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J Biol Chem. 1999 Apr 30;274(18):12642-9.

Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen.

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  • 1Fundación Valenciana de Investigaciones Biomédicas, Instituto de Investigaciones Citológicas, 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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