Zinc finger-containing ubiquitin peptidase 1 (ZUP1)

Zinc finger-containing ubiquitin peptidase 1 (ZUP1) is a protein-coding enzyme characterized by zinc finger motifs and a cysteine peptidase domain. ZUP1 acts as a K63-specific deubiquitinating enzyme, primarily catalyzing the cleavage of long K63-linked polyubiquitin chains internally rather than removing ubiquitin from the chain ends. This enzymatic activity is important for the regulation of DNA repair, maintenance of genome stability, and proper cellular response to DNA damage. ZUP1 is closely related to, but distinct from, proteases for other ubiquitin-like modifiers such as Ufm1. Recent research also implicates ZUP1 in the regulation of antiviral immunity by amplifying MAVS-mediated signaling in response to viral RNA. Loss or dysfunction of ZUP1 may contribute to disease phenotypes characterized by impaired DNA repair and immune dysregulation, including some cancers and autoinflammatory conditions. References: [1][3][4][5][6][2]

Other names

C6orf113ZUFSPdJ412I7.3Lys-63-specific deubiquitinase ZUFSPubiquitin carboxyl-terminal hydrolase ZUFSPzinc finger with UFM1-specific peptidase domain protein

Deubiquitination of specific ubiquitin chain linkages (K63-linked polyubiquitin), modulates DNA repair processes, antiviral innate immune amplification via MAVS complex