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Tripartite motif family-like protein 2 (TRIML2) is a protein-coding gene in the TRIM family, characterized by the presence of a RING domain, B-box, coiled-coil, and a C-terminal PRY/SPRY (also called B30.2) domain. The PRY/SPRY domain is involved in substrate/protein recognition and protein-protein interactions, and is known in other TRIM proteins to participate in innate immunity and antiviral functions. TRIML2 is a probable E3 ubiquitin-protein ligase, and may be regulated by the tumor suppressor p53 and also enhance p53 SUMOylation, suggesting a possible regulatory influence on p53-mediated cell functions. Multiple transcript variants exist due to alternative splicing. There is limited direct evidence for TRIML2 as a therapeutic target or for interacting drugs; its primary annotation is as a probable ligase, and functional paralogs include TRIML1. Disease association is minimal, with links mainly to a rare genetic syndrome rather than prominent therapeutic areas like cancer or inflammation.
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