BAIT

C4ORF27

chromosome 4 open reading frame 27
Fanconi Anemia Project
GO Process (0)
GO Function (0)
GO Component (1)

Gene Ontology Cellular Component

Homo sapiens
PREY

HMGN2

HMG17
high mobility group nucleosomal binding domain 2
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Serine ADP-Ribosylation Depends on HPF1.

Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I

ADP-ribosylation (ADPr) regulates important patho-physiological processes through its attachment to different amino acids in proteins. Recently, by precision mapping on all possible amino acid residues, we identified histone serine ADPr marks in the DNA damage response. However, the biochemical basis underlying this serine modification remained unknown. Here we report that serine ADPr is strictly dependent on histone PARylation factor 1 ... [more]

Mol. Cell Feb. 08, 2017; 0(0); [Pubmed: 28190768]

Throughput

  • Low Throughput

Additional Notes

  • HPF1 must be present for in vitro Serine ADP-ribosylation of the substrate by Parp1 in vitro

Curated By

  • BioGRID