MED29
Gene Ontology Molecular Function
Gene Ontology Cellular Component
MED1
Gene Ontology Biological Process
- ERK1 and ERK2 cascade [IDA]
- androgen biosynthetic process [IMP]
- androgen receptor signaling pathway [IDA]
- angiogenesis [ISS]
- cell morphogenesis [IMP]
- cellular lipid metabolic process [TAS]
- cellular response to epidermal growth factor stimulus [IDA]
- cellular response to steroid hormone stimulus [IDA]
- cellular response to thyroid hormone stimulus [IDA]
- erythrocyte development [ISS]
- fat cell differentiation [IDA]
- gene expression [TAS]
- intracellular steroid hormone receptor signaling pathway [IDA]
- keratinocyte differentiation [IMP]
- lens development in camera-type eye [ISS]
- mRNA transcription from RNA polymerase II promoter [ISS]
- megakaryocyte development [ISS]
- negative regulation of apoptotic process [ISS]
- negative regulation of keratinocyte proliferation [IMP]
- negative regulation of neuron differentiation [ISS]
- negative regulation of transcription from RNA polymerase II promoter [ISS]
- positive regulation of gene expression [IDA, IMP]
- positive regulation of keratinocyte differentiation [IMP]
- positive regulation of receptor activity [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription, DNA-templated [IDA]
- regulation of RNA biosynthetic process [IMP]
- regulation of cell cycle [NAS]
- regulation of transcription from RNA polymerase I promoter [IDA]
- small molecule metabolic process [TAS]
- thyroid hormone mediated signaling pathway [IMP]
- transcription initiation from RNA polymerase II promoter [IDA, TAS]
Gene Ontology Molecular Function- LBD domain binding [IPI]
- RNA polymerase II transcription cofactor activity [IDA]
- chromatin binding [IMP]
- core promoter binding [IDA]
- estrogen receptor binding [IPI]
- ligand-dependent nuclear receptor binding [IDA, IPI]
- ligand-dependent nuclear receptor transcription coactivator activity [IMP, NAS]
- mediator complex binding [IDA]
- nuclear hormone receptor binding [IPI]
- peroxisome proliferator activated receptor binding [IPI]
- protein binding [IPI]
- receptor activity [IDA]
- retinoic acid receptor binding [IPI]
- sequence-specific DNA binding RNA polymerase II transcription factor activity [ISS]
- thyroid hormone receptor binding [IDA, IPI]
- thyroid hormone receptor coactivator activity [IMP]
- transcription coactivator activity [IDA, IMP]
- transcription cofactor activity [IDA]
- transcription factor binding [IPI]
- vitamin D receptor binding [IPI, NAS, TAS]
- LBD domain binding [IPI]
- RNA polymerase II transcription cofactor activity [IDA]
- chromatin binding [IMP]
- core promoter binding [IDA]
- estrogen receptor binding [IPI]
- ligand-dependent nuclear receptor binding [IDA, IPI]
- ligand-dependent nuclear receptor transcription coactivator activity [IMP, NAS]
- mediator complex binding [IDA]
- nuclear hormone receptor binding [IPI]
- peroxisome proliferator activated receptor binding [IPI]
- protein binding [IPI]
- receptor activity [IDA]
- retinoic acid receptor binding [IPI]
- sequence-specific DNA binding RNA polymerase II transcription factor activity [ISS]
- thyroid hormone receptor binding [IDA, IPI]
- thyroid hormone receptor coactivator activity [IMP]
- transcription coactivator activity [IDA, IMP]
- transcription cofactor activity [IDA]
- transcription factor binding [IPI]
- vitamin D receptor binding [IPI, NAS, TAS]
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
MED1/TRAP220 exists predominantly in a TRAP/ Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription.
Human TRAP/Mediator is a key coactivator for many transcription factors that act through direct interactions with distinct subunits, and MED1/TRAP220 is the main subunit target for various nuclear receptors. Remarkably, the current study shows that MED1/TRAP220 only exists in a TRAP/Mediator subpopulation (less then 20% of the total) that is greatly enriched in specific TRAP/Mediator subunits and is tightly associated ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| MED29 MED1 | 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 | 3360420 | |
| MED1 MED29 | 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 | 0.9999 | BioGRID | 2226734 | |
| MED29 MED1 | 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 | 1 | BioGRID | 3187976 | |
| MED1 MED29 | 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 | 1 | BioGRID | 3114111 | |
| MED1 MED29 | 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. | Low | - | BioGRID | - | |
| MED1 MED29 | 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 | 24.4415 | BioGRID | 2945217 | |
| MED29 MED1 | 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 | - | |
| MED29 MED1 | 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 | - | |
| MED1 MED29 | 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 | 0.78 | BioGRID | 740876 | |
| MED29 MED1 | 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 | 1 | BioGRID | 1264466 |
Curated By
- BioGRID