Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
2.4.2.-
Transferases;
Glycosyltransferases;
Pentosyltransferases;
2.4.2.30
Transferases;
Glycosyltransferases;
Pentosyltransferases;
NAD+ ADP-ribosyltransferase
PDB | Resolution (Å) | PDB name |
---|---|---|
1UK0 | 3.0 | Crystal structure of catalytic domain of human poly(ADP-ribose) polymerase with a novel inhibitor |
1UK1 | 3.0 | Crystal structure of human poly(ADP-ribose) polymerase complexed with a potent inhibitor |
1WOK | 3.0 | Crystal structure of catalytic domain of human poly(ADP-ribose) polymerase complexed with a quinoxaline-type inhibitor |
2COK | Solution structure of BRCT domain of poly(ADP-ribose) polymerase-1 | |
2CR9 | Solution structure of WGR domain of poly(ADP-ribose) polymerase-1 | |
2CS2 | Solution structure of the second Zn-finger domain of poly(ADP-ribose) polymerase-1 | |
2DMJ | Solution structure of the first zf-PARP domain of human Poly(ADP-ribose)polymerase-1 | |
2JVN | Domain C of human PARP-1 | |
2L30 | Human PARP-1 zinc finger 1 | |
2L31 | Human PARP-1 zinc finger 2 | |
2N8A | 1H, 13C and 15N chemical shift assignments and solution structure for PARP-1 F1F2 domains in complex with a DNA single-strand break | |
2RCW | 2.8 | PARP complexed with A620223 |
2RD6 | 2.3 | PARP complexed with A861695 |
2RIQ | 1.7 | Crystal Structure of the Third Zinc-binding domain of human PARP-1 |
3GJW | 2.3 | PARP complexed with A968427 |
3GN7 | 2.5 | PARP complexed with A861696 |
3L3L | 2.5 | PARP complexed with A906894 |
3L3M | 2.5 | PARP complexed with A927929 |
3OD8 | 2.4 | Human PARP-1 zinc finger 1 (Zn1) bound to DNA |
3ODA | 2.64 | Human PARP-1 zinc finger 1 (Zn1) bound to DNA |
3ODC | 2.8 | Human PARP-1 zinc finger 2 (Zn2) bound to DNA |
3ODE | 2.95 | Human PARP-1 zinc finger 2 (Zn2) bound to DNA |
4AV1 | 3.1 | Crystal structure of the human PARP-1 DNA binding domain in complex with DNA |
4DQY | 3.25 | Structure of Human PARP-1 bound to a DNA double strand break |
4GV7 | 2.89 | Human ARTD1 (PARP1) - Catalytic domain in complex with inhibitor ME0328 |
4HHY | 2.3637 | Crystal structure of PARP catalytic domain in complex with novel inhibitors |
4HHZ | 2.7199 | Crystal structure of PARP catalytic domain in complex with novel inhibitors |
4L6S | 2.2 | PARP complexed with benzo[1,4]oxazin-3-one inhibitor |
4OPX | 3.314 | Structure of Human PARP-1 bound to a DNA double strand break in complex with (2R)-5-fluoro-2-methyl-2,3-dihydro-1-benzofuran-7-carboxamide |
4OQA | 3.65 | Structure of Human PARP-1 bound to a DNA double strand break in complex with (2Z)-2-(2,4-dihydroxybenzylidene)-3-oxo-2,3-dihydro-1-benzofuran-7-carboxamide |
4OQB | 3.362 | Structure of Human PARP-1 bound to a DNA double strand break in complex with (2Z)-2-{4-[2-(morpholin-4-yl)ethoxy]benzylidene}-3-oxo-2,3-dihydro-1-benzofuran-7-carboxamide |
4PJT | 2.35 | Structure of PARP1 catalytic domain bound to inhibitor BMN 673 |
4R5W | 2.84 | Human artd1 (parp1) - catalytic domain in complex with inhibitor xav939 |
4R6E | 2.2 | Human artd1 (parp1) - catalytic domain in complex with inhibitor niraparib |
4RV6 | 3.19 | Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib |
4UND | 2.2 | HUMAN ARTD1 (PARP1) - CATALYTIC DOMAIN IN COMPLEX WITH INHIBITOR TALAZOPARIB |
4UXB | 3.22 | Human ARTD1 (PARP1) - Catalytic domain in complex with inhibitor PJ34 |
4XHU | 2.089 | The complex structure of Timeless_PAB and PARP-1_catalytic domain |
4ZZZ | 1.9 | Structure of human PARP1 catalytic domain bound to an isoindolinone inhibitor |
