Ubiquitin-like containing PHD and RING finger domain 1 (UHRF1)

Ubiquitin-like containing PHD and RING finger domain 1 (UHRF1) is an epigenetic regulator and E3 ubiquitin ligase involved in the maintenance of DNA methylation, histone modification, and chromatin structure. It recognizes hemi-methylated DNA and recruits DNA methyltransferases (notably DNMT1) during DNA replication to preserve epigenetic marks[1][2][3]. UHRF1 functions as a master coordinator of multiple chromatin-modifying proteins and plays a crucial role in cell cycle control and tumor suppressor gene silencing through epigenetic mechanisms[2]. Aberrant overexpression of UHRF1 is observed in multiple types of cancer and is associated with poor prognosis, making it both a promising therapeutic target and a biomarker for diagnosis and prognosis in oncology[1][2][3]. UHRF1 exerts non-enzymatic reader functions via multiple domains (UBL, TTD, PHD, SRA, RING) to interact with histone modifications and DNA, orchestrating silencing of tumor suppressor genes and maintenance of epigenetic states[2][3].

Other names

ICBP90NP95RNF106Inverted CCAAT box-binding protein of 90 kDaNuclear protein 95

Inhibition of E3 ubiquitin ligase activity; Disruption of DNA methylation maintenance; Inhibition of protein-protein interactions with DNMT1