PREY

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

Structure and functional interactions of the Tsg101 UEV domain.

Pornillos O, Alam SL, Rich RL, Myszka DG, Davis DR, Sundquist WI

Human Tsg101 plays key roles in HIV budding and in cellular vacuolar protein sorting (VPS). In performing these functions, Tsg101 binds both ubiquitin (Ub) and the PTAP tetrapeptide 'late domain' motif located within the viral Gag protein. These interactions are mediated by the N-terminal domain of Tsg101, which belongs to the catalytically inactive ubiquitin E2 variant (UEV) family. We now ... [more]

EMBO J. May. 15, 2002; 21(10);2397-406 [Pubmed: 12006492]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction
  • NMR

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TSG101 UBC
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.

Low-BioGRID
672313
UBC TSG101
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
832378
TSG101 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
3400940
TSG101 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
672334
UBC TSG101
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1066756
UBC TSG101
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1516575
TSG101 UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
3400939
UBC TSG101
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
2296873

Curated By

  • BioGRID