{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUHRF1 (also known as NP95 or ICBP90) is a multifaceted epigenetic coordinator that ensures the faithful inheritance of DNA methylation patterns during cell division. It achieves this by employing a specialized SET and RING associated (SRA) domain that preferentially binds hemimethylated CpG dinucleotides, thereby recruiting the maintenance DNA methyltransferase DNMT1. In parallel, UHRF1 integrates signals from chromatin through its linked histone‐binding modules—the tandem Tudor domain and the plant homeodomain (PHD) finger—which recognize key histone marks such as H3K9 trimethylation, unmodified H3R2, and H3K4 unmodified states. These coordinated interactions enable UHRF1 to couple DNA methylation with histone modification patterns, as demonstrated by a series of structural and biochemical studies that revealed both its exclusive binding pockets and allosteric regulatory mechanisms."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOverexpression of UHRF1 is a common feature of many human malignancies where it functions as an oncogene by promoting aberrant epigenetic silencing of tumor suppressor genes. In cancer cells, UHRF1 not only influences the cell cycle by interacting with regulators such as pRB but also exploits its intrinsic RING E3 ubiquitin ligase activity to modulate the stability and activity of key chromatin modifiers. This deregulated activity leads to the repression of genes including BRCA1, p21, PPARG, and others, and is further enforced by altered post‐transcriptional regulation through miRNAs (for example, miR‑124 and miR‑145) and lncRNAs (such as UPAT). As a consequence, UHRF1 overexpression disrupts proper cell cycle checkpoint functions and promotes oncogenic transformation in diverse tumor types ranging from bladder and colorectal to prostate and liver cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in epigenetic programming and oncogene‐mediated transcriptional silencing, UHRF1 contributes to the maintenance of genomic stability by participating in the DNA damage response. It is recruited to sites of DNA double‐strand breaks and interstrand crosslinks where it facilitates the assembly of repair complexes through its ubiquitin ligase activity—such as catalyzing K63‑linked polyubiquitination events on targets like RIF1—to promote homologous recombination and efficient lesion processing."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "38", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Motoko Unoki, Toshihiko Nishidate, Yusuke Nakamura "}, {"type": "b", "children": [{"type": "t", "text": "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1208053"}], "href": "https://doi.org/10.1038/sj.onc.1208053"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15361834"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15361834"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Magnolia Bostick, Jong Kyong Kim, Pierre-Olivier Estève, et al. 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