PHD and RING finger domain-containing protein 1 (PHRF1)

PHD and RING finger domain-containing protein 1 (PHRF1) is a multi-domain nuclear protein characterized by its possession of a PHD finger, a motif that recognizes methylated histone H3 (notably H3K36me2 and H3K36me3), and a RING finger, mediating E3 ubiquitin ligase activity[3][1]. PHRF1 participates in chromatin biology including transcriptional regulation, DNA damage response through non-homologous end joining, and protein ubiquitination (notably of PARP1 and TGIF), contributing to genome integrity and cellular responses to genotoxic stress[1][3][5]. It is associated with transcriptional regulation via interactions with RNA polymerase II, splicing factors, and chromatin marks, and shown to regulate cell cycle checkpoint control and splicing-associated genes[1]. Overexpression or aberrant function of PHRF1 has been implicated in multiple cancers, in part owing to its contribution to DNA repair, chromatin dynamics, and suppression of tumorigenic signaling pathways[1][3].

Other names

PHRF1KIAA1542PPP1R125RNF221CTD-binding SR-like protein rA9protein phosphatase 1 regulatory subunit 125