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

SEPT9 negatively regulates ubiquitin-dependent downregulation of EGFR.

Diesenberg K, Beerbaum M, Fink U, Schmieder P, Krauss M

Septins constitute a family of GTP-binding proteins that are involved in a variety of biological processes. Several isoforms have been implicated in disease, but the molecular mechanisms underlying pathogenesis are poorly understood. Here, we show that depletion of SEPT9 decreases surface levels of epidermal growth factor receptors (EGFRs) by enhancing receptor degradation. We identify a consensus motif within the SEPT9 ... [more]

J. Cell. Sci. Jan. 15, 2015; 128(2);397-407 [Pubmed: 25472714]

Throughput

Low Throughput

Additional Notes

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
SH3KBP1 SEPT9	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.	Havrylov S (2009)	Low	-	BioGRID	-
SH3KBP1 SEPT9	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Diesenberg K (2015)	Low	-	BioGRID	1241619

Curated By

BioGRID

Interaction Summary

SH3KBP1

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein binding [IPI]

Gene Ontology Cellular Component

SEPT9