5A00 | 2.75 | Structure of human PARP1 catalytic domain bound to an isoindolinone inhibitor |
5DS3 | 2.6 | Crystal structure of constitutively active PARP-1 |
5HA9 | 4.01 | Crystal structure-based design and disovery of a novel PARP1 antiagonist (BL-PA10) that induces apoptosis and inhibits metastasis in triple negative breast cancer |
5KPN | 2.3 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5KPO | 2.65 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5KPP | 2.33 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5KPQ | 2.55 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5WRQ | 2.65 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5WRY | 2.3 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5WRZ | 2.2 | Structure of human PARP1 catalytic domain bound to a phthalazinone inhibitor |
5WS0 | 2.6 | Structure of human PARP1 catalytic domain bound to a benzoimidazole inhibitor |
5WS1 | 1.9 | Structure of human PARP1 catalytic domain bound to a benzoimidazole inhibitor |
5WTC | 2.2 | Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor |
5XSR | 2.3 | novel orally efficacious inhibitors complexed with PARP1 |
5XST | 2.3 | novel orally efficacious inhibitors complexed with PARP1 |
5XSU | 2.4 | novel orally efficacious inhibitors complexed with PARP1 |
6BHV | 2.3 | Human PARP-1 bound to NAD+ analog benzamide adenine dinucleotide (BAD) |
6GHK | 2.28 | Human PARP1 (ARTD1) - Catalytic domain in complex with inhibitor ME0527 |
6M3I | 1.98 | Crystal structure of HPF1/PARP1 complex |
6NRF | 2.0 | Crystal Structure of human PARP-1 ART domain bound to inhibitor UTT103 |
6NRG | 1.7 | Crystal Structure of human PARP-1 ART domain bound to inhibitor UTT57 |
6NRH | 1.5 | Crystal Structure of human PARP-1 ART domain bound inhibitor UTT63 |
6NRI | 2.2 | Crystal Structure of human PARP-1 ART domain bound to inhibitor UTT83 |
6NRJ | 1.65 | Crystal Structure of human PARP-1 ART domain bound to inhibitor UTT93 |
6NTU | 1.8 | Crystal Structure of human PARP-1 ART domain bound to inhibitor UKTT-15 |
6VKK | 2.1 | Crystal Structure of human PARP-1 CAT domain bound to inhibitor rucaparib |
6VKO | 2.8 | Crystal Structure of human PARP-1 CAT domain bound to inhibitor UKTT15 |
6VKQ | 2.9 | Crystal Structure of human PARP-1 CAT domain bound to inhibitor EB-47 |
6XVW | 2.0 | Catalytic domain of human PARP-1 in complex with the inhibitor MC2050 |
7AAA | 1.74 | Crystal structure of the catalytic domain of human PARP1 (apo) |
7AAB | 2.8 | Crystal structure of the catalytic domain of human PARP1 in complex with inhibitor EB-47 |
7AAC | 1.593 | Crystal structure of the catalytic domain of human PARP1 in complex with veliparib |
7AAD | 2.21 | Crystal structure of the catalytic domain of human PARP1 in complex with olaparib |
7CMW | 2.7 | Complex structure of PARP1 catalytic domain with pamiparib |
7KK2 | 1.695 | Structure of the catalytic domain of PARP1 |
7KK3 | 2.06 | Structure of the catalytic domain of PARP1 in complex with talazoparib |
7KK4 | 1.96 | Structure of the catalytic domain of PARP1 in complex with olaparib |
7KK5 | 1.7 | Structure of the catalytic domain of PARP1 in complex with niraparib |
7KK6 | 2.06 | Structure of the catalytic domain of PARP1 in complex with veliparib |
7ONR | 2.05 | PARP1 catalytic domain in complex with 8-chloroquinazolinone-based inhibitor (compound 9) |
7ONS | 1.97 | PARP1 catalytic domain in complex with isoquinolone-based inhibitor (compound 16) |
7ONT | 1.853 | PARP1 catalytic domain in complex with a selective pyridine carboxamide-based inhibitor (compound 22) |
7S68 | 3.3 | Structure of human PARP1 domains (Zn1, Zn3, WGR and HD) bound to a DNA double strand break. |
7S6H | 3.1 | Human PARP1 deltaV687-E688 bound to NAD+ analog EB-47 and to a DNA double strand break. |
7S6M | 3.2 | Human PARP1 deltaV687-E688 bound to a DNA double strand break. |
7S81 | 3.6 | Structure of human PARP1 domains (Zn1, Zn3, WGR, HD) bound to a DNA double strand break. |
7SCY | 4.1 | Nuc147 bound to single BRCT |
7SCZ | 3.5 | Nuc147 bound to multiple BRCTs |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:1990966 | ATP generation from poly-ADP-D-ribose |
Biological Process | GO:0030592 | DNA ADP-ribosylation |
Biological Process | GO:0006974 | DNA damage response |
Biological Process | GO:0006281 | DNA repair |
Biological Process | GO:0006915 | apoptotic process |
Biological Process | GO:0016051 | carbohydrate biosynthetic process |
Biological Process | GO:0034644 | cellular response to UV |
Biological Process | GO:1904646 | cellular response to amyloid-beta |
Biological Process | GO:0032869 | cellular response to insulin stimulus |
Biological Process | GO:1990090 | cellular response to nerve growth factor stimulus |
Biological Process | GO:0034599 | cellular response to oxidative stress |
Biological Process | GO:0071294 | cellular response to zinc ion |
Biological Process | GO:0046697 | decidualization |
Biological Process | GO:0006302 | double-strand break repair |
Biological Process | GO:0045087 | innate immune response |
Biological Process | GO:0030225 | macrophage differentiation |
Biological Process | GO:0032042 | mitochondrial DNA metabolic process |
Biological Process | GO:0043504 | mitochondrial DNA repair |
Biological Process | GO:0007005 | mitochondrion organization |
Biological Process | GO:2001170 | negative regulation of ATP biosynthetic process |
Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
Biological Process | GO:1904178 | negative regulation of adipose tissue development |
Biological Process | GO:0045824 | negative regulation of innate immune response |
Biological Process | GO:1904357 | negative regulation of telomere maintenance via telomere lengthening |
Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
Biological Process | GO:0034244 | negative regulation of transcription elongation by RNA polymerase II |
Biological Process | GO:0032786 | positive regulation of DNA-templated transcription, elongation |
Biological Process | GO:0043123 | positive regulation of I-kappaB kinase/NF-kappaB signaling |
Biological Process | GO:0060391 | positive regulation of SMAD protein signal transduction |
Biological Process | GO:0010613 | positive regulation of cardiac muscle hypertrophy |
Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
Biological Process | GO:0033148 | positive regulation of intracellular estrogen receptor signaling pathway |
Biological Process | GO:0051901 | positive regulation of mitochondrial depolarization |
Biological Process | GO:1904762 | positive regulation of myofibroblast differentiation |
Biological Process | GO:0060545 | positive regulation of necroptotic process |
Biological Process | GO:1901216 | positive regulation of neuron death |
Biological Process | GO:1900182 | positive regulation of protein localization to nucleus |
Biological Process | GO:1903518 | positive regulation of single strand break repair |
Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
Biological Process | GO:2000679 | positive regulation of transcription regulatory region DNA binding |
