OGT
Gene Ontology Biological Process
- apoptotic process [IDA]
- cellular response to retinoic acid [IMP]
- chromatin organization [TAS]
- circadian regulation of gene expression [ISS]
- histone H3-K4 trimethylation [IMP]
- histone H4-K16 acetylation [IDA]
- histone H4-K5 acetylation [IDA]
- histone H4-K8 acetylation [IDA]
- negative regulation of protein ubiquitination [ISS]
- phosphatidylinositol-mediated signaling [IDA]
- positive regulation of catalytic activity [IDA]
- positive regulation of granulocyte differentiation [IMP]
- positive regulation of histone H3-K27 methylation [IMP]
- positive regulation of histone H3-K4 methylation [IDA]
- positive regulation of proteolysis [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- protein O-linked glycosylation [IDA, IMP]
- regulation of Rac protein signal transduction [IDA]
- regulation of gluconeogenesis involved in cellular glucose homeostasis [ISS]
- regulation of glycolytic process [IDA]
- regulation of insulin receptor signaling pathway [IDA]
- response to insulin [IDA]
- response to nutrient [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function- acetylglucosaminyltransferase activity [TAS]
- enzyme activator activity [IDA]
- histone acetyltransferase activity (H4-K16 specific) [IDA]
- histone acetyltransferase activity (H4-K5 specific) [IDA]
- histone acetyltransferase activity (H4-K8 specific) [IDA]
- phosphatidylinositol-3,4,5-trisphosphate binding [IDA]
- protein N-acetylglucosaminyltransferase activity [IDA]
- protein O-GlcNAc transferase activity [IMP, ISS]
- protein binding [IPI]
- acetylglucosaminyltransferase activity [TAS]
- enzyme activator activity [IDA]
- histone acetyltransferase activity (H4-K16 specific) [IDA]
- histone acetyltransferase activity (H4-K5 specific) [IDA]
- histone acetyltransferase activity (H4-K8 specific) [IDA]
- phosphatidylinositol-3,4,5-trisphosphate binding [IDA]
- protein N-acetylglucosaminyltransferase activity [IDA]
- protein O-GlcNAc transferase activity [IMP, ISS]
- protein binding [IPI]
Gene Ontology Cellular Component
FARSA
Gene Ontology Biological Process
Gene Ontology Molecular Function
Co-fractionation
Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.
Publication
Panorama of ancient metazoan macromolecular complexes
Macromolecular complexes are essential to conserved biological processes, but their prevalence across animals is unclear. By combining extensive biochemical fractionation with quantitative mass spectrometry, here we directly examined the composition of soluble multiprotein complexes among diverse metazoan models. Using an integrative approach, we generated a draft conservation map consisting of more than one million putative high-confidence co-complex interactions for species ... [more]
Quantitative Score
- 0.126552686 [Confidence Score]
Throughput
- High Throughput
Additional Notes
- Fractionation was combined with mass spectrometry from five diverse animal species to predict co-complex protein interactions conserved across metazoa using an integrative computational scoring procedure along with an SVM approach. The significant data set of 16655 PPI, was derived from a set of more than 1M interactions by examining a ROC curve of predicted interactions against reference annotated complexes at a 67.5% cumulative precision.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| OGT FARSA | 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 | - |
Curated By
- BioGRID