Details for: HPF1

Gene ID: 54969

Symbol: HPF1

Ensembl ID: ENSG00000056050

Description: histone PARylation factor 1

Associated with

Other Information

Genular Protein ID: 1031277791

Symbol: HPF1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11230166

Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.

PubMed ID: 11230166

DOI: 10.1101/gr.gr1547r

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 27067600

Title: HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity.

PubMed ID: 27067600

DOI: 10.1016/j.molcel.2016.03.008

PubMed ID: 28190768

Title: Serine ADP-ribosylation depends on HPF1.

PubMed ID: 28190768

DOI: 10.1016/j.molcel.2017.01.003

PubMed ID: 30257210

Title: Interplay of histone marks with serine ADP-ribosylation.

PubMed ID: 30257210

DOI: 10.1016/j.celrep.2018.08.092

PubMed ID: 29480802

Title: Serine is the major residue for ADP-ribosylation upon DNA damage.

PubMed ID: 29480802

DOI: 10.7554/elife.34334

PubMed ID: 29954836

Title: Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.

PubMed ID: 29954836

DOI: 10.15252/embr.201745310

PubMed ID: 33186521

Title: An HPF1/PARP1-based chemical biology strategy for exploring ADP-ribosylation.

PubMed ID: 33186521

DOI: 10.1016/j.cell.2020.09.055

PubMed ID: 33141820

Title: Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1.

PubMed ID: 33141820

DOI: 10.1371/journal.pone.0240932

PubMed ID: 34732825

Title: Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.

PubMed ID: 34732825

DOI: 10.1038/s42003-021-02780-0

PubMed ID: 33683197

Title: HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.

PubMed ID: 33683197

DOI: 10.7554/elife.65773

PubMed ID: 34486521

Title: Structure and dynamics of the chromatin remodeler ALC1 bound to a PARylated nucleosome.

PubMed ID: 34486521

DOI: 10.7554/elife.71420

PubMed ID: 34874266

Title: Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling.

PubMed ID: 34874266

DOI: 10.7554/elife.71502

PubMed ID: 34108479

Title: Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition.

PubMed ID: 34108479

DOI: 10.1038/s41467-021-23800-x

PubMed ID: 34210965

Title: Serine-linked PARP1 auto-modification controls PARP inhibitor response.

PubMed ID: 34210965

DOI: 10.1038/s41467-021-24361-9

PubMed ID: 34625544

Title: The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.

PubMed ID: 34625544

DOI: 10.1038/s41467-021-26172-4

PubMed ID: 34795260

Title: HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.

PubMed ID: 34795260

DOI: 10.1038/s41467-021-27043-8

PubMed ID: 32028527

Title: HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.

PubMed ID: 32028527

DOI: 10.1038/s41586-020-2013-6

PubMed ID: 32939087

Title: Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.

PubMed ID: 32939087

DOI: 10.1038/s41586-020-2725-7

PubMed ID: 33589610

Title: HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.

PubMed ID: 33589610

DOI: 10.1038/s41467-021-21302-4

Sequence Information:

  • Length: 346
  • Mass: 39436
  • Checksum: DF411C9AE254E1E1
  • Sequence:
  • MVGGGGKRRP GGEGPQCEKT TDVKKSKFCE ADVSSDLRKE VENHYKLSLP EDFYHFWKFC 
    EELDPEKPSD SLSASLGLQL VGPYDILAGK HKTKKKSTGL NFNLHWRFYY DPPEFQTIII 
    GDNKTQYHMG YFRDSPDEFP VYVGINEAKK NCIIVPNGDN VFAAVKLFLT KKLREITDKK 
    KINLLKNIDE KLTEAARELG YSLEQRTVKM KQRDKKVVTK TFHGAGLVVP VDKNDVGYRE 
    LPETDADLKR ICKTIVEAAS DEERLKAFAP IQEMMTFVQF ANDECDYGMG LELGMDLFCY 
    GSHYFHKVAG QLLPLAYNLL KRNLFAEIIE EHLANRSQEN IDQLAA

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.