SMARCA5
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- ATP-dependent chromatin remodeling [IMP]
- CENP-A containing nucleosome assembly [TAS]
- DNA-templated transcription, initiation [IDA]
- chromatin remodeling [IDA]
- nucleosome assembly [IDA, TAS]
- nucleosome positioning [IDA]
- regulation of transcription from RNA polymerase II promoter [TAS]
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
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.
Publication
Panorama of ancient metazoan macromolecular complexes
Macromolecular complexes are essential to conserved biological processes, but their prevalence across animals is unclear. By combining extensive biochemical fractionation with quantitative mass spectrometry, here we directly examined the composition of soluble multiprotein complexes among diverse metazoan models. Using an integrative approach, we generated a draft conservation map consisting of more than one million putative high-confidence co-complex interactions for species ... [more]
Quantitative Score
- 0.193863157 [Confidence Score]
Throughput
- High Throughput
Additional Notes
- Fractionation was combined with mass spectrometry from five diverse animal species to predict co-complex protein interactions conserved across metazoa using an integrative computational scoring procedure along with an SVM approach. The significant data set of 16655 PPI, was derived from a set of more than 1M interactions by examining a ROC curve of predicted interactions against reference annotated complexes at a 67.5% cumulative precision.
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
SMARCA5 HDAC2 | 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 | - | |
HDAC2 SMARCA5 | 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 | - | |
HDAC2 SMARCA5 | 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 | 0.904 | BioGRID | 741664 | |
SMARCA5 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 | 3432283 | |
SMARCA5 HDAC2 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | 504025 | |
SMARCA5 HDAC2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
HDAC2 SMARCA5 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - |
Curated By
- BioGRID