TRIM proteins primarily function as ubiquitin ligases that regulate the innate response to infection.

The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family.

[11] Results obtained in human TRIM25 knock-out cells suggest that it may not play a key role in RIG-I activation.

[15][16][17] TRIM25 binds RNAs (either single- or double-stranded) through an RNA-binding domain (RBD) residing in its C-terminal PRY/SPRY region in conjunction with CCD.

[14][12] To avoid IFN production, the non structural protein (NS1) of influenza will interact with CCD domain of TRIM25 to block RIG-I ubiquitination.