Q5RHR0
SS
Gene name |
parp1 |
Protein name |
Poly [ADP-ribose] polymerase 1 |
Names |
PARP-1 , EC 2.4.2.30 , ADP-ribosyltransferase diphtheria toxin-like 1 , ARTD1 , DNA ADP-ribosyltransferase PARP1 , EC 2.4.2.- , NAD, + ADP-ribosyltransferase 1 , ADPRT 1 , Poly[ADP-ribose] synthase 1 , Protein poly-ADP-ribosyltransferase PARP1 , EC 2.4.2.- |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:560788 |
EC number |
2.4.2.30: Pentosyltransferases |
Protein Class |
|
Descriptions
PARP2, also known as ARTD2, is an enzyme that becomes activated by DNA damage, specifically by 5′-phosphorylated DNA ends. It catalyzes poly-ADP-ribosylation, a post-translational modification involved in DNA repair processes. PARP2 plays a crucial role in DNA damage detection and repair, with its activity being essential for maintaining genomic stability and proper cellular function in response to genotoxic stress. In its inactive state, PARP2’s regulatory domain (RD) covers the active site, preventing substrate NAD+ binding. DNA damage recognition leads to RD unfolding and reorganization, enabling the enzyme to access and modify target macromolecules for ADP-ribosylation. The activation of PARP2 by DNA damage induces significant conformational changes in the enzyme, which relieve its autoinhibited state. This allows PARP2 to bind NAD+ and histone PARylation factor 1 (HPF1), altering its residue specificity during DNA repair.
Autoinhibitory domains (AIDs)
Target domain |
787-1013 (ART domain) |
Relief mechanism |
Ligand binding, Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
0 structures for Q5RHR0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| No available structures | |||||
No variants for Q5RHR0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RHR0 | |||||
No associated diseases with Q5RHR0
8 regional properties for Q5RHR0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | BRCT domain | 385 - 466 | IPR001357 |
| domain | Zinc finger, PARP-type | 10 - 92 | IPR001510-1 |
| domain | Zinc finger, PARP-type | 113 - 203 | IPR001510-2 |
| domain | Poly(ADP-ribose) polymerase, regulatory domain | 661 - 793 | IPR004102 |
| domain | WGR domain | 541 - 637 | IPR008893 |
| domain | Poly(ADP-ribose) polymerase, catalytic domain | 787 - 1013 | IPR012317 |
| domain | PARP1-like, PADR1 domain, zinc ribbon fold | 286 - 325 | IPR012982 |
| domain | PARP1-like, PADR1 domain, N-terminal helical subdomain | 225 - 284 | IPR049296 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.2.30 | Pentosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromatin | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| nuclear replication fork | The Y-shaped region of a nuclear replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| site of DNA damage | A region of a chromosome at which DNA damage has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix. |
14 GO annotations of molecular function
| Name | Definition |
|---|---|
| damaged DNA binding | Binding to damaged DNA. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| NAD+ ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+- protein-aspartate ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+-protein ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+-protein-glutamate ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+-protein-histidine ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+-protein-serine ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+-protein-tyrosine ADP-ribosyltransferase activity | Catalysis of the reaction |
| nucleosome binding | Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures. |
| nucleotidyltransferase activity | Catalysis of the transfer of a nucleotidyl group to a reactant. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| zinc ion binding | Binding to a zinc ion (Zn). |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| double-strand break repair | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. |
| innate immune response | Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. |
| negative regulation of innate immune response | Any process that stops, prevents, or reduces the frequency, rate or extent of the innate immune response. |
