{"metadata":{"accession":"PF10228","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR064898","hierarchy":null,"name":{"name":"Histone PARylation factor 1","short":"HPF1"},"description":[{"text":"<p>Histone PARylation factor 1 (HPF1, previously known as C4orf27) is a key regulator of ADP-ribosylation (ADPr) signaling in response to DNA damage. It forms a complex with PARP-1 (poly(ADP-ribose) polymerase 1), creating a composite active site. HPF1 is essential for Ser-ADPr (ADPr on serine residues), which represents the major fraction of ADPr synthesised after DNA damage. This protein is organised into two tightly-associated domains connected via an elaborate linker, showing an alpha-beta structure [[cite:PUB00081458],[cite:PUB00101317],[cite:PUB00101318],[cite:PUB00101316]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00081458":{"PMID":27067600,"ISBN":null,"volume":"62","issue":"3","year":2016,"title":"HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity.","URL":null,"raw_pages":"432-42","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Gibbs-Seymour I","Fontana P","Rack JG","Ahel I."],"DOI_URL":"http://dx.doi.org/10.1016/j.molcel.2016.03.008"},"PUB00101317":{"PMID":28190768,"ISBN":null,"volume":"65","issue":"5","year":2017,"title":"Serine ADP-Ribosylation Depends on HPF1.","URL":null,"raw_pages":"932-940.e6","medline_journal":"Mol Cell","ISO_journal":"Mol Cell","authors":["Bonfiglio JJ","Fontana P","Zhang Q","Colby T","Gibbs-Seymour I","Atanassov I","Bartlett E","Zaja R","Ahel I","Matic I."],"DOI_URL":null},"PUB00101318":{"PMID":33589610,"ISBN":null,"volume":"12","issue":"1","year":2021,"title":"HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.","URL":null,"raw_pages":"1028","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Sun FH","Zhao P","Zhang N","Kong LL","Wong CCL","Yun CH."],"DOI_URL":null},"PUB00101316":{"PMID":32028527,"ISBN":null,"volume":"579","issue":"7800","year":2020,"title":"HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.","URL":null,"raw_pages":"598-602","medline_journal":"Nature","ISO_journal":"Nature","authors":["Suskiewicz MJ","Zobel F","Ogden TEH","Fontana P","Ariza A","Yang JC","Zhu K","Bracken L","Hawthorne WJ","Ahel D","Neuhaus D","Ahel I."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":42,"interactions":0,"matches":1797,"pathways":0,"proteins":1724,"proteomes":1319,"sets":0,"structural_models":{"alphafold":1506},"structures":11,"taxa":4217},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":32,"alignment:full":1333},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6m3g","name":"Crystal structure of human HPF1"}}}