Recombinant Human UHRF1 protein
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Recombinant Human UHRF1 protein is a Human Full Length protein, in the 2 to 793 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE.
View Alternative Names
ICBP90, NP95, RNF106, UHRF1, E3 ubiquitin-protein ligase UHRF1, Inverted CCAAT box-binding protein of 90 kDa, Nuclear protein 95, Nuclear zinc finger protein Np95, RING finger protein 106, RING-type E3 ubiquitin transferase UHRF1, Transcription factor ICBP90, Ubiquitin-like PHD and RING finger domain-containing protein 1, Ubiquitin-like-containing PHD and RING finger domains protein 1, HuNp95, hNp95, hUHRF1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human UHRF1 protein (AB198770)
4-20% SDS-PAGE analysis of ab198770 with Coomassie staining.
Lane 1 : 2 μg ab198770
Lane 2 : Protein marker
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
UHRF1 engages in preserving the DNA methylation landscape ensuring proper gene expression patterns. It is part of a multi-protein complex and processes both histone modification and DNA methylation. Its presence is critical for gene silencing through the recruitment of DNMT1 and histone deacetylases. UHRF1 therefore influences regulatory regions of genes important for cell cycle progression and development.
Pathways
UHRF1 integrates into methylation-dependent gene silencing and cell cycle regulation. It actively participates in DNA damage repair pathways by modulating the p53 pathway aiding cell survival post-DNA damage. UHRF1 closely interacts with epigenetic regulators such as DNMT1 and histone deacetylases bridging methylation and chromatin remodeling to ensure proper cell cycle and transcriptional control.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification : through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. Plays a role in DNA repair by cooperating with UHRF2 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation. Acts as a critical player of proper spindle architecture by catalyzing the 'Lys-63'-linked ubiquitination of KIF11, thereby controlling KIF11 localization on the spindle (PubMed : 37728657).
Post-translational modifications
Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.. Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage.
Subcellular localisation
Nucleus
Target data
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Product promise
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