TRIM25 (D9T7G) Rabbit mAb #13773

TRIM25, also termed Estrogen-responsive Finger Protein (EFP), is a member of the tripartite motif-containing (TRIM) family of proteins, characterized by the presence of a RING domain, one or two B-box motifs, and a coiled-coil region (1). TRIM25 was first identified in a search for estrogen-responsive genes (2), and studies have subsequently shown TRIM25 to be overexpressed in many breast cancer tumors (3). A potentially oncogenic role for TRIM25 was suggested by studies showing that suppression of TRIM25 expression inhibited growth of MCF7 cells in vitro and in mouse xenograft models (4). Functional studies largely suggest that TRIM25 functions as a ubiquitin E3 or ISG15 E3 ligase. For example, TRIM25 was shown to induce K63-linked ubiquitination of Rig-I, resulting in Rig-I-mediated activation of downstream signaling cascades that drive the host antiviral innate immune response (5). Notably, it was reported that the influenza A virus non-structural protein 1 inhibits TRIM25-mediated ubiquitination of Rig-I, which may have evolved as a mechanism to evade the host innate immune response (6).