Family Search for PF10228 (DUF2228)
PF10228 hits 7 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.
HPF1_HUMAN / Q9NWY4 Histone PARylation factor 1 from Homo sapiens (Human) (see 18 papers)
Aligns to 77:328 / 346 (72.8%), covers 100.0% of PF10228, 369.9 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).
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, 358.4 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.
Or search for genetic data about PF10228 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory