AR
Gene Ontology Biological Process
- androgen receptor signaling pathway [IDA]
- cell growth [NAS]
- cell proliferation [NAS]
- cell-cell signaling [TAS]
- gene expression [TAS]
- intracellular receptor signaling pathway [IDA]
- negative regulation of extrinsic apoptotic signaling pathway [IDA]
- negative regulation of integrin biosynthetic process [IDA]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of cell proliferation [IDA]
- positive regulation of integrin biosynthetic process [IDA]
- positive regulation of phosphorylation [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase III promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- prostate gland development [NAS]
- protein oligomerization [IDA]
- regulation of establishment of protein localization to plasma membrane [IDA]
- sex differentiation [NAS]
- signal transduction [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [IDA]
- transport [TAS]
Gene Ontology Molecular Function- DNA binding [NAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- RNA polymerase II transcription factor binding [IPI]
- androgen binding [NAS]
- androgen receptor activity [IDA, IMP, NAS, TAS]
- beta-catenin binding [IDA, IPI, TAS]
- chromatin binding [IDA]
- enzyme binding [IPI]
- ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IDA]
- protein binding [IPI]
- protein dimerization activity [NAS]
- receptor binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
- DNA binding [NAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- RNA polymerase II transcription factor binding [IPI]
- androgen binding [NAS]
- androgen receptor activity [IDA, IMP, NAS, TAS]
- beta-catenin binding [IDA, IPI, TAS]
- chromatin binding [IDA]
- enzyme binding [IPI]
- ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IDA]
- protein binding [IPI]
- protein dimerization activity [NAS]
- receptor binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
Gene Ontology Cellular Component
NELFCD
Gene Ontology Biological Process
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
Trihydrophobin 1 attenuates androgen signal transduction through promoting androgen receptor degradation.
The androgen-signaling pathway plays critical roles in normal prostate development, benign prostatic hyperplasia, established prostate cancer, and in prostate carcinogenesis. In this study, we report that trihydrophobin 1 (TH1) is a potent negative regulator to attenuate the androgen signal-transduction cascade through promoting androgen receptor (AR) degradation. TH1 interacts with AR both in vitro and in vivo, decreases the stability of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| AR NELFCD | 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 | - | |
| NELFCD AR | 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 | - | |
| NELFCD AR | 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 | - |
Curated By
- BioGRID