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HUB1(UBL5) Blocking Peptide (N-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9BZL1 |
|---|---|
| Other Accession | Q9EPV8, Q3T0Z3, NP_077268 |
| Gene ID | 59286 |
|---|---|
| Other Names | Ubiquitin-like protein 5, UBL5 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 18~38 of HUMAN UBL5 |
| 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 | UBL5 |
|---|---|
| Function | Ubiquitin-like protein that plays a role in cell proliferation and sister chromatid cohesion by associating with spliceosomal proteins (PubMed:25092792). Participates thereby in pre- mRNA splicing by maintaining spliceosome integrity. Promotes the functional integrity of the Fanconi anemia DNA repair pathway by interacting with FANCI component and subsequently mediating the formation of FANCI homodimers (PubMed:25862789). Plays also a protective role against ER stress-induced apoptosis (PubMed:37315790). |
| Cellular Location | Cytoplasm. Nucleus. Nucleus, Cajal body |
| Tissue Location | Ubiquitous. Highest level of expression in heart, skeletal muscle, kidney, liver, iris and lymphoblasts |
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Provided below are standard protocols that you may find useful for product applications.
Background
UBL5 is a widely expressed human protein that is strongly conserved across phylogeny. Orthologs of UBL5 occur in every eukaryotic genome characterized to date. The yeast ortholog of UBL5, HUB1, was reported to be a ubiquitin-like protein modifier important for modulation of protein function. However, unlike ubiquitin and all other ubiquitin-like modifiers, UBL5 and its yeast ortholog HUB1 both contain a C-terminal di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other ubiquitin-like modifiers. Here we describe the three-dimensional structure of UBL5 determined by NMR. The overall structure of the protein was found to be very similar to ubiquitin despite the low approximately 25% residue similarity. The signature C-terminal di-tyrosine residues in UBL5 are involved in the final beta sheet of the protein. This is very different to the di-glycine motif found in ubiquitin, which extends beyond the final beta sheet. In addition, we have confirmed an earlier report of an interaction between UBL5 and the cyclin-like kinase, CLK4, which we have determined is specific and does not extend to other cyclin-like kinase family members.
References
Friedman, J.S., et al., Genomics 71(2):252-255 (2001).
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