| + |
NAT10 | up-regulates quantity by stabilization 
acetylation
|
PARP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273715 |
Lys949 |
PKGKHSVkGLGKTTP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31616951 |
MORC2 directly interacts with PARP1. MORC2 mediates the interaction between PARP1 and NAT10 and thereby promotes NAT10-mediated PARP1 acetylation at K949, which blocks CHFR-mediated ubiquitination and degradation of PARP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATR | down-regulates activity 
phosphorylation
|
PARP1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277551 |
Ser179 |
FRPEYSAsQLKGFSL |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 33811702 |
Specifically, ATR binds to and phosphorylates PARP1 at Ser179 after the ionophore treatments. This site-specific phosphorylation inactivates PARP1, inhibiting ionophore-induced necrosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
ERK1/2 | up-regulates
phosphorylation
|
PARP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244669 |
Ser372 |
VAATPPPsTASAPAA |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16627622 |
Parp1 phosphorylation by erk1/2 is required for maximal parp-1 activation after dna damage. S372a and t373a mutations impaired parp-1 activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244673 |
Thr373 |
AATPPPStASAPAAV |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16627622 |
Parp1 phosphorylation by erk1/2 is required for maximal parp-1 activation after dna damage. S372a and t373a mutations impaired parp-1 activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| Pathways: | Acute Myeloid Leukemia, COVID-19 Causal Network, FLT3-ITD in AML, FLT3-ITD signaling, Inhibition of Apoptosis |
| + |
MAPK1 | up-regulates
phosphorylation
|
PARP1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146220 |
Ser372 |
VAATPPPsTASAPAA |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16627622 |
Parp1 phosphorylation by erk1/2 is required for maximal parp-1 activation after dna damage. S372a and t373a mutations impaired parp-1 activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146224 |
Thr373 |
AATPPPStASAPAAV |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16627622 |
Parp1 phosphorylation by erk1/2 is required for maximal parp-1 activation after dna damage. S372a and t373a mutations impaired parp-1 activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
PRKACA | up-regulates activity
phosphorylation
|
PARP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276651 |
Ser465 |
FLQDVSAsTKSLQEL |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 25069723 |
In the presence of cAMP, recombinant PKA directly phosphorylated recombinant PARP1 on serines 465 (in the automodification domain) and 782 and 785 (both in the catalytic domain). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276652 |
Ser782 |
YSLLRGGsDDSSKDP |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 25069723 |
In the presence of cAMP, recombinant PKA directly phosphorylated recombinant PARP1 on serines 465 (in the automodification domain) and 782 and 785 (both in the catalytic domain). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276653 |
Ser785 |
LRGGSDDsSKDPIDV |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 25069723 |
In the presence of cAMP, recombinant PKA directly phosphorylated recombinant PARP1 on serines 465 (in the automodification domain) and 782 and 785 (both in the catalytic domain). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
CDK5 | down-regulates activity
phosphorylation
|
PARP1 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276357 |
Ser782 |
YSLLRGGsDDSSKDP |
in vitro |
|
| pmid |
sentence |
| 21922195 |
These results would suggest that the phosphorylation of PARP-1 via Cdk5's kinase activity is necessary for its persistence at damage sites.Based on these results and the recruitment data, we hypothesize that the phosphorylation of the PARP-1 protein by Cdk5 on one or more of the serines 782, 785, and 786 results in an attenuation of its ribosylating activity facilitating its persistence at the sites of DNA damage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276358 |
Ser785 |
LRGGSDDsSKDPIDV |
in vitro |
|
| pmid |
sentence |
| 21922195 |
These results would suggest that the phosphorylation of PARP-1 via Cdk5's kinase activity is necessary for its persistence at damage sites.Based on these results and the recruitment data, we hypothesize that the phosphorylation of the PARP-1 protein by Cdk5 on one or more of the serines 782, 785, and 786 results in an attenuation of its ribosylating activity facilitating its persistence at the sites of DNA damage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276359 |
Ser786 |
RGGSDDSsKDPIDVN |
in vitro |
|
| pmid |
sentence |
| 21922195 |
These results would suggest that the phosphorylation of PARP-1 via Cdk5's kinase activity is necessary for its persistence at damage sites.Based on these results and the recruitment data, we hypothesize that the phosphorylation of the PARP-1 protein by Cdk5 on one or more of the serines 782, 785, and 786 results in an attenuation of its ribosylating activity facilitating its persistence at the sites of DNA damage. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
Caspase 3 complex | down-regulates activity
