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
RBBP4
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- ATP-dependent chromatin remodeling [IDA]
- CENP-A containing nucleosome assembly [TAS]
- DNA replication-dependent nucleosome assembly [IDA]
- DNA replication-independent nucleosome assembly [IDA]
- G2/M transition of mitotic cell cycle [TAS]
- chromatin assembly [IDA]
- chromatin remodeling [IDA]
- mitotic cell cycle [TAS]
- negative regulation of cell proliferation [TAS]
- nucleosome assembly [TAS]
- regulation of cell cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Mutual regulation between OGT and XIAP to control colon cancer cell growth and invasion.
O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer. However, the mechanism regulating its expression in cancer cells is not well understood. This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| OGT RBBP4 | Co-fractionation 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. | High | - | BioGRID | 3431102 |
Curated By
- BioGRID