BAIT

ACN

Ba, CG10437, CG10473, Dmel\CG10473, dAcn, hkl, l(2)37Ba, Dmel_CG10473
Acinus
GO Process (4)
GO Function (1)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Drosophila melanogaster
PREY

BIN1

150001_at, BcDNA:RE02417, Bin 1, CG6046, Dmel\CG6046, SAP18, bin1/dSAP18, dSAP18, Dmel_CG6046
Bicoid interacting protein 1
Drosophila melanogaster

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex.

Murachelli AG, Ebert J, Basquin C, Le Hir H, Conti E

The ASAP complex interacts with the exon-junction complex (EJC), a messenger ribonucleoprotein complex involved in post-transcriptional regulation. The three ASAP subunits (Acinus, RNPS1 and SAP18) have been individually implicated in transcriptional regulation, pre-mRNA splicing and mRNA quality control. To shed light on the basis for and consequences of ASAP's interaction with the EJC, we have determined the 1.9-A resolution structure ... [more]

Nat. Struct. Mol. Biol. Apr. 01, 2012; 19(4);378-86 [Pubmed: 22388736]

Throughput

  • Low Throughput

Additional Notes

  • table 1, figure 2.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ACN BIN1
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
669871

Curated By

  • BioGRID