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

Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain.

Hirano S, Suzuki N, Slagsvold T, Kawasaki M, Trambaiolo D, Kato R, Stenmark H, Wakatsuki S

ESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE-Ub complex structure, Ub binds far from the proposed PI-binding site ... [more]

Nat. Struct. Mol. Biol. Nov. 01, 2006; 13(11);1031-2 [Pubmed: 17057714]

Throughput

Low Throughput

Additional Notes

#LPPI
Likely protein-protein interaction

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
VPS36 UBC	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Hirano S (2006)	Low	-	BioGRID	672099
UBC VPS36	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Zhang X (2017)	High	-	BioGRID	2297366

Curated By

BioGRID

Interaction Summary

VPS36

Gene Ontology Biological Process

Gene Ontology Molecular Function

ubiquitin binding [IDA]

Gene Ontology Cellular Component

UBC