cell polarity [ISS]
- long-term synaptic potentiation [ISS]
- negative regulation of insulin receptor signaling pathway [IMP]
- negative regulation of peptidyl-tyrosine phosphorylation [IMP]
- negative regulation of protein complex assembly [IMP]
- peptidyl-serine phosphorylation [IDA]
- platelet activation [TAS]
- positive regulation of ERK1 and ERK2 cascade [IMP]
- positive regulation of NF-kappaB transcription factor activity [ISS]
- positive regulation of T-helper 2 cell cytokine production [ISS]
- positive regulation of T-helper 2 cell differentiation [ISS]
- positive regulation of excitatory postsynaptic membrane potential [ISS]
- positive regulation of insulin receptor signaling pathway [ISS]
- positive regulation of interleukin-10 secretion [ISS]
- positive regulation of interleukin-13 secretion [ISS]
- positive regulation of interleukin-4 production [ISS]
- positive regulation of interleukin-5 secretion [ISS]
- protein phosphorylation [IDA]
- signal transduction [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
Protein Scaffolds Control Localized Protein Kinase Cζ Activity.
Atypical protein kinase C (aPKC) isozymes modulate insulin signaling and cell polarity, but how their activity is controlled in cells is not well understood. These enzymes are constitutively phosphorylated, insensitive to second messengers, and have relatively low activity. Here we show that protein scaffolds not only localize but also differentially control the catalytic activity of the aPKC PKCζ, thus promoting ... [more]
Throughput
- Low Throughput
Additional Notes
- interaction inferred from loss of FRET fluorescence: hit protein (a C kinase) binds to bait protein fused to C kinase activity reporter (CKAR) allowing active hit protein variants to phosphorylate the reporter inter-fluorophore spacer disrupting fluorescence resonance energy transfer (FRET)
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PARD6A PRKCZ | 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 | 575446 | |
| PRKCZ PARD6A | 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 | 0.8975 | BioGRID | 2259140 | |
| PRKCZ PARD6A | 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 | 0.9616 | BioGRID | 3120482 | |
| PRKCZ PARD6A | 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 | - | |
| PRKCZ PARD6A | 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 | - | |
| PARD6A PRKCZ | 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 | - | |
| PARD6A PRKCZ | 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 | - | |
| PRKCZ PARD6A | 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 | - | |
| PARD6A PRKCZ | 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 | - | |
| PRKCZ PARD6A | 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. | High | - | BioGRID | - |
Curated By
- BioGRID