HIRIP3 interacts with the HIRA histone chaperone []. It can be phosphorylated by the serine-threonine kinase CK2 and may be involved in chromatin metabolism [].
This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones [].
