BAIT
EP300
KAT3B, RSTS2, p300, RP1-85F18.1
E1A binding protein p300
GO Process (29)
GO Function (15)
GO Component (3)
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- N-terminal peptidyl-lysine acetylation [IDA]
- Notch signaling pathway [TAS]
- apoptotic process [IMP]
- cellular response to hypoxia [TAS]
- chromatin organization [TAS]
- circadian rhythm [ISS]
- histone H2B acetylation [IDA]
- histone H4 acetylation [IMP]
- innate immune response [TAS]
- internal peptidyl-lysine acetylation [IDA]
- internal protein amino acid acetylation [IDA]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [IDA]
- mitotic cell cycle [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- nervous system development [TAS]
- positive regulation by host of viral transcription [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response [ISS]
- positive regulation of type I interferon production [TAS]
- protein stabilization [ISS]
- regulation of androgen receptor signaling pathway [IDA]
- regulation of cell cycle [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of transcription, DNA-templated [IDA]
- regulation of tubulin deacetylation [IDA]
- response to estrogen [IDA]
- response to hypoxia [IDA]
Gene Ontology Molecular Function- DNA binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- acetyltransferase activity [IDA, IMP]
- activating transcription factor binding [IPI]
- androgen receptor binding [IPI]
- beta-catenin binding [IPI]
- chromatin binding [IMP]
- core promoter binding [IDA]
- histone acetyltransferase activity [IDA]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA]
- nuclear hormone receptor binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- transferase activity, transferring acyl groups [IDA]
- DNA binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- acetyltransferase activity [IDA, IMP]
- activating transcription factor binding [IPI]
- androgen receptor binding [IPI]
- beta-catenin binding [IPI]
- chromatin binding [IMP]
- core promoter binding [IDA]
- histone acetyltransferase activity [IDA]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA]
- nuclear hormone receptor binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- transferase activity, transferring acyl groups [IDA]
Homo sapiens
PREY
ALDOA
ALDA, GSD12, HEL-S-87p
aldolase A, fructose-bisphosphate
GO Process (16)
GO Function (8)
GO Component (9)
Gene Ontology Biological Process
- ATP biosynthetic process [IMP]
- actin filament organization [TAS]
- blood coagulation [TAS]
- carbohydrate metabolic process [TAS]
- fructose 1,6-bisphosphate metabolic process [IDA]
- fructose metabolic process [IMP]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [IMP, TAS]
- muscle cell cellular homeostasis [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- protein homotetramerization [ISS]
- regulation of cell shape [IDA]
- small molecule metabolic process [TAS]
- striated muscle contraction [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
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.
Publication
Acetylation of ELF5 suppresses breast cancer progression by promoting its degradation and targeting CCND1.
E74-like ETS transcription factor 5 (ELF5) is involved in a wide spectrum of biological processes, e.g., mammogenesis and tumor progression. We have identified a list of p300-interacting proteins in human breast cancer cells. Among these, ELF5 was found to interact with p300 via acetylation, and the potential acetylation sites were identified as K130, K134, K143, K197, K228, and K245. Furthermore, ... [more]
NPJ Precis Oncol Mar. 19, 2021; 5(1);20 [Pubmed: 33742100]
Throughput
- Low Throughput
Curated By
- BioGRID