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Facts about E3 ubiquitin-protein ligase UHRF2.
Ubiquitinates cyclins, CCND1 and CCNE1, in a seemingly phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP resulting in its degradation by the proteasome.
Mouse | |
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Gene Name: | Uhrf2 |
Uniprot: | Q7TMI3 |
Entrez: | 109113 |
Belongs to: |
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No superfamily |
DKFZp434B0920; DKFZp686G0837; E3 ubiquitin-protein ligase UHRF2; EC 6.3.2; EC 6.3.2.-; MGC33463; NIRFUbiquitin-like-containing PHD and RING finger domains protein 2; Np95/ICBP90-like RING finger protein; Np95-like RING finger protein; Nuclear protein 97; Nuclear zinc finger protein Np97; RNF107RING finger protein 107; Ubiquitin-like PHD and RING finger domain-containing protein 2; ubiquitin-like with PHD and ring finger domains 2; ubiquitin-like, containing PHD and RING finger domains, 2; URF2
Mass (kDA):
90.106 kDA
Mouse | |
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Location: | 19|19 C1 |
Sequence: | 19; |
If you are looking for the best use of the UHRF2 marking, then this article is for you. This article will discuss how this nuclear E3 ubiquitin-protein ligase regulates cell cycle, proliferation, and migration. Boster has high-affinity primary antibody for this marker. They are highly cited within the research community. Their antibodies are validated in ELISA, Western Blotting, and Immunohistochemistry.
UHRF2 is a nuclear E2 ubiquitin -protein ligaser. It is associated to a ring domain, and is essential in SUMO-mediated ubiquitination. Overexpression of UHRF2 induces SUMO-mediated ubiquitination of ZNF131, whereas knockdown of the protein inhibits ZNF131 SUMOylation. The activity of SUMO E3 is dependent upon the NCR and the SRA domains. However the RING domain plays a crucial part in SUMOylation.
The activity of UHRF2 is critical for the regulation of cell-cycle and DNA methylation. UHRF2 plays a vital role in DNA methylation. It also regulates gene expression, nuclear protein ubiquitination, and gene expression. It also plays an important role in neuron-related gene expression and in the maintenance of the cell's cyclins.
Interestingly, both UHRF2 and ZNF131 have nuclear localization domains, which allow for interaction with 5hmC-containing genomic regions. UHRF2 is a 5hmC reader because of the interaction between the two proteins. The deletions of the SRA or NCR domains will decrease UHRF2's affinity for ZNF131.
The MBS2605809 ELISA Kit is used to detect UHRF2. The ELISA test uses a HRP colorimetric detection system to detect the protein in native form. The most suitable samples are tissue homogenates or secretions. A quality control assay should be included in the kit to ensure best results. Before it is released for research, it's been tested for reproducibility.
The plasmid for human UHRF2 encodes a 3xMyc tag protein (UBC9). COSMO Genetech verified the sequences. Bioneer synthesized UHRF2-specific SiRNA duplexes. The plasmid was transfected by Lipofectamine 2000 in order to test UHRF2's activity in cells.
The UHRF2 E3 Ubiquitin Ligase has a tandem Tudor domain, a SRA/YDG motif, and a multi-domain E3 domain. It has been shown that it plays an important role within the cell cycle by interfacing with many cyclins as well as cyclindependent kinases. Evidence is emerging that UHRF2 is involved in DNA damage repair and tumorigenesis.
Interdigital remodeling in mice occurs in a sequential fashion. The interdigital cells undergo a proliferation arrest, DNA damage and senescence, before massive apoptosis. Overexpression of the Uhrf1 gene decreased the number of cells entering the S phase, which is characteristic of senescent tissues. Overexpression of Uhrf genes resulted in decreased cell death during loss-of function experiments. UHRF2 expression increased after limb morphogenesis.
To test whether UHRF2 is a tumor suppressor, scientists carried out a loss-of-function assay. Two NSCLC cell types (95D- and A549) were infected to produce shRNAs for UHRF2. Western blot results revealed that shRNA-UHRF2 treatment resulted a greater cell proliferation and migration. Transwell and scratch assays both showed enhanced migration and invasion.
UHRF2 is not only involved in cell proliferation but also regulates apoptosis. Specifically, it regulates the expression of pro-apoptotic genes and inhibits tumor radiosensitivity. It has been shown that UHRF2-overexpression causes cell death in NSCLC cells. This suggests that it may be a tumor suppressor.
In micromass cultures, the Uhrf gene has been implicated in inhibiting Chondrogenesis in limb-skeletal progenitors. In this model, the Uhrf gene regulates transcription of a set of genes involved with skeletal development. These genes are essential in determining the fates skeletal progenitors. If these genes become inactive, chondrogenesis ceases. Instead, the cells divide into chondrocytes.
