Deubiquitinating protein VCPIP1 (VCPIP1)

Deubiquitinating protein VCPIP1 (VCPIP1) is an **OTU-domain deubiquitinating enzyme** involved in diverse cellular processes, including **protein deubiquitination, DNA-protein cross-link repair, reassembly of the Golgi apparatus and endoplasmic reticulum after mitosis, and protein localization to chromatin**[5]. VCPIP1 interacts with the **valosin-containing protein (VCP/p97), P47, and the SNARE complex** to promote **membrane fusion events** essential for Golgi and ER integrity post-mitosis[1][3]. It can recruit proteasome subunits, such as **PSMC3**, and regulate stability of specific proteins like the **hepatitis B virus X protein (HBx)**, linking it to viral infection and oncogenesis[2][4]. **VCPIP1’s activity spans both enzymatic and scaffolding functions** independent of its DUB activity[2]. Genetic alterations in VCPIP1 or its interacting partners are associated with **cancer, neurodegenerative diseases, and rare genetic syndromes**[5]. While inhibitors targeting VCPIP1 are under investigation, none are currently clinically approved, and the essential nature of its cellular roles suggests a need for caution to avoid disrupting fundamental protein homeostasis[5].

Other names

KIAA1850VCIP135VCP/p47 complex-interacting 135-kDa proteindeubiquitinating protein VCIP135valosin-containing protein p97/p47 complex-interacting protein 1VCP/p47 complex-interacting protein p135DUBA3FLJ23132

Drugs targeting deubiquitinating enzymes often act by inhibiting or modulating enzymatic deubiquitination activity, but specific mechanism for direct VCPIP1 modulators not established as of current knowledge[2][5].