Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

Publication

PRISMA and BioID disclose a motifs-based interactome of the intrinsically disordered transcription factor C/EBP?.

Ramberger E, Sapozhnikova V, Kowenz-Leutz E, Zimmermann K, Nicot N, Nazarov PV, Perez-Hernandez D, Reimer U, Mertins P, Dittmar G, Leutz A

C/EBP? represents a paradigm intrinsically disordered transcription factor containing short linear motifs and post-translational modifications (PTM). Unraveling C/EBP? protein interaction networks is a prerequisite for understanding the multi-modal functions of C/EBP? in hematopoiesis and leukemia. Here, we combined arrayed peptide matrix screening (PRISMA) with BioID to generate an in vivo validated and isoform specific interaction map of C/EBP?. The myeloid C/EBP? ... [more]

iScience Jun. 25, 2021; 24(6);102686 [Pubmed: 34189442]

Throughput

  • High Throughput

Additional Notes

  • Used arrayed peptide matrix screening (PRISMA) method
  • significance threshold (FDR less than 0.1)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
EDF1 CEBPA
Reconstituted Complex
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.

Low-BioGRID
-

Curated By

  • BioGRID