BAIT

OTUB2

C14orf137, OTB2, OTU2
OTU deubiquitinase, ubiquitin aldehyde binding 2
GO Process (4)
GO Function (1)
GO Component (1)
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

Biochemical Activity (Deubiquitination)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.

Altun M, Walter TS, Kramer HB, Herr P, Iphoefer A, Bostroem J, David Y, Komsany A, Ternette N, Navon A, Stuart DI, Ren J, Kessler BM

Ovarian tumor domain containing proteases cleave ubiquitin (Ub) and ubiquitin-like polypeptides from proteins. Here we report the crystal structure of human otubain 2 (OTUB2) in complex with a ubiquitin-based covalent inhibitor, Ub-Br2. The ubiquitin binding mode is oriented differently to how viral otubains (vOTUs) bind ubiquitin/ISG15, and more similar to yeast and mammalian OTUs. In contrast to OTUB1 which has ... [more]

PLoS ONE Jan. 16, 2015; 10(1);e0115344 [Pubmed: 25590432]

Throughput

  • Low Throughput

Additional Notes

  • OTUB2 cleaves a broader range of di-Ub linked by naturally occurring isopeptide linkages with a preference for Lys63 di-Ub
  • OTUB2 exhibits a more permissive cleavage profile including Lys48-, Lys63 (di/tetra-Ub)-and K6/K11 (di-Ub)-linkages

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
OTUB2 UBC
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Low-BioGRID
946847
OTUB2 UBC
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Low-BioGRID
950463
OTUB2 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
1253974
UBC OTUB2
Protein-peptide
Protein-peptide

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

High-BioGRID
2904527
UBC OTUB2
Reconstituted Complex
Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Low-BioGRID
2446298

Curated By

  • BioGRID