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J Biol Chem, Vol. 274, Issue 18, 12642-12649, April 30, 1999

Characterization of a Novel Type of Serine/Threonine Kinase That Specifically Phosphorylates the Human Goodpasture Antigen

Angel Raya, Fernando Revert, Samuel Navarro, and Juan Saus

From the  Fundación Valenciana de Investigaciones Biomédicas, Instituto de Investigaciones Citológicas, 46010 Valencia and the  Departamento de Patología, Facultad de Medicina, Universitat de Valencia, 46010 Valencia, Spain

Goodpasture disease is an autoimmune disorder that occurs naturally only in humans. Also exclusive to humans is the phosphorylation process that targets the unique N-terminal region of the Goodpasture antigen. Here we report the molecular cloning of GPBP (Goodpasture antigen-binding protein), a previously unknown 624-residue polypeptide. Although the predicted sequence does not meet the conventional structural requirements for a protein kinase, its recombinant counterpart specifically binds to and phosphorylates the exclusive N-terminal region of the human Goodpasture antigen in vitro. This novel kinase is widely expressed in human tissues but shows preferential expression in the histological structures that are targets of common autoimmune responses. The work presented in this report highlights a novel gene to be explored in human autoimmunity.

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