Ubiquitin-fold modifier 1

Definition:

Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. Ufmylation of TRIP4 regulates nuclear receptors-mediated transcription.

References:

[1]. Kanako Tatsumi, et al. A novel type of E3 ligase for the Ufm1 conjugation system. J Biol Chem. 2010 Feb 19;285(8):5417-27. [Content Brief]

[2]. Masaaki Komatsu, et al. A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier. EMBO J. 2004 May 5;23(9):1977-86. [Content Brief]

[3]. Hee Min Yoo, et al. Modification of ASC1 by UFM1 is crucial for ERα transactivation and breast cancer development. Mol Cell. 2014 Oct 23;56(2):261-274. [Content Brief]

[4]. Walaa Oweis, et al. Trans-Binding Mechanism of Ubiquitin-like Protein Activation Revealed by a UBA5-UFM1 Complex. Cell Rep. 2016 Sep 20;16(12):3113-3120. [Content Brief]

[5]. Michael S Nahorski, et al. Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation in brain development. Brain. 2018 Jul 1;141(7):1934-1945. [Content Brief]

[6]. Jin Rui Liang, et al. A Genome-wide ER-phagy Screen Highlights Key Roles of Mitochondrial Metabolism and ER-Resident UFMylation. Cell. 2020 Mar 19;180(6):1160-1177.e20. [Content Brief]

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