NIRF/UHRF2 Polyclonal

NIRF (Np95/ICBP90-like RING finger protein), also known as E3 ubiquitin-protein ligase UHRF2, Nuclear zinc finger protein Np97 or RING finger protein 107, is a nuclear protein involved in cell cycle regulation. NIRF contains a PHD finger, two RING fingers, a ubiquitin-like domain and a YDG/SRA domain. It shares high structural homology with UHRF1 (also called ICBP90 in humans and Np95 in mice), however, in contrast to UHRF1, NIRF acts as a negative regulator of cell proliferation. It associates with the Cdk2-cyclin complex in its dephosphorylated form and induces G1 arrest. NIRF plays an important role in the regulation of the G1/S transition by blocking cell entry into the S-phase. While associated with Cdk2, NIRF becomes phosphorylated. NIRF can also act as a ubiquitin ligase, and it ubiquitinates PCNP. In addition, NIRF can recruit and bind HDAC1 via its SRA domain. The overexpression of NIRF results in an increase of G1 phase cells.