BAIT

ACOT13

PNAS-27, THEM2, HT012
acyl-CoA thioesterase 13
GO Process (2)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

ACOT13

PNAS-27, THEM2, HT012
acyl-CoA thioesterase 13
GO Process (2)
GO Function (1)
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 thioesterase superfamily member 2.

Cheng Z, Song F, Shan X, Wei Z, Wang Y, Dunaway-Mariano D, Gong W

Hotdog-fold has been identified in more than 1000 proteins, yet many of which in eukaryotes are less studied. No structural or functional studies of human thioesterase superfamily member 2 (hTHEM2) have been reported before. Since hTHEM2 exhibits about 20% sequence identity to Escherichia coli PaaI protein, it was proposed to be a thioesterase with a hotdog-fold. Here, we report the ... [more]

Biochem. Biophys. Res. Commun. Oct. 13, 2006; 349(1);172-7 [Pubmed: 16934754]

Throughput

  • Low Throughput

Additional Notes

  • ACOT13 crystalized from E. coli was a tetramer

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ACOT13 ACOT13
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
907738
ACOT13 ACOT13
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
887749

Curated By

  • BioGRID