CREBBP
Gene Ontology Biological Process
- N-terminal peptidyl-lysine acetylation [IDA]
- Notch signaling pathway [TAS]
- cellular lipid metabolic process [TAS]
- cellular response to hypoxia [TAS]
- chromatin organization [TAS]
- embryonic digit morphogenesis [TAS]
- gene expression [TAS]
- histone acetylation [IDA]
- homeostatic process [NAS]
- innate immune response [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA, ISS]
- positive regulation of type I interferon production [TAS]
- protein complex assembly [TAS]
- regulation of smoothened signaling pathway [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of transcription, DNA-templated [IDA, TAS]
- response to hypoxia [TAS]
- signal transduction [NAS]
- small molecule metabolic process [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- MRF binding [IDA]
- RNA polymerase II activating transcription factor binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- RNA polymerase II transcription coactivator activity [TAS]
- RNA polymerase II transcription factor binding [IPI]
- RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription [IDA]
- acetyltransferase activity [IDA]
- core promoter proximal region sequence-specific DNA binding [IDA]
- histone acetyltransferase activity [IDA]
- p53 binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- signal transducer activity [TAS]
- transcription coactivator activity [IDA, IPI]
- transcription factor binding [IPI]
- MRF binding [IDA]
- RNA polymerase II activating transcription factor binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- RNA polymerase II transcription coactivator activity [TAS]
- RNA polymerase II transcription factor binding [IPI]
- RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription [IDA]
- acetyltransferase activity [IDA]
- core promoter proximal region sequence-specific DNA binding [IDA]
- histone acetyltransferase activity [IDA]
- p53 binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- signal transducer activity [TAS]
- transcription coactivator activity [IDA, IPI]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
- cytoplasm [IDA]
- nuclear body [IDA]
- nuclear chromatin [IDA]
- nucleoplasm [IDA, TAS]
- nucleus [IC, IDA]
MAPT
Gene Ontology Biological Process
- apoptotic process [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- generation of neurons [NAS]
- microtubule cytoskeleton organization [IDA]
- positive regulation of axon extension [IDA]
- positive regulation of microtubule polymerization [IDA]
- regulation of autophagy [IGI]
- regulation of microtubule polymerization [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Acetylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Intrinsic Tau Acetylation Is Coupled to Auto-Proteolytic Tau Fragmentation.
Tau proteins are abnormally aggregated in a range of neurodegenerative tauopathies including Alzheimer's disease (AD). Recently, tau has emerged as an extensively post-translationally modified protein, among which lysine acetylation is critical for normal tau function and its pathological aggregation. Here, we demonstrate that tau isoforms have different propensities to undergo lysine acetylation, with auto-acetylation occurring more prominently within the lysine-rich ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID