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(Mouse) Uhrf2 Blocking Peptide (Center)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q7TMI3 |
|---|
| Gene ID | 109113 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase UHRF2, 632-, NIRF, Np95-like ring finger protein, Nuclear protein 97, Nuclear zinc finger protein Np97, Ubiquitin-like PHD and RING finger domain-containing protein 2, Ubiquitin-like-containing PHD and RING finger domains protein 2, Uhrf2, Nirf |
| Target/Specificity | The synthetic peptide sequence is selected from aa 472-485 of HUMAN Uhrf2 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | Uhrf2 |
|---|---|
| Synonyms | Nirf |
| Function | E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair. Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:23434322, PubMed:28402695). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (PubMed:28115522). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thus inducing G1 arrest. Ubiquitinates also PCNP leading to its degradation by the proteasome. Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteasomal degradation. Promotes also DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation. Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (By similarity). |
| Cellular Location | Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:21598301}. Chromosome {ECO:0000250|UniProtKB:Q96PU4}. Note=Enriched at genomic loci that are enriched for 5-hydroxy-methylcytosine (5hmC) {ECO:0000250|UniProtKB:Q96PU4} |
| Tissue Location | Mostly detected in several tissues, including the thymus, spleen, lung, adrenal gland, and ovary. In addition, found in several tissues in the brain (cerebellum, hippocampus, and cerebral cortex). |
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Background
E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131 (By similarity). E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells.
References
Davenport J.W.,et al.Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
Mori T.,et al.Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
Carninci P.,et al.Science 309:1559-1563(2005).
Pichler G.,et al.J. Cell. Biochem. 112:2585-2593(2011).
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