Ubiquitin protein ligase E3 component n-recognin 7 (UBR7)

Ubiquitin protein ligase E3 component n-recognin 7 (UBR7) is an E3 ubiquitin ligase characterized by both a plant homeodomain (PHD) and a UBR box domain, conferring activity in monoubiquitination of histone H2B at lysine 120, which is important for chromatin regulation and gene expression[1][2]. UBR7 plays roles in epigenetic regulation, suppressing tumorigenesis and metastasis of triple-negative breast cancer by maintaining specific chromatin states and influencing cell adhesion gene expression[1]. It acts as a histone chaperone for post-nucleosomal histone H3 and has a unique substrate recognition profile among UBR family ligases[2]. UBR7 is also involved in nucleotide metabolism by regulating the degradation of PRPS-associated protein, thereby maintaining nucleotide biosynthesis, which is particularly relevant in leukemia proliferation[4]. Mutations in UBR7 are linked to neurodevelopmental syndromes featuring epilepsy, hypothyroidism, and ptosis[3]. As of now, no drugs are known to directly target UBR7.

Other names

Putative E3 ubiquitin-protein ligase UBR7C14orf130N-recognin-7RING-type E3 ubiquitin transferase UBR7LICAS

Drugs targeting UBR7 would likely act by modulating its E3 ubiquitin ligase activity, altering histone ubiquitination or influencing nucleotide biosynthesis via the PRPS pathway (hypothetical; no drugs currently specified in the literature).