Ubiquitin-conjugating enzyme E2 D2 (UBE2D2)

Ubiquitin-conjugating enzyme E2 D2 (UBE2D2) is a member of the E2 family of ubiquitin-conjugating enzymes and acts as an essential intermediary in protein ubiquitination, partnering with E3 ligases to mediate the transfer of ubiquitin to target proteins[1][3]. UBE2D2 is involved in the regulated degradation of misfolded, damaged, or short-lived proteins via the ubiquitin-proteasome system (UPS), marking them for proteasome-mediated degradation and ensuring cellular protein quality control[1][2][3]. It influences major cell signaling pathways, including receptor tyrosine kinases (RTKs), Hedgehog, TGFβ, and NFκB, and participates in transcriptional regulation via histone ubiquitination and DNA repair mechanisms[3]. UBE2D2 has critical roles in maintaining proteostasis, especially during aging, and in regulating levels of key proteins such as the tumor suppressor p53[1][2][3]. Dysfunction or altered regulation of UBE2D2 can contribute to diseases including cancer, neurodegenerative disorders, and inflammation[1][2][3].

Other names

PUBC1UBC4UBC5BUBCH4UBCH5BUbcH5BUBC4/5E2 ubiquitin-conjugating enzyme D2E2(17)KB2Ubiquitin carrier protein D2Ubiquitin-protein ligase D2p53-regulated ubiquitin-conjugating enzyme 1Ubiquitin-conjugating enzyme E2-17 kDa 2

Drugs or molecules that would interact with UBE2D2 would likely act by inhibiting or modulating ubiquitin transfer, affecting protein degradation pathways, but no specific MoAs or approved drugs are cited[1][3].