SCUBA

HPF1 — Histone PARylation factor 1

HPF1 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

HPF1's module in each cell type

Cell typeModuleShares the module with
Gamma-delta T cellsT cell Survival
T cell maturation
ARFRP1, BCL2L1, C6orf47, CHD9, DAXX, DEF6, DENND2D, DHPS +26 more
MacrophagesMitotic Spindle Assembly
Cell cycle
ACTL6A, AKR7A2, ANP32E, BOLA3, BUB3, CCDC167, CENPW, CENPX +34 moreView in SCUBA

About the gene

SynonymsC4orf27, FLJ20534
Chromosome4: 169729470-169757944
Predicted locationIntracellular
Essential geneNo
Protein classPredicted intracellular proteins
Biological processDNA damage, DNA repair

Function

Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response. Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins. Serine ADP- ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. Serine ADP- ribosylation of proteins constitutes the primary form of ADP- ribosylation of proteins in response to DNA damage. HPF1 acts by completing the active site of PARP1 and PARP2: forms a composite active site composed of residues from HPF1 and PARP1 or PARP2. While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains. HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.