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.

Publication

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.

Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F

Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin synthesis. When isolated from tissue, AANAT copurifies with isoforms epsilon and zeta of 14-3-3. We have determined the structure of AANAT bound to 14-3-3zeta, an association that is phosphorylation dependent. AANAT is bound in the central channel of the 14-3-3zeta dimer, and is held in place by extensive interactions both with ... [more]

Cell Apr. 20, 2001; 105(2);257-67 [Pubmed: 11336675]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
YWHAZ AANAT	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.	Obsil T (2001)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

YWHAZ

Gene Ontology Biological Process

Gene Ontology Molecular Function

identical protein binding [IPI]poly(A) RNA binding [IDA]protein binding [IPI]protein kinase binding [IPI]transcription factor binding [IPI]

Gene Ontology Cellular Component

AANAT