Tripartite Motif Containing Protein 50 (TRIM50)

The deduced 487-amino acid protein has an N-terminal RING domain, followed by a B-box type-2 domain, a coiled-coil region, and an RFP (TRIM27)-like/B30.2 domain.Northern blot analysis of several mouse tissues detected high Trim50 expression in stomach, much weaker expression in testis, and little to no expression in other tissues examined. Ectopically expressed mouse Trim50 localized to discrete cytoplasmic foci that partly colocalized with peroxisomes. Expression and mutation analyses revealed that the RING and RFP domains of Trim50 include nuclear localization and export signals, respectively. Crosslinking experiments showed Trim50 trimerized to form a complex of about 250 kD by SDS-PAGE.