Cell Signaling Technology

Product Pathways - Protein Stability

UBR5 Antibody #8755

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M Mk (Dg) (Pg) Endogenous 300 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  Mk=Monkey  Dg=Dog  Pg=Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

UBR5 Antibody recognizes endogenous levels of total UBR5 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human UBR5 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using UBR5 Antibody.

Background

Human E3 identified by differential display (UBR5/EDD) is a 300 kDa HECT domain-containing ubiquitin E3 ligase that is a component of the N-end rule pathway and recognizes proteins bearing specific destabilizing N-terminal residues, leading to their ubiquitination and subsequent degradation (1). UBR5 represents an ortholog of HYD, the Drosophila hyperplastic discs tumor suppressor gene product. UBR5 mRNA is expressed in many tissues and is frequently overexpressed in breast and ovarian cancers, suggesting a possible role in tumor development (2-4). UBR5 contains three putative nuclear localization signals, an N-terminal UBA domain (mediates interaction of UBR5 with ubiquitin), a central UBR1-like zinc finger motif (mediates substrate recognition), a PABC domain (peptide domain found in the poly(A)-binding protein PABP), and a C-terminal HECT ubiquitination domain (2,5-8). UBR5 has been shown to bind to and ubiquitinate the topoisomerase II beta-binding protein TopBP1, and to bind to and potentiate progesterone receptor-mediated transcriptional transactivation (9,10). More recently, it has been reported that UBR5 binds to the DNA damage checkpoint kinase Chk2 and acts upstream of Chk2 (11), supporting the notion that UBR5 is involved in pathways regulating the DNA damage response. Furthermore, it has been demonstrated that downregulation of PABP results in UBR5-mediated degradation of the PABP-associated protein Paip2, which interferes with protein translation by displacing PABP from mRNA (12). This indicates that UBR5 is involved in the regulation of PABP activity and, thus, in controlling translation efficiency.

  1. Sriram, S.M. et al. (2011) Nat Rev Mol Cell Biol 12, 735-47.
  2. Callaghan, M.J. et al. (1998) Oncogene 17, 3479-91.
  3. Clancy, J.L. et al. (2003) Oncogene 22, 5070-81.
  4. Fuja, T.J. et al. (2004) Cancer Res 64, 942-51.
  5. Deo, R.C. et al. (2001) Proc Natl Acad Sci U S A 98, 4414-9.
  6. Honda, Y. et al. (2002) J Biol Chem 277, 3599-605.
  7. Henderson, M.J. et al. (2002) J Biol Chem 277, 26468-78.
  8. Kozlov, G. et al. (2004) EMBO J 23, 272-81.
  9. Honda, Y. et al. (2002) J Biol Chem 277, 3599-605.
  10. Henderson, M.J. et al. (2002) J Biol Chem 277, 26468-78.
  11. Henderson, M.J. et al. (2006) J Biol Chem 281, 39990-40000.
  12. Yoshida, M. et al. (2006) EMBO J 25, 1934-44.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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