Ubiquitin-conjugating enzyme E2 J1

Definition:

Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) and is essential for cells to recover from ER stress. Plays a role in MAPKAPK2-dependent translational control of TNF-alpha synthesis. Acts also as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the E3 ubiquitin-protein ligase RNF26.; (Microbial infection) Promotes Dengue virus RNA replication by negatively regulating IFN-beta signaling and mediating 'Lys-48'-linked ubiquitination on IRF3.

References:

[1]. Uwe Lenk, et al. A role for mammalian Ubc6 homologues in ER-associated protein degradation. J Cell Sci. 2002 Jul 15;115(Pt 14):3007-14. [Content Brief]

[2]. Takashi Sato, et al. STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein. Mol Cell. 2012 Jul 13;47(1):99-110. [Content Brief]

[3]. Tingting Feng, et al. Ubiquitin-conjugating enzyme UBE2J1 negatively modulates interferon pathway and promotes RNA virus infection. Virol J. 2018 Aug 29;15(1):132. [Content Brief]

[4]. Tom Cremer, et al. The ER-embedded UBE2J1/RNF26 ubiquitylation complex exerts spatiotemporal control over the endolysosomal pathway. Cell Rep. 2021 Jan 19;34(3):108659. [Content Brief]

[5]. Muthukumar Elangovan, et al. The role of ubiquitin-conjugating enzyme Ube2j1 phosphorylation and its degradation by proteasome during endoplasmic stress recovery. J Cell Commun Signal. 2017 Sep;11(3):265-273. [Content Brief]

[6]. Manoj B Menon, et al. Endoplasmic reticulum-associated ubiquitin-conjugating enzyme Ube2j1 is a novel substrate of MK2 (MAPKAP kinase-2) involved in MK2-mediated TNFα production. Biochem J. 2013 Dec 1;456(2):163-72. [Content Brief]

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