BAIT

HIST1H2BA

H2BFU, STBP, TSH2B, TSH2B.1, bA317E16.3
histone cluster 1, H2ba
GO Process (4)
GO Function (0)
GO Component (3)
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

PARP1 ADP-ribosylates lysine residues of the core histone tails.

Messner S, Altmeyer M, Zhao H, Pozivil A, Roschitzki B, Gehrig P, Rutishauser D, Huang D, Caflisch A, Hottiger MO

The chromatin-associated enzyme PARP1 has previously been suggested to ADP-ribosylate histones, but the specific ADP-ribose acceptor sites have remained enigmatic. Here, we show that PARP1 covalently ADP-ribosylates the amino-terminal histone tails of all core histones. Using biochemical tools and novel electron transfer dissociation mass spectrometric protocols, we identify for the first time K13 of H2A, K30 of H2B, K27 and ... [more]

Nucleic Acids Res. Oct. 01, 2010; 38(19);6350-62 [Pubmed: 20525793]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HIST1H2BA PARP1
Affinity Capture-MS
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.

High0.9398BioGRID
1197144
HIST1H2BA PARP1
Affinity Capture-MS
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.

High0.9507BioGRID
2251687

Curated By

  • BioGRID