HIRA-interacting protein 3 (HIRIP3)

HIRA-interacting protein 3 (HIRIP3) is a mammalian nuclear protein, identified through its binding to HIRA, which is a core regulator of chromatin organization. HIRIP3 directly interacts with core histones H2A, H2B, and H3, acting as a histone chaperone that assists in chromatin assembly by carrying H2A-H2B complexes and facilitating their deposition onto DNA. It modulates the selectivity of histone phosphorylation, notably enabling CK2 kinase-mediated phosphorylation of H2A at serine 1[2][4][5][7]. HIRIP3 is implicated in chromatin metabolism and has developmental relevance via its interactions within the larger HIRA protein complex, but it is not considered a therapeutic target, receptor, or druggable protein currently. There are no reported drugs, mechanisms of drug action, or associated biomarkers for HIRIP3. Notably, alterations in genes overlapping with or encoding HIRIP3 may contribute to certain developmental syndromes[4][5][6].

Other names

HIRIP3HIRA interacting protein 3HIRA-interacting protein 3

No drugs target HIRIP3, but mechanistically, it acts as a histone chaperone, facilitating the deposition of H2A-H2B dimers and enabling CK2-dependent phosphorylation of H2A