BAIT

UBC

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

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens
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

The Crystal Structure and Conformations of an Unbranched Mixed Tri-Ubiquitin Chain Containing K48 and K63 Linkages.

Padala P, Soudah N, Giladi M, Haitin Y, Isupov MN, Wiener R

The ability of ubiquitin to function in a wide range of cellular processes is ascribed to its capacity to cause a diverse spectrum of modifications. While a target protein can be modified with monoubiquitin, it can also be modified with ubiquitin chains. The latter include seven types of homotypic chains as well as mixed ubiquitin chains. In a mixed chain, ... [more]

J. Mol. Biol. Dec. 08, 2016; 429(24);3801-3813 [Pubmed: 29111344]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
UBC 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.

High-BioGRID
948042
UBC 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
932008
UBC 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
1428798
UBC 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
816992
UBC UBC
Proximity Label-MS
Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

High-BioGRID
2658935
UBC UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
948007
UBC UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1428799
UBC UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
3545581

Curated By

  • BioGRID