|Other Accession||O70481, NP_777576.1|
|Other Names||E3 ubiquitin-protein ligase UBR1, 632-, N-recognin-1, Ubiquitin-protein ligase E3-alpha-1, Ubiquitin-protein ligase E3-alpha-I, UBR1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 260-274 of HUMAN UBR1|
|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.|
|Function||E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth.|
|Cellular Location||Cytoplasm, cytosol|
|Tissue Location||Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
The N-end rule pathway is one proteolytic pathway of the ubiquitin system. The recognition component of this pathway, encoded by this gene, binds to a destabilizing N-terminal residue of a substrate protein and participates in the formation of a substrate-linked multiubiquitin chain. This leads to the eventual degradation of the substrate protein. The protein described in this record has a RING-type zinc finger and a UBR-type zinc finger. Mutations in this gene have been associated with Johanson-Blizzard syndrome.
Elting, M., et al. Am. J. Med. Genet. A 146A (23), 3058-3061 (2008) :
Alkhouri, N., et al. World J. Gastroenterol. 14(44):6863-6866(2008)
Yamaguchi, Y., et al. BMC Med. Genet. 9, 22 (2008) :
Schmidt, R.L., et al. Cancer Res. 67(24):11798-11810(2007)
Wei, S., et al. Mol. Pharmacol. 72(3):725-733(2007)
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