Tripartite motif family like 1 (TRIML1)

Tripartite motif family like 1 (TRIML1) is a human protein encoded by the TRIML1 gene, classified within the tripartite motif (TRIM) family of proteins[1][5]. It possesses domains characteristic of E3 ubiquitin-protein ligases, specifically containing a RING finger, B-box(es), and coiled-coil motifs—structural features typical of TRIM family members[1][4]. The complete biological function of TRIML1 in humans remains undetermined; however, data from the mouse ortholog suggest a role in binding ubiquitin-specific protease 5 and importance in blastocyst development[1][3][7]. E3 ubiquitin ligases, including TRIM family proteins more broadly, regulate protein degradation and cellular signaling processes, impacting cell trafficking, DNA repair, and other functions[2][4][6]. While significant disease and therapeutic interest exists for TRIM family proteins, no direct link has yet been established for TRIML1 as a drug target or as a biomarker, and its functional role in disease remains largely speculative based on current evidence[1][4][5]. TRIML1 is best described as a poorly characterized, probable E3 ubiquitin-protein ligase, with established structural classification but lack of clear specific biological or therapeutic function.

Other names

Probable E3 ubiquitin-protein ligase TRIML1RNF209FLJ36180RING finger protein 209RING-type E3 ubiquitin transferase TRIML1Tripartite motif family-like protein 1

None known