Histone PARylation factor 1 (HPF1, previously known as C4orf27) is a key regulator of ADP-ribosylation signaling in response to DNA damage. It has been demonstrated that HPF1 forms a complex with PARP-1 (poly(ADP-ribose) polymerase 1) and is recruited to DNA lesions in a PARP-1-dependent manner, but independently of PARP-1 catalytic ADP-ribosylation activity. HPF1 has also been shown limit DNA damage-induced hyper-automodification of PARP-1 by promoting PARP-1-dependent in trans ADP-ribosylation of histones [].
This entry represents a conserved domain found at the N terminus of a number of fungal proteins. These proteins are largely annotated as being hyphally-regulated cell wall proteins that are induced in response to hyphal development. Proteins containing this domain include Hpf1 from budding yeasts and Hyr1 from Candida albicans. Hpf1 can reduce haziness in white wine []. Hyr1 is a GPI-anchored hyphal cell wall protein required for hyphal growth and virulence. It is involved in innate immune cell evasion through confering resistance to neutrophil killing [, ].
