CLOCK
Gene Ontology Biological Process
- DNA damage checkpoint [IMP]
- cellular response to ionizing radiation [IDA]
- chromatin organization [TAS]
- circadian regulation of gene expression [IDA, IMP, ISS]
- circadian rhythm [TAS]
- histone acetylation [IMP]
- negative regulation of glucocorticoid receptor signaling pathway [ISS]
- negative regulation of transcription, DNA-templated [ISS]
- photoperiodism [TAS]
- positive regulation of NF-kappaB transcription factor activity [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IGI]
- positive regulation of transcription, DNA-templated [IDA, ISS]
- proteasome-mediated ubiquitin-dependent protein catabolic process [ISS]
- regulation of hair cycle [IMP]
- regulation of insulin secretion [ISS]
- regulation of transcription from RNA polymerase II promoter [TAS]
- regulation of transcription, DNA-templated [ISS]
- regulation of type B pancreatic cell development [ISS]
- response to redox state [IDA]
- spermatogenesis [ISS]
Gene Ontology Molecular Function- DNA binding [IDA]
- E-box binding [IDA]
- 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 [ISS]
- RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription [ISS]
- chromatin DNA binding [ISS]
- core promoter binding [ISS]
- histone acetyltransferase activity [IMP]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- sequence-specific DNA binding transcription factor activity [ISS]
- DNA binding [IDA]
- E-box binding [IDA]
- 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 [ISS]
- RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription [ISS]
- chromatin DNA binding [ISS]
- core promoter binding [ISS]
- histone acetyltransferase activity [IMP]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- sequence-specific DNA binding transcription factor activity [ISS]
Gene Ontology Cellular Component
ARNTL
Gene Ontology Biological Process
- circadian regulation of gene expression [IDA, ISS]
- circadian rhythm [TAS]
- negative regulation of TOR signaling [ISS]
- negative regulation of fat cell differentiation [ISS]
- negative regulation of glucocorticoid receptor signaling pathway [ISS]
- negative regulation of transcription, DNA-templated [ISS]
- oxidative stress-induced premature senescence [ISS]
- positive regulation of canonical Wnt signaling pathway [ISS]
- positive regulation of circadian rhythm [ISS]
- positive regulation of skeletal muscle cell differentiation [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IGI]
- positive regulation of transcription, DNA-templated [IDA, IMP]
- proteasome-mediated ubiquitin-dependent protein catabolic process [ISS]
- regulation of cell cycle [ISS]
- regulation of cellular senescence [ISS]
- regulation of hair cycle [IMP]
- regulation of insulin secretion [ISS]
- regulation of neurogenesis [ISS]
- regulation of transcription, DNA-templated [ISS]
- regulation of type B pancreatic cell development [ISS]
- response to redox state [IDA]
- spermatogenesis [ISS]
Gene Ontology Molecular Function- DNA binding [IDA, IGI]
- E-box binding [IDA]
- Hsp90 protein binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity [ISS]
- aryl hydrocarbon receptor binding [IPI]
- core promoter binding [ISS]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- transcription regulatory region sequence-specific DNA binding [ISS]
- DNA binding [IDA, IGI]
- E-box binding [IDA]
- Hsp90 protein binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity [ISS]
- aryl hydrocarbon receptor binding [IPI]
- core promoter binding [ISS]
- protein binding [IPI]
- sequence-specific DNA binding [ISS]
- transcription regulatory region sequence-specific DNA binding [ISS]
Gene Ontology Cellular Component
PCA
A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.
Publication
Sumoylation controls CLOCK-BMAL1-mediated clock resetting via CBP recruitment in nuclear transcriptional foci.
CLOCK-BMAL1 is a key transcription factor complex of the molecular clock system that generates circadian gene expression and physiology in mammals. Here, we demonstrate that sumoylation of BMAL1 mediates the rapid activation of CLOCK-BMAL1 by CREB-binding protein (CBP) in nuclear foci and also the resetting of the circadian clock. Under physiological conditions, a bimolecular fluorescence complementation-based fluorescence resonance energy transfer ... [more]
Throughput
- Low Throughput
Additional Notes
- BiFC assay
- Figure 1
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ARNTL CLOCK | Affinity Capture-Luminescence Affinity Capture-Luminescence An interaction is inferred when a bait protein, tagged with luciferase, is enzymatically detected in immunoprecipitates of the prey protein as light emission. The prey protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag. | Low | - | BioGRID | - | |
| ARNTL CLOCK | 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 | - | |
| ARNTL CLOCK | 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 | 2219675 | |
| CLOCK ARNTL | 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 | 3056441 | |
| CLOCK ARNTL | 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 | - | |
| ARNTL CLOCK | 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 | - | |
| CLOCK ARNTL | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
| CLOCK ARNTL | 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 | - | |
| ARNTL CLOCK | 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 | 2535899 | |
| CLOCK ARNTL | 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 | 2535901 | |
| ARNTL CLOCK | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | 2724025 | |
| ARNTL CLOCK | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| CLOCK ARNTL | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| CLOCK ARNTL | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| ARNTL CLOCK | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID