SUV39H1
Gene Ontology Biological Process
- cellular response to DNA damage stimulus [IDA]
- cellular response to hypoxia [IDA]
- chromatin organization [TAS]
- chromatin silencing at rDNA [IDA]
- histone H3-K9 dimethylation [ISS]
- histone H3-K9 trimethylation [ISS]
- negative regulation of circadian rhythm [ISS]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of transcription, DNA-templated [ISS]
Gene Ontology Molecular Function- S-adenosylmethionine-dependent methyltransferase activity [IDA]
- chromatin binding [TAS]
- histone methyltransferase activity [IDA]
- histone methyltransferase activity (H3-K9 specific) [IDA]
- histone-lysine N-methyltransferase activity [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- transcription regulatory region sequence-specific DNA binding [ISS]
- S-adenosylmethionine-dependent methyltransferase activity [IDA]
- chromatin binding [TAS]
- histone methyltransferase activity [IDA]
- histone methyltransferase activity (H3-K9 specific) [IDA]
- histone-lysine N-methyltransferase activity [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- transcription regulatory region sequence-specific DNA binding [ISS]
Gene Ontology Cellular Component
HDLBP
Gene Ontology Molecular Function
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
On the mechanism of induction of heterochromatin by the RNA-binding protein vigilin.
Vigilin is an RNA-binding protein localized to both the cytoplasm and the nucleus and has been previously implicated in heterochromatin formation and chromosome segregation. We demonstrate here that the C-terminal domain of human vigilin binds to the histone methyltransferase SUV39H1 in vivo. This association is independent of RNA and maps to a site on vigilin that is not involved in ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID