Target intelligence / Profile preview

Ubiquitin-protein ligase E3D (UBE3D)

Target
UBE3D
Molecular classification
Enzyme, E3 ubiquitin-protein ligase, HECT domain-containing E3 ligase
01

Overview

Ubiquitin-protein ligase E3D (UBE3D) is a member of the HECT (Homologous to E6AP Carboxyl Terminus) domain-containing E3 ubiquitin ligases, enzymes that mediate the transfer of ubiquitin molecules to specific substrate proteins, thereby regulating their degradation, activity, or cellular location[1][3]. UBE3D functions at least in part through interactions with ubiquitin-conjugating enzymes (E2s), such as UBE2C, and substrates like cyclin B. It plays a crucial role in processes such as the DNA damage response, especially homologous recombination-mediated repair in heterochromatin regions, by facilitating chromatin relaxation and coordinating the recruitment of DNA repair factors (e.g., PCNA and KAP1)[1]. Mutations of UBE3D, including the V379M variant, have been associated with diseases such as age-related macular degeneration, possibly via impaired recruitment of DNA repair cofactors under oxidative stress[1]. UBE3D is considered a potential drug target in oncology and age-related eye diseases, but currently there are no drugs directly targeting this ligase for therapeutic purposes[1][3].

Other names
UBE3DC6orf157H10BHUBE2CBPDKFZp434A1520YJR141WHECT-type E3 ubiquitin transferase E3DUbcH10-binding protein with a HECT-like domainUbiquitin-conjugating enzyme E2C-binding proteinUBCH10 binding protein with a HECT-like domain
02

Biological functions

Protein ubiquitinationDNA damage responseHomologous recombination repairChromatin relaxation/de-condensationCyclin B regulation
03

Disease associations

CancerAge-related macular degeneration (AMD)Other DNA repair–related disorders
04

Safety considerations

Potential genome instability if inhibited, as homologous recombination and DNA repair capacity are impairedPossible impacts on cell viability during genotoxic stress
05

Biomarkers

V379M single nucleotide variant (disease-associated, notably in AMD)

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