| negative regulation of transcription by RNA polymerase II | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| protein auto-ADP-ribosylation | The ADP-ribosylation by a protein of one or more of its own amino acid residues, or residues on an identical protein. |
| regulation of circadian sleep/wake cycle, sleep | Any process that modulates the frequency, rate or extent of sleep; a readily reversible state of reduced awareness and metabolic activity that occurs periodically in many animals. |
| replication fork reversal | Replication fork processing that involves the unwinding of blocked forks to form four-stranded structures resembling Holliday junctions, which are subsequently resolved. |
14 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P18493 | PARP1 | Poly [ADP-ribose] polymerase 1 | Bos taurus (Bovine) | SS |
| P26446 | PARP1 | Poly [ADP-ribose] polymerase 1 | Gallus gallus (Chicken) | SS |
| P35875 | Parp | Poly [ADP-ribose] polymerase | Drosophila melanogaster (Fruit fly) | SS |
| Q9UGN5 | PARP2 | Poly [ADP-ribose] polymerase 2 | Homo sapiens (Human) | EV |
| Q9Y6F1 | PARP3 | Protein mono-ADP-ribosyltransferase PARP3 | Homo sapiens (Human) | PR |
| P09874 | PARP1 | Poly [ADP-ribose] polymerase 1 | Homo sapiens (Human) | SS |
| O50017 | PARP2 | Poly [ADP-ribose] polymerase 2 | Zea mays (Maize) | SS |
| O88554 | Parp2 | Poly [ADP-ribose] polymerase 2 | Mus musculus (Mouse) | SS |
| P11103 | Parp1 | Poly [ADP-ribose] polymerase 1 | Mus musculus (Mouse) | SS |
| P27008 | Parp1 | Poly [ADP-ribose] polymerase 1 | Rattus norvegicus (Rat) | SS |
| Q0JMY1 | PARP2-B | Poly [ADP-ribose] polymerase 2-B | Oryza sativa subsp. japonica (Rice) | SS |
| Q5Z8Q9 | PARP2-A | Poly [ADP-ribose] polymerase 2-A | Oryza sativa subsp. japonica (Rice) | SS |
| Q11207 | PARP2 | Poly [ADP-ribose] polymerase 2 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9ZP54 | PARP1 | Poly [ADP-ribose] polymerase 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADSQDDKLY | KAEYAKSGRA | SCKKCKDNIA | KDSLRMAIMV | QSPMFDGKVP | HWHHFSCFWL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RAAVQSPSDI | SGFTDLRWDD | QEKVKTAIES | GGATGGKGGQ | KGAAKGEKTL | NDFAVEYAKS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NRSTCKGCDQ | KIEKDQIRVS | KKTVDPEKPQ | LGLIDRWYHT | GCFVSRREEL | IFKPEYSAAQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKGFAVLRDE | DKEELKKRLP | AVKSEGKRKA | DEVDGGVSKK | QKKEDEKLEQ | NLKDQSQLIW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GIKDKLKKFC | SINDMKELLI | ANSQEVPSGE | SNIVDRLSDC | MAFGSLKPCE | TCKGQLVFKS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DAYYCTGDIS | AWTKCVFKTQ | TPDRKDWVTP | KEFSEIPFLK | KFKFKRQDRV | FPKDAPPAAA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TPSSGSTTSA | ATSVSSASKN | LTEAPADKPL | TGMKLLAVGK | LSKNKDDLKK | FVEDLGGKIT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GTASKAALCI | SSKKEIEKMS | KKMEEVRDAG | VRVVADDFLT | DIKESGKALQ | ELISLHAISP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WGAEVKVEAP | AAAAATKSTG | AHSSKSTGKV | KEEEGGSKSK | KMKLTVKGGA | AVDPDSGLEN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CAHVLEQNGK | IYSATLGLVD | IVRGTNSYYK | LQLLEDDVQK | RYWVFRSWGR | VGTTIGGNKL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DKFYDKNSAM | DNFCGVYEEK | TGNAWASSNF | TKYPNKFYPL | EIDYGQDEEA | VKKLTQSAGA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KSQLEKPVQD | LIRMIFDVES | MKKAMVEFEI | DLQKMPLGKL | SKRQIQSAYS | LLSEVQQAVA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DSSSESLILD | LSNRFYTLIP | HDFGMKKPPL | LSNVDYIQQK | VQMLDNLLDI | EVAYSLLRGG |
| 790 | 800 | 810 | 820 | 830 | 840 |
| VENNEKDPID | INYEKLKTKI | EVVDKSSHEA | QLILQYVKNT | HAATHNTYTL | DVEEIFKIER |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EGEYQRYRPF | KELPNRQLLW | HGSRTTNYAG | ILSQGLRIAP | PEAPVTGYMF | GKGVYFADMV |
| 910 | 920 | 930 | 940 | 950 | 960 |
| SKSANYCHTS | QADPVGLILL | GEVALGNMHE | LKKASHITKL | PKGKHSVKGL | GRSAPDPRAT |
| 970 | 980 | 990 | 1000 | 1010 | |
| VSLNGVDIPL | GKGMNTNIDD | TSLLYNEYIV | YDVSQVNLKY | LLKIRFNYQT | SLW |