Ubiquitin protein ligase E3 component n-recognin 3 (UBR3)

Ubiquitin protein ligase E3 component n-recognin 3 (UBR3) is an E3 ubiquitin ligase enzyme in the N-recognin (UBR) family that functions together with E2 conjugating enzymes to mediate ubiquitination and proteasomal degradation of target proteins[3][7]. While structurally similar to other N-end rule E3 ligases such as UBR1 and UBR2, UBR3 has distinct substrate specificity and is unable to target classical N-end rule substrates[1]. Instead, UBR3 is implicated in diverse biological processes including cellular protein quality control, maintenance of genomic stability through the polyubiquitylation and regulation of APE1 (a DNA repair enzyme), modulation of sensory pathways (notably olfactory development and function), cardiac ion channel regulation (notably Nav1.5), and the control of inflammatory and degenerative responses (e.g., through DUSP1/p38 MAPK signaling in intervertebral disc disease)[1][3]. UBR3 dysregulation has been linked to embryonic and neonatal lethality in mice, sensory and behavioral alterations, cardiac arrhythmia susceptibility, inflammatory tissue injury, and genetic risk for IgA nephropathy, highlighting its relevance as a potential therapeutic target across a range of disease areas[1][3][7].

Other names

E3 ubiquitin-protein ligase UBR3KIAA2024ZNF650N-recognin-3RING-type E3 ubiquitin transferase UBR3Ubiquitin-protein ligase E3-alpha-3Ubiquitin-protein ligase E3-alpha-IIIZinc finger protein 650DKFZp434P117FLJ37422