SNW1
Gene Ontology Biological Process
- Notch signaling pathway [TAS]
- cellular response to retinoic acid [IDA]
- gene expression [TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [IMP]
- mRNA splicing, via spliceosome [IC, IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- positive regulation by host of viral transcription [IDA, IMP]
- positive regulation of histone H3-K4 methylation [IMP]
- positive regulation of mRNA splicing, via spliceosome [IMP]
- positive regulation of neurogenesis [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transforming growth factor beta receptor signaling pathway [IDA]
- positive regulation of vitamin D receptor signaling pathway [IDA]
- regulation of retinoic acid receptor signaling pathway [IDA]
- regulation of transcription from RNA polymerase II promoter [TAS]
- regulation of vitamin D receptor signaling pathway [IDA]
- retinoic acid receptor signaling pathway [IDA]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
EEF1G
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing.
Nuclear coactivator-62 kDa/Ski-interacting protein (NCoA62/SKIP) is a putative vitamin D receptor (VDR) and nuclear receptor coactivator protein that is unrelated to other VDR coactivators such as those in the steroid receptor coactivator (SRC) family. The mechanism through which NCoA62/SKIP functions in VDR-activated transcription is unknown. In the present study, we identified a nuclear localization sequence in the COOH terminus of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EEF1G SNW1 | 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 | 3441107 | |
| EEF1G SNW1 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3792022 |
Curated By
- BioGRID