Alternative splicing results in multiple transcript variants encoding different isoforms.

An additional transcript variant has been identified, but its full length sequence has not been determined.

While the exact mechanisms by which SMURF1 contributes to neurodegenerative disorders are still not fully understood, there is growing evidence, research studies may suggest that SMURF1 may be a potential target for therapeutic intervention in protein aggregation and improving cellular proteostasis in neurodegenerative diseases.

The SMURF1 protein is modified by the SCF(FBXL15) complex at two lysine residues, Lys-381 and Lys-383, which leads to its degradation by the proteasome.

The C2 domain plays a crucial role in mediating the interaction of Smurfs with intracellular membranes.