Biological Process | GO:0070213 | protein auto-ADP-ribosylation |
Biological Process | GO:0016540 | protein autoprocessing |
Biological Process | GO:0071168 | protein localization to chromatin |
Biological Process | GO:0036211 | protein modification process |
Biological Process | GO:0070212 | protein poly-ADP-ribosylation |
Biological Process | GO:0044030 | regulation of DNA methylation |
Biological Process | GO:0010990 | regulation of SMAD protein complex assembly |
Biological Process | GO:1905051 | regulation of base-excision repair |
Biological Process | GO:0050790 | regulation of catalytic activity |
Biological Process | GO:0045188 | regulation of circadian sleep/wake cycle, non-REM sleep |
Biological Process | GO:1903376 | regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway |
Biological Process | GO:0032880 | regulation of protein localization |
Biological Process | GO:0071932 | replication fork reversal |
Biological Process | GO:1904044 | response to aldosterone |
Biological Process | GO:0010332 | response to gamma radiation |
Biological Process | GO:0023019 | signal transduction involved in regulation of gene expression |
Biological Process | GO:0000723 | telomere maintenance |
Biological Process | GO:0006366 | transcription by RNA polymerase II |
Biological Process | GO:0007179 | transforming growth factor beta receptor signaling pathway |
Molecular Function | GO:0003677 | DNA binding |
Molecular Function | GO:0140294 | NAD DNA ADP-ribosyltransferase activity |
Molecular Function | GO:0051287 | NAD binding |
Molecular Function | GO:0003950 | NAD+ ADP-ribosyltransferase activity |
Molecular Function | GO:0140806 | NAD+- protein-aspartate ADP-ribosyltransferase activity |
Molecular Function | GO:0140822 | NAD+-histone H2BE35 glutamate ADP-ribosyltransferase activity |
Molecular Function | GO:0140816 | NAD+-histone H2BS6 serine ADP-ribosyltransferase activity |
Molecular Function | GO:0140817 | NAD+-histone H3S10 serine ADP-ribosyltransferase activity |
Molecular Function | GO:1990404 | NAD+-protein ADP-ribosyltransferase activity |
Molecular Function | GO:0140807 | NAD+-protein-glutamate ADP-ribosyltransferase activity |
Molecular Function | GO:0140815 | NAD+-protein-histidine ADP-ribosyltransferase activity |
Molecular Function | GO:0140805 | NAD+-protein-serine ADP-ribosyltransferase activity |
Molecular Function | GO:0140808 | NAD+-protein-tyrosine ADP-ribosyltransferase activity |
Molecular Function | GO:0070412 | R-SMAD binding |
Molecular Function | GO:0003723 | RNA binding |
Molecular Function | GO:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
Molecular Function | GO:0003682 | chromatin binding |
Molecular Function | GO:0003684 | damaged DNA binding |
Molecular Function | GO:0008047 | enzyme activator activity |
Molecular Function | GO:0019899 | enzyme binding |
Molecular Function | GO:0042826 | histone deacetylase binding |
Molecular Function | GO:0042802 | identical protein binding |
Molecular Function | GO:0030331 | nuclear estrogen receptor binding |
Molecular Function | GO:0031491 | nucleosome binding |
Molecular Function | GO:0016779 | nucleotidyltransferase activity |
Molecular Function | GO:0042803 | protein homodimerization activity |
Molecular Function | GO:0019901 | protein kinase binding |
Molecular Function | GO:0008270 | zinc ion binding |
Cellular Component | GO:0000785 | chromatin |
Cellular Component | GO:0000781 | chromosome, telomeric region |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0016020 | membrane |
