The thyroid receptor interacting protein-6 (TRIP6) was first identified as a ligand-dependent binding partner for the thyroid hormone receptor in a yeast two-hybrid screen. A partial TRIP6 cDNA clone that was isolated in the initial screen encodes two copies of the LIM domain. The LIM domain is a double zinc-finger structure that mediates protein-protein interactions. Here we report the complete amino acid sequence of human TRIP6. The TRIP6 protein displays a proline-rich N-terminal region linked to three tandemly arrayed C-terminal LIM domains. The global molecular architecture and sequence of TRIP6 place it in the same family as the adhesion plaque protein, zyxin, and the lipoma preferred partner (LPP). Zyxin and LPP are implicated in cellular signaling and tumorigenesis, respectively. By radiation hybrid mapping, the human TRIP6 gene was assigned to a segment of chromosome 7q22 that is commonly deleted in malignant myeloid diseases and uterine leiomyoma.