BAIT

ZFAND5

ZA20D2, ZFAND5A, ZNF216, RP11-63P12.8
zinc finger, AN1-type domain 5
GO Process (0)
GO Function (1)
GO Component (0)

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

Independent interactions of ubiquitin-binding domains in a ubiquitin-mediated ternary complex.

Garner TP, Strachan J, Shedden EC, Long JE, Cavey JR, Shaw B, Layfield R, Searle MS

Ubiquitin (Ub) modifications are transduced by receptor proteins that use Ub-binding domains (UBDs) to recognize distinct interaction faces on the Ub surface. We report the nuclear magnetic resonance (NMR) solution structures of the A20-like zinc finger (A20 Znf) UBD of the Ub receptor ZNF216, and its complex with Ub, and show that the binding surface on Ub centered on Asp58 ... [more]

Biochemistry Oct. 25, 2011; 50(42);9076-87 [Pubmed: 21923101]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction
  • nmr

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ZFAND5 UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
2574929

Curated By

  • BioGRID