Anti-E3 ubiquitin-protein ligase UBR1 Antibody, clone 6H9.1 clone 6H9.1, from mouse

E3 ubiquitin-protein ligase UBR1 (UniProt: Q8IWV7; also known as EC: 2.3.2.27, N-Recognin-1, RING-type E3 ubiquitin transferase UBR1, Ubiquitin-protein ligase E3-alpha-1, Ubiquitin-protein ligase E3-alpha-I) is encoded by the UBR1 gene (Gene ID: 197131) in human. E3 ubiquitin-protein ligase UBR1 is a component of the N-end rule pathway. It 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. It may also be involved in pancreatic homeostasis. Two isoforms of UBR1 have been described that are produced by alternative splicing. UBR1 is broadly expressed protein with highest levels reported in skeletal muscle, kidneys, and pancreas. UBR1 has two zinc finger domains. The UBR-type domain is localized to amino acids 97 to 168 and it forms a pocket that mediates recognition of type 1 N-degrons. It exhibits preference for arginine in first position and displays poor affinity for histidine. The second zinc finger domain, RING-type, atypical, is localized to amino acids 1098-1201. Mutations in UBR1 gene are causative factor in Johanson-Blizzard syndrome that is characterized by congenital exocrine pancreatic insufficiency, malformations such as nasal wing aplasia, and mental retardation.