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Significance Ubiquitin fold modifier 1 (UFM1) is a ubiquitin-like posttranslational modifier that is essential for tissue development in metazoans. Genetic ablation of UFM1 or the genes that encode the enzymes that conjugate UFM1 to protein targets causes endoplasmic reticulum (ER) stress, suggesting a role for this modification in ER protein homeostasis. Here, we show that RPL26, a largely uncharacterized ribosomal protein, is the primary cellular target of UFMylation. Ribosomal RPL26 is subject to a dynamic cycle of UFMylation and de-UFMylation, catalyzed by enzymes that are tethered to the cytoplasmic surface of the ER. UFMylated RPL26 and the UFMylation machinery are in close proximity to the SEC61 translocon, suggesting a role for UFMylation in protein biogenesis at the ER.

Ribosomal protein RPL26 is the principal target of UFMylation