Overview
| Uniprot ID | Q9NWY4 |
|---|
| Protein Name | Histone PARylation factor 1 |
|---|
| Gene Name | HPF1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 27 |
TTDVKKSKFCEADVS |
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:32028527, PubMed:32939087, PubMed:33186521, PubMed:33589610, PubMed:33683197, PubMed:34108479, PubMed:34210965, PubMed:34486521, PubMed:34625544, PubMed:34732825, PubMed:34795260, PubMed:34874266). 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:33589610, PubMed:33683197, PubMed:34486521, PubMed:34625544, PubMed:34732825, PubMed:34795260, PubMed:34874266). 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:33683197, PubMed:34732825, PubMed:34795260). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed:29954836, PubMed:30257210)
Protein Sequence
10
MVGGGGKRRP
20
GGEGPQCEKT
30
TDVKKSKFCE
40
ADVSSDLRKE
50
VENHYKLSLP
60
EDFYHFWKFC
70
EELDPEKPSD
80
SLSASLGLQL
90
VGPYDILAGK
100
HKTKKKSTGL
110
NFNLHWRFYY
120
DPPEFQTIII
130
GDNKTQYHMG
140
YFRDSPDEFP
150
VYVGINEAKK
160
NCIIVPNGDN
170
VFAAVKLFLT
180
KKLREITDKK
190
KINLLKNIDE
200
KLTEAARELG
210
YSLEQRTVKM
220
KQRDKKVVTK
230
TFHGAGLVVP
240
VDKNDVGYRE
250
LPETDADLKR
260
ICKTIVEAAS
270
DEERLKAFAP
280
IQEMMTFVQF
290
ANDECDYGMG
300
LELGMDLFCY
310
GSHYFHKVAG
320
QLLPLAYNLL
330
KRNLFAEIIE
340
EHLANRSQEN
IDQLAA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0090734 |
site of DNA damage |
| Molecular Function |
GO:0003682 |
chromatin binding |
| Molecular Function |
GO:0042393 |
histone binding |
| Molecular Function |
GO:0072572 |
poly-ADP-D-ribose binding |
| Molecular Function |
GO:0140768 |
protein ADP-ribosyltransferase-substrate adaptor activity |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0140861 |
DNA repair-dependent chromatin remodeling |
| Biological Process |
GO:0006302 |
double-strand break repair |
| Biological Process |
GO:0010835 |
regulation of protein ADP-ribosylation |
Reference
PMID: N/A