BAIT

UBC

HMG20
ubiquitin C
GO Process (75)
GO Function (3)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens

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

Conformational and dynamic changes at the interface contribute to ligand binding by ubiquitin.

Sundd M

Ubiquitin interacts with numerous domains and motifs in its lifetime that vary in structure but bind the same hydrophobic patch. To identify the structural features of ubiquitin that make it an exceptional protein-protein interaction partner, we have studied the interaction of ubiquitin with the signal transducing adaptor molecule-1 ubiquitin interacting motif (UIM) using nuclear magnetic resonance. Our studies bring to ... [more]

Biochemistry Oct. 16, 2012; 51(41);8111-24 [Pubmed: 23035694]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction
  • NMR

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
STAM UBC
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
437592
STAM UBC
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
676614
STAM UBC
Protein-peptide
Protein-peptide

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

Low-BioGRID
1101096
STAM UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1516472
UBC STAM
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1516578
STAM UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
428384
STAM UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
814659
UBC STAM
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
814448
UBC STAM
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1060015
UBC STAM
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
2881136
UBC STAM
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
2297016

Curated By

  • BioGRID