HHT2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
STH1
Gene Ontology Biological Process
- ATP-dependent chromatin remodeling [IDA]
- G2/M transition of mitotic cell cycle [IMP]
- base-excision repair [IMP]
- chromatin remodeling at centromere [IMP]
- chromosome segregation [IGI]
- cytoskeleton organization [IGI, IMP]
- double-strand break repair [IMP]
- meiotic nuclear division [IMP]
- nucleosome disassembly [IDA]
- nucleosome positioning [IMP]
- regulation of transcription, DNA-templated [IMP]
- transcription elongation from RNA polymerase II promoter [IDA]
- transfer RNA gene-mediated silencing [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- RSC complex [IDA]
- nucleus [IDA]
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
Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms.
There is a close relationship between histone acetylation and ATP-dependent chromatin remodeling that is not fully understood. We show that acetylation of histone H3 tails affects SWI/SNF (mating type switching/ sucrose non fermenting) and RSC (remodels structure of chromatin) remodeling in several distinct ways. Acetylation of the histone H3 N-terminal tail facilitated recruitment and nucleosome mobilization by the ATP-dependent chromatin ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| STH1 HHT2 | 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 | 3 | BioGRID | 3597322 | |
| STH1 HHT2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| STH1 HHT2 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| STH1 HHT2 | Synthetic Growth Defect Synthetic Growth Defect A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell. | Low | - | BioGRID | 160704 |
Curated By
- BioGRID