SMARCC2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HDAC2
Gene Ontology Biological Process
- ATP-dependent chromatin remodeling [IDA]
- blood coagulation [TAS]
- chromatin remodeling [IC]
- circadian regulation of gene expression [ISS]
- dendrite development [ISS]
- embryonic digit morphogenesis [ISS]
- epidermal cell differentiation [ISS]
- eyelid development in camera-type eye [ISS]
- fungiform papilla formation [ISS]
- hair follicle placode formation [ISS]
- histone H3 deacetylation [ISS]
- histone H4 deacetylation [ISS]
- histone deacetylation [IMP]
- maintenance of chromatin silencing [IMP]
- negative regulation of MHC class II biosynthetic process [IC]
- negative regulation of apoptotic process [ISS]
- negative regulation of cell cycle [TAS]
- negative regulation of neuron projection development [ISS]
- negative regulation of sequence-specific DNA binding transcription factor activity [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of transcription, DNA-templated [IC, IMP]
- neurotrophin TRK receptor signaling pathway [TAS]
- odontogenesis of dentin-containing tooth [ISS]
- positive regulation of cell proliferation [IMP]
- positive regulation of collagen biosynthetic process [IC]
- positive regulation of proteolysis [IMP]
- positive regulation of receptor biosynthetic process [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription, DNA-templated [IC]
Gene Ontology Molecular Function- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II repressing transcription factor binding [IPI]
- chromatin binding [ISS]
- deacetylase activity [ISS]
- enzyme binding [IPI]
- histone deacetylase activity [IDA]
- nucleosomal DNA binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein deacetylase activity [IMP]
- sequence-specific DNA binding [IDA]
- transcription factor binding [IPI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II repressing transcription factor binding [IPI]
- chromatin binding [ISS]
- deacetylase activity [ISS]
- enzyme binding [IPI]
- histone deacetylase activity [IDA]
- nucleosomal DNA binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein deacetylase activity [IMP]
- sequence-specific DNA binding [IDA]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
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.
Publication
REST repression of neuronal genes requires components of the hSWI.SNF complex.
A function of the transcription factor REST is to block the expression of neuronal phenotypic traits in non-neuronal cells. Previous studies have shown that REST-mediated repression requires histone deacetylase activity and that recruitment of deacetylases is mediated by two co-repressors, Sin3A and CoREST. In this study, we show that a repressor domain in CoREST interacts with BRG1-associated factor (BAF) 57, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| SMARCC2 HDAC2 | 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 | 3452874 |
Curated By
- BioGRID