UHRF2 is expressed in many cell types, including those with tumor-forming potential. The marker is known to promote proliferation of many different types of cancer cell lines when it is overexpressed. It also inhibits cell death, apoptosis, and cell cycle arrest at G0/G1.
The UHRF2 E3 Ligase is an E3 protein with a novel binding spot on lysine 23 or 18. It also features a unique set-and-ring-associated (SRA), domain. It also has a new gene domain, the RING finger. It has been shown to bind DNA containing hemimethylated lysine 9 at replication fork.
Further studies are needed to fully understand the function of UHRF2 in various cancers. While previous research has suggested that the protein may be involved in tumor progression or metastasis, no studies have examined whether it is involved in other processes. This protein has been implicated in various cancers, including prostate cancer, breast cancer, and ovarian cancer. The study also suggested that UHRF2 could serve as a biomarker in ICC.
This gene is involved in many human diseases, including cancer. Although the function of UHRF1 is not completely understood, it is important that UHRF1 expression is high in GC tumours. Further studies of the UHRF2 gene in GC tumorigenesis are needed to clarify whether UHRF1 promotes cancer development. Two studies showed that UHRF1 knockdown inhibited invasion, growth, and migration and increased caspase-3 activity.
In aggressive gastric tumor cells, UHRF1 overexpression has been associated with increased proliferative capability. Reduced levels of UHRF1 induced by miR-146a/b reactivated p53 and tumor-suppressor gene c-hdr1 through hypomethylation. UHRF1 knockdown prevented tumor growth by blocking EMT, and migration in ICC.
UHRF2 is a novel transcription factor that is involved in the regulation of E-cadherin. It is important for you to know that this gene is downregulated when cancer cells develop. UHRF2 downregulation can increase your risk of developing a disease. UHRF2 can also be known to promote tumor growth, although it is not understood how. In this study, we focused only on cancer cells where UHRF2 was reduced.
Our findings show that the UHRF2 genes is associated with tumor growth and lymph node metastasis. In addition, we found that UHRF2 expression is a risk factor independently of the other factors. We also found UHRF2 was highly heterogeneous in NSCLC samples and high expression in tumors and normal tissues. This suggests that UHRF2 could be a therapeutic target for NSCLC.
These results show that UHRF2 can regulate migration. It is associated with bladder cancer progression and angiogenesis. Our results are published in the journals Tumor Biol. and Prostate 2011. These journals include the findings of researchers from Santa Cruz Biotechnology and BD Transduction Laboratories. This study was published by Elangovan, Thirugnanam, Zheng, and Bosland.
The UHRF2 gene also plays a role in cell cycle. In addition, it interacts with several important factors in cell cycle. NSCLC cells are more likely to migrate if UHRF2 is decreased. In fact UHRF1 gene downregulation in human cancer cells increases the likelihood for migration. It also induces CXCR4 synthesis, which is required to induce EMT. It is still unclear how UHRF2 expression occurs in human tumor cells.
The UHRF2 protein in cancer cells is an E3-ligase that regulates TIP60's ubiquitination. UHRF2 expression increased TIP60 stability while UHRF2 was depleted. When UHRF2 in HepG2 cells was depleted, the relationship between UHRF2 (and H3K9ac) was reversed.
Although the role of Uhrf gene is unknown, it is known they regulate gene expression within skeletal progenitors. They are known to influence transcription of genes related to differentiation, proliferation, apoptosis, and other functions. The UHRF2 marker could regulate the fate and expression levels of skeletal progenitors. Uhrf genes, in addition to being an important marker of cell-to–cell communications, also regulate cell–to–cell contacts.
In HepG2 cells, the expression of TIP60 is not stabilized. By contrast, UHRF2 stabilizes TIP60 expression by targeting its RING finger domain and ubiquitination. This could explain the importance of UHRF2 for cell-to–cell communication. There are still other ways to target UHRF2 in order to promote invasion. This includes genetic modification of HDAC1.
The UHRF2 gene plays an important role in apoptosis in the context of cancer. It regulates transcription of tumor suppressor gene genes and selectively regulates expression of proapoptotic gene. It also modulates DNA repair capacity in tumors. Bak1 expression correlates to cell death. This gene is a distinctive member of Bcl2 Family. It has been implicated with interdigital regression. Hypomethylation has been linked to cell deaths.
PMID: 21598301 by Pichler G., et al. Cooperative DNA and histone binding by Uhrf2 links the two major repressive epigenetic pathways.
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