Recombinant Human UHRF1 protein (His-DDDDK tag N-Terminus)
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Recombinant Human UHRF1 protein (His-DDDDK tag N-Terminus) 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 zinc finger protein Np95, RING finger protein 106, Transcription factor ICBP90, Ubiquitin-like PHD and RING finger domain-containing protein 1, HuNp95, Nuclear protein 95, hNp95, hUHRF1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human UHRF1 protein (His-DDDDK tag N-Terminus) (AB198770)
4-20% SDS-PAGE analysis of ab198770 with Coomassie staining.
Lane 1 : 2 μg ab198770
Lane 2 : Protein marker
Complementary Products
![Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-UHRF1 antibody [EPR18803-11] (AB213223)](https://content.abcam.com/products/images/uhrf1-antibody-epr18803-11-ab213223--immunohistochemistry-formalin-pfa-fixed-paraffin-embedded-sections-img132737.jpg)
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
E3 ubiquitin-protein ligase that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification (PubMed : 10646863, PubMed : 15009091, PubMed : 19056828, PubMed : 23022729, PubMed : 24013172, PubMed : 27595565, PubMed : 30104358, PubMed : 30392929, PubMed : 30392931, PubMed : 39607687). Plays a key role in DNA methylation inheritance by promoting recruitment of DNMT1 to hemimethylated DNA and ensure faithful propagation of the DNA methylation patterns through DNA replication (PubMed : 23022729, PubMed : 24013172, PubMed : 27595565, PubMed : 30104358, PubMed : 30392929, PubMed : 30392931, PubMed : 39607687). Acts both as a histone reader and writer : specifically recognizes and binds (1) hemimethylated DNA at replication forks and (2) histone H3 trimethylated at 'Lys-9' and unmethylated at 'Arg-2' (H3K9me3 and H3R2me0, respectively), thereby activating its E3 ubiquitin-protein ligase activity (PubMed : 15361834, PubMed : 17673620, PubMed : 17967883, PubMed : 18772889, PubMed : 21745816, PubMed : 21777816, PubMed : 22100450, PubMed : 22837395, PubMed : 23022729, PubMed : 27595565, PubMed : 30104358). UHRF1 then mediates histone H3 'Lys-18' monoubiquitination (H3K18ub), a docking site for DNMT1, leading to DNMT1 recruitment and replication-coupled DNA methylation maintenance (PubMed : 27595565). Also mediates histone H3 'Lys-14' and 'Lys-23' ubiquitination (H3K14ub and H3K23ub) at lower level (PubMed : 24013172, PubMed : 27595565). Histone ubiquitin ligase activity also stimulates the methyltransferase activity of SUV39H1 and/or SUV39H2, promoting accumulation of H3K9me3 histone mark to reinformce heterochromatin state (PubMed : 39631394). 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 (PubMed : 21777816). Plays a role in DNA repair by cooperating with UHRF2 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation (PubMed : 30335751). Also ubiquitinates non-histone proteins, such as histone H3, KIF11 and PML (PubMed : 22945642, PubMed : 37728657). 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 by PKA decreases the binding to H3K9me3 (PubMed:15178447, PubMed:22837395). Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome (PubMed:22411829).. Ubiquitinated; which leads to proteasomal degradation (PubMed:15009091). Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation (PubMed:17967883, PubMed:21745816, PubMed:22411829). Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination (PubMed:22411829). Polyubiquitination may be stimulated by DNA damage (PubMed:15009091).
Subcellular localisation
Nucleus
Target data
Product promise
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