Cellular Component | GO:0005739 | mitochondrion |
Cellular Component | GO:0016604 | nuclear body |
Cellular Component | GO:0005635 | nuclear envelope |
Cellular Component | GO:0043596 | nuclear replication fork |
Cellular Component | GO:0005730 | nucleolus |
Cellular Component | GO:0005654 | nucleoplasm |
Cellular Component | GO:0005634 | nucleus |
Cellular Component | GO:0032993 | protein-DNA complex |
Cellular Component | GO:0032991 | protein-containing complex |
Cellular Component | GO:0090734 | site of DNA damage |
Cellular Component | GO:0035861 | site of double-strand break |
Cellular Component | GO:0005667 | transcription regulator complex |
InterPro | InterPro name |
---|---|
IPR001357 | BRCT domain |
IPR001510 | Zinc finger, PARP-type |
IPR004102 | Poly(ADP-ribose) polymerase, regulatory domain |
IPR008288 | Poly [ADP-ribose] polymerase |
IPR008893 | WGR domain |
IPR012317 | Poly(ADP-ribose) polymerase, catalytic domain |
IPR012982 | PADR1, zinc ribbon fold |
IPR036420 | BRCT domain superfamily |
IPR036616 | Poly(ADP-ribose) polymerase, regulatory domain superfamily |
IPR036930 | WGR domain superfamily |
IPR036957 | Zinc finger, PARP-type superfamily |
IPR038650 | PADR1, C-terminal domain superfamily |
IPR047572 | PADR1 domain |
Pfam | Pfam name |
---|---|
PF00533 | BRCA1 C Terminus (BRCT) domain |
PF00644 | Poly(ADP-ribose) polymerase catalytic domain |
PF00645 | Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region |
PF02877 | Poly(ADP-ribose) polymerase, regulatory domain |
PF05406 | WGR domain |
PF08063 | PADR1 (NUC008) domain |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-110362 | POLB-Dependent Long Patch Base Excision Repair | Leaf | R-HSA-73894 | DNA Repair |
R-HSA-192814 | vRNA Synthesis | Leaf | R-HSA-1643685 | Disease |
R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | Leaf | R-HSA-74160 | Gene expression (Transcription) |
R-HSA-3108214 | SUMOylation of DNA damage response and repair proteins | Leaf | R-HSA-392499 | Metabolism of proteins |
R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | Leaf | R-HSA-73894 | DNA Repair |
R-HSA-5696394 | DNA Damage Recognition in GG-NER | Leaf | R-HSA-73894 | DNA Repair |
R-HSA-5696395 | Formation of Incision Complex in GG-NER | Leaf | R-HSA-73894 | DNA Repair |
R-HSA-5696400 | Dual Incision in GG-NER | Leaf | R-HSA-73894 | DNA Repair |
Location | ECO term | Pubmed |
---|---|---|
Chromosome | ECO:0000269 | PubMed:15607977 |
Chromosome | ECO:0000269 | PubMed:22683995 |
Chromosome | ECO:0000269 | PubMed:23230272 |
Chromosome | ECO:0000269 | PubMed:26344098 |
Chromosome | ECO:0000269 | PubMed:27568560 |
Chromosome | ECO:0000269 | PubMed:30675909 |
Chromosome | ECO:0000269 | PubMed:32241924 |
Chromosome | ECO:0000269 | PubMed:32358582 |
Chromosome | ECO:0000269 | PubMed:33168626 |
Chromosome | ECO:0000269 | PubMed:33412112 |
Chromosome | ECO:0000269 | PubMed:34625544 |
Chromosome | ECO:0000269 | PubMed:34795260 |
Chromosome | ECO:0000269 | PubMed:35013556 |
Chromosome | ECO:0000269 | PubMed:35104452 |
Chromosome | ECO:0000269 | PubMed:9721847 |
Cytoplasm | ECO:0000269 | PubMed:33168626 |
Cytoplasm, cytosol | ECO:0000269 | PubMed:33168626 |
Cytoplasm, cytosol | ECO:0000269 | PubMed:35460603 |
Nucleus | ECO:0000269 | PubMed:17177976 |
Nucleus | ECO:0000269 | PubMed:21799911 |
Nucleus | ECO:0000269 | PubMed:23230272 |
Nucleus | ECO:0000269 | PubMed:35460603 |
Nucleus, nucleolus | ECO:0000269 | PubMed:9518481 |