cleavage
|
PARP1 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256465 |
|
|
Mus musculus |
L-929 Cell |
| pmid |
sentence |
| 11907276 |
Caspase-3 cleaves parp-1. During cd95-mediated apoptosis proteolytic inactivation of parp-1 by caspases prevents atp depletion and thereby ensures the execution of the apoptotic process |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PARP1 | up-regulates activity
relocalization
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272478 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19629035 |
PARP1 collaborates with Mre11 to promote replication fork restart after release from replication blocks, most likely by recruiting Mre11 to the replication fork to promote resection of DNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-Iodo-3-nitrobenzamide | down-regulates
chemical inhibition
|
PARP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193474 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates activity
cleavage
|
PARP1 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116178 |
|
|
Mus musculus |
L-929 Cell |
| pmid |
sentence |
| 11907276 |
Caspase-3 cleaves parp-1. During cd95-mediated apoptosis proteolytic inactivation of parp-1 by caspases prevents atp depletion and thereby ensures the execution of the apoptotic process |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
veliparib | down-regulates
chemical inhibition
|
PARP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189183 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DNA_damage | up-regulates 
|
PARP1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260065 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17891139 |
We identify the major poly(ADP-ribosyl)ated sites of p53 by PARP-1 and find that PARP-1-mediated poly(ADP-ribosyl)ation blocks the interaction between p53 and the nuclear export receptor Crm1, resulting in nuclear accumulation of p53. These findings molecularly link PARP-1 and p53 in the DNA-damage response, providing the mechanism for how p53 accumulates in the nucleus in response to DNA damage.|PARP-1 is super-activated by binding to damaged DNA, and poly(ADP-ribosyl)ates p53. Poly(ADP-ribosyl)ation probably induces a structural change that mask the NES, and thus Crm1 can no longer target p53 to the nuclear export machinery, resulting in accumulation of p53 in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling, Mitochondrial Control of Apoptosis |
| + |
FLT3 | up-regulates quantity by expression
transcriptional regulation
|
PARP1 |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261554 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21228325 |
Interestingly, quantitative RT-PCR analysis demonstrated a 2-fold increase in PARP-1 expression. Western blotting analysis of protein nuclear extracts from FLT3/ITD B-cells confirmed that PARP1 was up-regulated, compared with wild-type controls |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling |
| + |
PARP1 | up-regulates quantity by expression
transcriptional regulation
|
THBD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254892 |
|
|
Homo sapiens |
Mesothelioma Cell |
| pmid |
sentence |
| 21489980 |
Silencing of PARP1 resulted in a strong down-regulation of TM expression in Met-5A cells, while restoring TM expression in H28 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | up-regulates quantity
binding
|
CHD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264526 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26895424 |
Non-homologous end-joining (NHEJ) is the dominant DSB repair pathway in human cells, but our understanding of how it operates in chromatin is limited. Here, we define a mechanism that plays a crucial role in regulating NHEJ in chromatin. This mechanism is initiated by DNA damage-associated poly(ADP-ribose) polymerase 1 (PARP1), which recruits the chromatin remodeler CHD2 through a poly(ADP-ribose)-binding domain. CHD2 in turn triggers rapid chromatin expansion and the deposition of histone variant H3.3 at sites of DNA damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | up-regulates activity
relocalization
|
KDM5B |
0.363 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271574 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33859667 |
The mechanism of KDM5B recruitment is quite specific and requires the presence of nucleosomes containing histone variant MacroH2A1.1 and PARylation by PARP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1038915-60-4 | down-regulates
chemical inhibition
|
PARP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194399 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZNF365 | up-regulates activity
binding
|
PARP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23966166 |
We identified ZNF365 as a necessary component of the HR repair pathway. ZNF365 interacts with PARP1 and tethers MRE11 to the nucleolytic resection sites for replication fork recovery |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | down-regulates quantity by repression 
transcriptional regulation
|
SERPINF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254891 |
|
|
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 18312852 |
