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PMID:8797804

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Citation

De Valck, D, Heyninck, K, Van Criekinge, W, Contreras, R, Beyaert, R and Fiers, W (1996) A20, an inhibitor of cell death, self-associates by its zinc finger domain. FEBS Lett. 384:61-4

Abstract

A20 is a primary response gene which is induced after monocyte adherence or cytokine stimulation of a variety of cells. The A20 protein belongs to a novel class of Cys2/Cys2 zinc finger proteins, and has been characterized as an inhibitor of both apoptotic and necrotic cell death. In order to clarify its molecular mechanism of action, we used the yeast-based two-hybrid system to screen for A20-associated proteins. Here we report that A20 is able to self-associate, and demonstrate that the latter interaction is mediated by its zinc finger domain.

Links

PubMed

Keywords

Base Sequence; Binding Sites; Breast Neoplasms; Cell Death; Cell Line; Cloning, Molecular; Cysteine; DNA Primers; Female; Gene Expression/drug effects; Humans; Intracellular Signaling Peptides and Proteins; Molecular Sequence Data; Nuclear Proteins; Polymerase Chain Reaction; Protein Binding; Protein Biosynthesis; Proteins/isolation & purification; Proteins/metabolism; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/isolation & purification; Recombinant Proteins/pharmacology; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha/pharmacology; Zinc Fingers

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:TNAP3

enables

GO:0043621: protein self-association

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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