E3 ubiquitin-protein ligase SHPRH (SHPRH)

E3 ubiquitin-protein ligase SHPRH (SHPRH) is a multifunctional protein characterized by DNA helicase, PHD, and RING finger domains, and is ubiquitously expressed in human tissues[2][3][4]. It acts predominantly as a nucleosome-stimulated ATPase and E3 ubiquitin ligase, orchestrating DNA repair by promoting non-canonical polyubiquitination of PCNA in response to genotoxic stress[2][7]. SHPRH is a functional homolog of yeast RAD5 and is implicated in chromatin remodeling and transcriptional regulation through its domain architecture[2][3][5]. Dysregulation and reduced expression of SHPRH have been observed in cancers such as glioblastoma, where it acts as a tumor suppressor by stabilizing its own protein levels and regulating cell proliferation via ubiquitination pathways[1][2]. SHPRH gene variations are associated with inherited DNA repair syndromes including xeroderma pigmentosum and Fanconi anemia[2][5].

Other names

SNF2 histone linker PHD RING helicaseKIAA2023FLJ90837bA545I5.2RING-type E3 ubiquitin transferase SHPRHRAD52610103K11Rik

Drugs targeting this protein would theoretically modulate DNA repair via influencing ubiquitination of PCNA and related DNA damage response; currently, no specific drugs are listed in search results[1][2][5].