Upregulation of PEDF expression by PARP inhibition contributes to the decrease in hyperglycemia-induced apoptosis in HUVECs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Caspase 7 complex | down-regulates
cleavage
|
PARP1 |
0.708 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256470 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11058599 |
Caspase-7 cleaves parp;redundancy exists between the caspase-3 and -7 at the level of parp proteolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis |
| + |
olaparib | down-regulates
chemical inhibition
|
PARP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195016 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
PARP1 | up-regulates activity
binding
|
POLA1 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261270 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9518481 |
We provide evidence that in proliferating cells: (i) PARP is physically associated with the catalytic subunit of the DNA polymerase α–primase tetramer, an association confirmed by confocal microscopy, demonstrating that both enzymes are co-localized at the nuclear periphery of HeLa cells.|(iii) PARP-deficient cells derived from PARP knock-out mice exhibited reduced DNA polymerase activity, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
PARP1 |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271470 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 23268447 |
Here, we show that checkpoint with Forkhead-associated (FHA) and RING finger domain protein (CHFR), an E3 ubiquitin ligase, is recruited to DSBs by poly(ADP-ribose) (PAR). Moreover, CHFR ubiquitinates PAR polymerase 1 (PARP1) and regulates chromatin-associated PARP1 in vivo. Moreover, the poly-ubiquitin chain on PARP1 could be recognized by both anti-K48 and K63-linked poly-ubiquitin chain antibodies, suggesting that CHFR mediates a mixed poly-ubiquitin chain linkage on PARP1. With MG132 treatment, ubiquitinated PARP1 was significantly accumulated (Figure 4D), suggesting that the ubiquitination of PARP1 is likely involved in protein degradation. Consistently, we found that following DNA damage, PARP1 quickly dissociated from the chromatin in the wild-type cells (Figure 4F). However, in the Chfr−/− cells, the dissociation of PARP1 from the chromatin was significantly delayed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A-966492 | down-regulates
chemical inhibition
|
PARP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205698 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | form complex 
binding
|
SNAIL/RELA/PARP1 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22223884 |
Therefore, we conclude that the endogenous proteins PARP1, p65NF-κB and Snail1 form a ternary complex in the nuclei of cells that are actively expressing fibronectin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | up-regulates activity
relocalization
|
TP53 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261321 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17891139 |
We identify the major poly(ADP-ribosyl)ated sites of p53 by PARP-1 and find that PARP-1-mediated poly(ADP-ribosyl)ation blocks the interaction between p53 and the nuclear export receptor Crm1, resulting in nuclear accumulation of p53. These findings molecularly link PARP-1 and p53 in the DNA-damage response, providing the mechanism for how p53 accumulates in the nucleus in response to DNA damage.|PARP-1 is super-activated by binding to damaged DNA, and poly(ADP-ribosyl)ates p53. Poly(ADP-ribosyl)ation probably induces a structural change that mask the NES, and thus Crm1 can no longer target p53 to the nuclear export machinery, resulting in accumulation of p53 in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling, Mitochondrial Control of Apoptosis |
| + |
LSM-1988 | down-regulates
chemical inhibition
|
PARP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189394 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | down-regulates
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111680 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11907276 |
Caspase-3 cleaves parp-1. During cd95-mediated apoptosis proteolytic inactivation of parp-1 by caspases prevents atp depletion and thereby ensures the execution of the apoptotic process |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, COVID-19 Causal Network, Death Receptor Signaling, FLT3-ITD in AML, FLT3-ITD signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
CASP7 | down-regulates
cleavage
|
PARP1 |
0.708 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83703 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11058599 |
Caspase-7 cleaves parp;redundancy exists between the caspase-3 and -7 at the level of parp proteolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis |
| + |
PARP1 | down-regulates quantity by repression
transcriptional regulation
|
THBD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254893 |
|
|
Homo sapiens |
Squamous Cell Carcinoma Cell |
| pmid |
sentence |
| 21489980 |
Silencing of PARP1 resulted in a strong down-regulation of TM expression in Met-5A cells, while restoring TM expression in H28 cells. We propose that methylation of the TM promoter is responsible for silencing of TM expression in MM tissue, a process that is regulated by PARP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PARP1
- 
- 