EP300
- Aliases
-
- E1A binding protein p300
- E1A-associated protein p300
- E1A-binding protein, 300kD
- EC 2.3.1.48
- EP300
- KAT3B
- P300
- RSTS2
- histone acetyltransferase p300
- p300
- p300 HAT
- Description
- EP300, or E1A binding protein p300, functions as a histone acetyltransferase and regulates transcription via chromatin remodeling. EP300 is important in the processes of cell proliferation and differentiation, and also functions as acetyltransferase for nonhistone targets. EP300 mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. This gene has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and thus plays a role in the stimulation of hypoxia-induced genes such as VEGF.
Attributes
- QA State
- Curated
- Type
- Protein
- HGNC Name
- EP300
- Certifications
-
- None
- QA State for Breast
- Under Review
Non-Public Biomarker
Organ-specific information for this biomarker is currently being annotated or is "under review". Logging in may give you privileges to view additional information. Contact the Informatics Center if you believe you should have access.
Non-Public Biomarker
Organ-specific information for this biomarker is currently being annotated or is "under review". Logging in may give you privileges to view additional information. Contact the Informatics Center if you believe you should have access.
- Development and validation of sandwich ELISA microarrays with minimal assay interference.
- Discovery and preliminary confirmation of novel early detection biomarkers for triple-negative breast cancer using preclinical plasma samples from the Women's Health Initiative observational study.
- Plasma biomarker profiles differ depending on breast cancer subtype but RANTES is consistently increased.
Non-Public Biomarker
Organ-specific information for this biomarker is currently being annotated or is "under review". Logging in may give you privileges to view additional information. Contact the Informatics Center if you believe you should have access.