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-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.

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

  • figure 1c.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ACN BIN1
Co-crystal Structure
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.

Low-BioGRID
669873

Curated By

  • BioGRID