Back to your search result

Description

E3 ubiquitin-protein ligase UBR5 (UniProt, O95071, also known as EC: 2.3.2.26, E3 ubiquitin-protein ligase, HECT domain-containing 1, HECT-type E3 ubiquitin transferase UBR5, Hyperplastic discs protein homolog, hHYD, Progestin-induced protein) is encoded by the UBR5 (also known as EDD, EDD1, HYD, KIAA0896) gene (Gene ID: 51366) in human. UBR5 is a widely expressed nuclear E3 ligase that is most abundant in testis and expressed at high levels in brain, pituitary and kidney. It is a component of the N-end rule pathway that 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. UBR5 is involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination and may play a role in control of cell cycle progression. It is shown to regulate DNA topoisomerase II binding protein (TopBP1) in the DNA damage response and may have a tumor suppressive function. It acts as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of Lys-63-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. URB5 contains a zinc-finger domain (aa 1177-1245), a poly(A)-binding protein C-terminal (PABC) domain(aa 2377-2454), and a (Homologous to the E6-AP Carboxyl Terminus (HECT) domain (aa 2462-2799). Two isoforms of UBR5 have been described that are produced by alternative splicing.