Family Search for PF10228 (HPF1)

April 2024: See Interactive Tools for Functional Annotation of Bacterial Genomes for advice on using these tools.

PF10228 hits 7 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.

HPF1_HUMAN / Q9NWY4 Histone PARylation factor 1 from Homo sapiens (Human) (see 18 papers)
NP_060337 histone PARylation factor 1 from Homo sapiens
Aligns to 77:328 / 346 (72.8%), covers 100.0% of PF10228, 376.5 bits

• function: Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response (PubMed:28190768, PubMed:29480802, PubMed:29954836, PubMed:33186521, PubMed:32028527, PubMed:32939087, PubMed:34486521, PubMed:34874266, PubMed:34210965, PubMed:34625544, PubMed:33589610, PubMed:34732825, PubMed:33683197, PubMed:34795260, PubMed:34108479). 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 (PubMed:28190768, PubMed:29480802, PubMed:29954836, PubMed:32028527, PubMed:32939087, PubMed:34486521, PubMed:34874266, PubMed:34625544, PubMed:33589610, PubMed:34732825, PubMed:33683197, PubMed:34795260). 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 (PubMed:27067600, PubMed:28190768, PubMed:32939087, PubMed:33589610). Serine ADP- ribosylation of proteins constitutes the primary form of ADP- ribosylation of proteins in response to DNA damage (PubMed:29480802). 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 (PubMed:32028527, PubMed:33589610). 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 (PubMed:34732825, PubMed:33683197, PubMed:34795260). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed:29954836, PubMed:30257210).
  subunit: Interacts with PARP1 (via the PARP catalytic domain) (PubMed:27067600, PubMed:32028527, PubMed:33589610). Interacts with PARP2 (via the PARP catalytic domain) (PubMed:27067600, PubMed:33141820, PubMed:34108479, PubMed:32028527, PubMed:32939087). Interacts with core nucleosomes in a PARP1- and PARP2-dependent manner (PubMed:27067600, PubMed:32939087).
• Germline HPF1 retrogene insertion in RB1 gene involved in cancer predisposition.
  Le, Journal of medical genetics 2023 (PubMed)
  • GeneRIF: Germline HPF1 retrogene insertion in RB1 gene involved in cancer predisposition.
• HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.
  Sun, Nature communications 2021
  • GeneRIF: HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.
• HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.
  Rudolph, eLife 2021
  • GeneRIF: HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.
• Serine-linked PARP1 auto-modification controls PARP inhibitor response.
  Prokhorova, Nature communications 2021
  • GeneRIF: Serine-linked PARP1 auto-modification controls PARP inhibitor response.
• The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
  Hendriks, Nature communications 2021
  • GeneRIF: The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
• Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.
  Kurgina, Communications biology 2021
  • GeneRIF: Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.
• HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.
  Langelier, Nature communications 2021
  • GeneRIF: HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.
• HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.
  Suskiewicz, Nature 2020
  • GeneRIF: HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation; as HPF1 forms a joint active site with PARP1 or PARP2, our data implicate HPF1 as an important determinant of the response to clinical PARP inhibitors
• More
• Slow Dissociation from the PARP1-HPF1 Complex Drives Inhibitor Potency.
  Stojanovic, Biochemistry 2023
  • “...PARP1HPF1 complex ( PDF ) Supplementary Material bi3c00243_si_001.pdf Accession Codes PARP1, UniProtKB P09874. HPF1, UniProtKB: Q9NWY4. Author Contributions P.S. performed most of the assays and data analysis. J.R. performed some of the assays, designed and optimized the assay format, and assisted with the data analysis. P.S.,...”
• Hyperthermia enhances the efficacy of chemotherapeutic drugs in heat-sensitive cells through interfering with DNA damage repair.
  Ni, Annals of translational medicine 2022
  • “...cells treated with chemotherapy alone (group B) Protein accession Gene name Protein description D/B ratio Q9NWY4 HPF1 Histone PARylation factor 1 0.8315 A6NHR9 SMCHD1 Structural maintenance of chromosomes flexible hinge domain-containing protein 1 0.831 P50851 LRBA Lipopolysaccharide-responsive and beige-like anchor protein 0.8215 Q12873 CHD3 Chromodomain-helicase-DNA-binding protein...”
• Alleviation of a polyglucosan storage disorder by enhancement of autophagic glycogen catabolism
  Kakhlon, EMBO molecular medicine 2021
  • “...DR1 associated protein 1(DRAP1) + Q9UBB4 Ataxin 10(ATXN10) + Q96A33 Coiledcoil domain containing 47(CCDC47) + Q9NWY4 Histone PARylation factor 1(HPF1) + Q9UI26 Importin 11(IPO11) + a A functional assembly which includes at least one protein and other macromolecules and/or ligands. b Small, spherical organelles enclosed by...”
• Structure and dynamics of the chromatin remodeler ALC1 bound to a PARylated nucleosome.
  Bacic, eLife 2021
  • “...Q86WJ1 Recombinant DNA reagent Human HPF1 (1346) pET28a (plasmid) Gaullier et al., 2020 UniProt ID Q9NWY4 Recombinant DNA reagent Human PARP1 (11014) pET28a (plasmid) Langelier et al., 2017 UniProt ID P09874 Recombinant DNA reagent Human PARP2 Isoform 2 (1-570) pET28a (plasmid) GenScript UniProt ID Q9UGN5 Software,...”
• HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.
  Rudolph, eLife 2021
  • “...PARP1 UniProt P09874 As described in Rudolph et al., 2018 Peptide, recombinant protein HPF1 UniProt Q9NWY4 As described in manuscript Sequenced-based reagent p18mer DNA IDT 5-phosphate-GGGTTGCGGCCGCTTGGG-3; double-stranded Strain, strain background ( Escherichia coli ) Rosetta DE3 pLys EMD Millipore 70956 Chemically competent cells Other 384-well plates...”
• Brain Proteomic Profiling in Intractable Epilepsy Caused by TSC1 Truncating Mutations: A Small Sample Study.
  Liu, Frontiers in neurology 2020
  • “...protein gamma (PURG) 0.007938768 2.38 Nucleus P15559 NAD(P)H dehydrogenase [quinone] 1 (NQO1) 0.03367561 2.4 Cytoplasm Q9NWY4 Histone PARylation factor 1 (HPF1) 0.044527851 2.55 P54105 Methylosome subunit pICln (CLNS1A) 0.045372858 2.56 Cytoplasm/Nucleus O00273 DNA fragmentation factor subunit alpha (DFFA) 0.019867376 2.58 Cytoplasm Q96BW5 Phosphotriesterase-related protein (PTER) 0.010206613...”
• Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.
  Bilokapic, Nature 2020
  • “...inverse PCR (iPCR) using plasmids that contained the gene for the full-length protein: HPF1 (UniProt Q9NWY4) and PARP2 (UniProt Q9UGN52). iPCR reactions were set up in a total volume of 25 l. 10 l of purified PCR product was incubated with 5 U of T4 PNK...”
• Establishment of neutralizing rat monoclonal antibodies for fibroblast growth factor-2.
  Tanaka, Monoclonal antibodies in immunodiagnosis and immunotherapy 2014
• More

