BAIT
AUH
AU RNA binding protein/enoyl-CoA hydratase
GO Process (3)
GO Function (3)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
AUH
AU RNA binding protein/enoyl-CoA hydratase
GO Process (3)
GO Function (3)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase.
BACKGROUND: The AU binding homolog of enoyl-CoA hydratase (AUH) is a bifunctional protein that has two distinct activities: AUH binds to RNA and weakly catalyzes the hydration of 2-trans-enoyl-coenzyme A (enoyl-CoA). AUH has no sequence similarity with other known RNA binding proteins, but it has considerable sequence similarity with enoyl-CoA hydratase. A segment of AUH, named the R peptide, binds ... [more]
Structure Dec. 01, 2001; 9(12);1253-63 [Pubmed: 11738050]
Throughput
- Low Throughput
Curated By
- BioGRID