BAIT
HIST1H3A
H3/A, H3FA
histone cluster 1, H3a
GO Process (4)
GO Function (1)
GO Component (7)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
YWHAE
AU019196, RP23-78H4.1
tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide
GO Process (8)
GO Function (12)
GO Component (6)
Gene Ontology Biological Process
- cerebral cortex development [IMP]
- hippocampus development [IMP]
- negative regulation of peptidyl-serine dephosphorylation [ISO]
- negative regulation of protein dephosphorylation [IDA]
- neuron migration [IGI, IMP]
- protein targeting [IDA]
- regulation of membrane repolarization [ISO]
- regulation of potassium ion transmembrane transporter activity [ISO]
Gene Ontology Molecular Function- MHC class II protein complex binding [ISO]
- enzyme binding [ISO]
- histone deacetylase binding [ISO]
- ion channel binding [ISO]
- phosphoprotein binding [ISO]
- phosphoserine binding [ISO]
- poly(A) RNA binding [ISO]
- potassium channel regulator activity [ISO]
- protein binding [IPI]
- protein complex binding [ISO]
- protein domain specific binding [IDA]
- protein heterodimerization activity [ISO]
- MHC class II protein complex binding [ISO]
- enzyme binding [ISO]
- histone deacetylase binding [ISO]
- ion channel binding [ISO]
- phosphoprotein binding [ISO]
- phosphoserine binding [ISO]
- poly(A) RNA binding [ISO]
- potassium channel regulator activity [ISO]
- protein binding [IPI]
- protein complex binding [ISO]
- protein domain specific binding [IDA]
- protein heterodimerization activity [ISO]
Gene Ontology Cellular Component
Mus musculus
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
Analysis of phosphorylation-dependent protein-protein interactions of histone h3.
Multiple posttranslational modifications (PTMs) of histone proteins including site-specific phosphorylation of serine and threonine residues govern the accessibility of chromatin. According to the histone code theory, PTMs recruit regulatory proteins or block their access to chromatin. Here, we report a general strategy for simultaneous analysis of both of these effects based on a SILAC MS scheme. We applied this approach ... [more]
ACS Chem. Biol. Jan. 16, 2015; 10(1);138-45 [Pubmed: 25330109]
Throughput
- Low Throughput
Curated By
- BioGRID