Q8CFE2 Histone PARylation factor 1 from Mus musculus
Aligns to 77:328 / 346 (72.8%), covers 100.0% of PF10228, 372.6 bits

• Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis
  Huang, Molecular cell 2020
  • “...wild-type (Wt) or catalytically inactive mutant (W170A) NMNAT-1 (UniProt entry Q9EPA7), and HPF1 (UniProt entry Q8CFE2) was expressed in E. coli strain BL21(DE3) using a pET19b-based bacterial expression vector. The transformed bacteria were grown in LB containing ampicillin at 37 C until the OD595 reached 0.40.6....”

HPF1_DANRE / Q7SXS8 Histone PARylation factor 1 from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
Aligns to 80:329 / 348 (71.8%), covers 100.0% of PF10228, 355.4 bits

• 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.
  subunit: Interacts with PARP1 (via the PARP catalytic domain). Interacts with PARP2 (via the PARP catalytic domain). Interacts with core nucleosomes in a parp1- and parp2-dependent manner.
  disruption phenotype: Morpholino knockdown of the protein causes malformation anbd delayed hatching.

A7RS11 Histone PARylation factor 1 from Nematostella vectensis
Aligns to 62:310 / 327 (76.1%), covers 100.0% of PF10228, 343.2 bits

• HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
  Suskiewicz, Nature 2020
  • “...DNA damage. Materials and methods Plasmids and mutagenesis The gene for Nematostella vectensis HPF1 (UniProt A7RS11) was codon-optimised for Escherichia coli expression, synthesised, and subcloned into pET28a with a C-terminal His 6 -tag. The gene encoding human HPF1 was recloned from pDONR211 5 into pET28a for...”

B7P8X7 Histone PARylation factor 1 from Ixodes scapularis
Aligns to 99:347 / 372 (66.9%), covers 100.0% of PF10228, 312.8 bits

• Phosphoproteomic Analysis of Haemaphysalis longicornis Saliva Reveals the Influential Contributions of Phosphoproteins to Blood-Feeding Success
  Agwunobi, Frontiers in cellular and infection microbiology 2021
  • “...5 (8.3%) Chromatin/chromatin-binding, or -regulatory protein (PC00077) DEK_C domain-containing protein (B7P839); apoptotic protease-activating factor, putative (B7P8X7); DNA replication factor/protein phosphatase inhibitor SET/SPR-2, putative (B7Q573) 3 (5%) Cytoskeletal protein (PC00085) SH3 domain-containing protein (B7P0V4); Aldolase_II domain-containing protein (B7P1C8); PDZ domain-containing protein (B7P6T6); Microtubule-binding protein, putative (B7PPL3); LIM...”

NP_649589 histone PARylation factor 1 from Drosophila melanogaster
Aligns to 176:428 / 449 (56.3%), covers 100.0% of PF10228, 281.1 bits

• Solution structure of a zinc-finger domain that binds to poly-ADP-ribose.
  Isogai, Genes to cells : devoted to molecular & cellular mechanisms 2010 (PubMed)
  • GeneRIF: the three-dimensional structure of the poly-ADP-ribose (pADPr)-binding zinc-finger domain from Drosophila melanogaster CG1218-PA

XP_036010205 histone PARylation factor 1 isoform X3 from Mus musculus
Aligns to 1:169 / 187 (90.4%), covers 62.9% of PF10228, 204.6 bits

• HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.
  Sun, Nature communications 2021
  • GeneRIF: HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.

Or search for genetic data about PF10228 in the Fitness Browser