| UHRF1 Protein | |
|---|---|
| Protein Name | Ubiquitin-like with PHD and RING finger domains 1 |
| Alternative Names | UHRF1, ICBP90, TNP1 |
| Molecular Weight | 110 kDa |
| Length | 793 amino acids |
| UniProt ID | Q96T23 |
| Cellular Location | Nucleus |
The UHRF1 protein is a key epigenetic regulator that functions as a master organizer of DNA methylation and histone modifications. It bridges the inheritance of epigenetic marks during cell division by recruiting DNA methyltransferase 1 (DNMT1) to replication forks and reading histone modifications through its multiple domain architecture. UHRF1 is essential for maintaining genomic stability and is frequently dysregulated in cancer and neurodegenerative diseases.
UHRF1 is an 82 kDa protein containing five conserved domains: an N-terminal ubiquitin-like (UBL) domain, a tandem Tudor domain (TTD) that specifically recognizes trimethylated lysine 9 on histone H3 (H3K9me3), a plant homeodomain (PHD) finger that binds unmodified H3 tail, a SET and RING-associated (SRA) domain that binds hemimethylated CpG dinucleotides, and a C-terminal RING finger domain with E3 ubiquitin ligase activity.
UHRF1 contains multiple domains:
UHRF1 has multiple functions:
UHRF1 interacts with:
The study of Uhrf1 Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.