P35875
SS
Gene name |
Parp (CG40411) |
Protein name |
Poly [ADP-ribose] polymerase |
Names |
PARP , EC 2.4.2.30 , NAD, + ADP-ribosyltransferase , ADPRT , Poly[ADP-ribose] synthase , Protein ADP-ribosyltransferase Parp , EC 2.4.2.- |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG40411 |
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 |
770-994 (ART domain) |
Relief mechanism |
Ligand binding, Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
0 structures for P35875
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| No available structures | |||||
No variants for P35875
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P35875 | |||||
No associated diseases with P35875
8 regional properties for P35875
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | BRCT domain | 380 - 461 | IPR001357 |
| domain | Zinc finger, PARP-type | 7 - 89 | IPR001510-1 |
| domain | Zinc finger, PARP-type | 111 - 200 | IPR001510-2 |
| domain | Poly(ADP-ribose) polymerase, regulatory domain | 644 - 776 | IPR004102 |
| domain | WGR domain | 525 - 622 | IPR008893 |
| domain | Poly(ADP-ribose) polymerase, catalytic domain | 770 - 994 | IPR012317 |
| domain | PARP1-like, PADR1 domain, zinc ribbon fold | 281 - 321 | IPR012982 |
| domain | PARP1-like, PADR1 domain, N-terminal helical subdomain | 222 - 280 | 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 | |
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| Cajal body | A class of nuclear body, first seen after silver staining by Ramon y Cajal in 1903, enriched in small nuclear ribonucleoproteins, and certain general RNA polymerase II transcription factors; ultrastructurally, they appear as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter; involved in aspects of snRNP biogenesis; the protein coilin serves as a marker for Cajal bodies. Some argue that Cajal bodies are the sites for preassembly of transcriptosomes, unitary particles involved in transcription and processing of RNA. |
| chromosome | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. |
| euchromatin | A dispersed and relatively uncompacted form of chromatin that is in a transcription-competent conformation. |
| histone locus body | A nuclear body associated with the histone gene locus that is thought to contain all of the factors necessary for histone mRNA transcription and pre-mRNA processing. In Drosophila, U7 snRNP is located in the histone locus body rather than the distinct Cajal body. |
| 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. |
| polytene chromosome | A type of chromosome in a polyploid cell, formed when multiple copies of homologous chromosomes are aligned side by side to give a giant chromosome in which distinct chromosome bands are readily visible. |
| polytene chromosome puff | A swelling at a site along the length of a polytene chromosome, thought to be the site of active transcription. |
| 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. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| histone binding | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. |
| 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 ADP-ribosyltransferase activity | Catalysis of the reaction |
| NAD+-protein-serine ADP-ribosyltransferase activity | Catalysis of the reaction |
| nucleotidyltransferase activity | Catalysis of the transfer of a nucleotidyl group to a reactant. |
| zinc ion binding | Binding to a zinc ion (Zn). |
15 GO annotations of biological process
| Name | Definition |
|---|---|
| Cajal body organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Cajal bodies, nuclear bodies that appear ultrastructurally as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter and are enriched in ribonucleoproteins, and certain general RNA polymerase II transcription factors. |
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| DNA damage response | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
| dorsal/ventral axis specification, ovarian follicular epithelium | Polarization of the ovarian follicle cells along the dorsal/ventral axis. An example of this process is found in Drosophila melanogaster. |
| double-strand break repair | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. |
| heat shock-mediated polytene chromosome puffing | The decondensing (loosening) and swelling of the chromosomal sites of heat shock genes on polytene chromosomes in response to a heat shock stimulus. |
| innate immune response | Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. |
| maintenance of protein location in nucleus | Any process in which a protein is maintained in the nucleus and prevented from moving elsewhere. These include sequestration within the nucleus, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the nucleus. |
| nucleolus organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleolus. |
| polytene chromosome puffing | The decondensing (loosening) and swelling of the chromosomal sites of target genes on polytene chromosomes following response to a stimulus, to facilitate sudden bursts of transcriptional activity in response to transient environmental signals. |
| positive regulation of antibacterial peptide biosynthetic process | Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis. |
| positive regulation of peptidoglycan recognition protein signaling pathway | Any process that increases the rate, frequency, or extent of the peptidoglycan recognition protein signaling pathway. |
| positive regulation of protein localization to nucleus | Any process that activates or increases the frequency, rate or extent of protein localization to nucleus. |
| regulation of chromatin organization | Any process that modulates the frequency, rate or extent of chromatin organization. |
| regulation of RNA splicing | Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA. |
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 |
| 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 |
| Q5RHR0 | parp1 | Poly [ADP-ribose] polymerase 1 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDIELPYLAE | YARTGRATCK | GCKSTISKDT | LRIAVMVQSA | FHDAKVPNWF | HKTCFFKNQR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PSSVGDIQNI | GNLRFADQKE | LTDLVENIQE | VISAQLGKKR | SKAFNLALKD | FGIEYAKSSR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| STCRGCEQKI | NKDLVRLRKT | VYDTEVGMKY | GGQPLWHHLE | CFAQLRSELG | WFASGEDMPG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FQSLADDDQA | KVKNAIPPIK | SEELPDTKRA | KMELSDTNEE | GEKKQRLKDQ | NDAYFRFRDD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IKNKMKKKDI | DILLKFNNQQ | PVTGDTEKLF | DQTADLLTFG | AIESCSECNS | CQFIVNKSGY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ICNGNHSEWT | KCNKLLKEPT | RSACIVPKEL | KALYNFLNTV | KEIPSTRIFN | NFPPNKSTFS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RSLLKTNKNN | DVLVRPTIPR | ISPPLYNLKF | SIIGLKNQHK | ELRKRIENLG | GKFEVKISEN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TIAIISTELE | IQKKSTRMKF | AEELGIHIVP | IEFLDFVEAD | TEGAIKYINS | TCICSWGTDP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KSRIPKETTK | SLNSNSIYTK | SMPVSRTFKV | KDGLAVDPDS | GLEDIAHVYV | DSNNKYSVVL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GLTDIQRNKN | SYYKVQLLKA | DKKEKYWIFR | SWGRIGTNIG | NSKLEEFDTS | ESAKRNFKEI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YADKTGNEYE | QRDNFVKRTG | RMYPIEIQYD | DDQKLVKHES | HFFTSKLEIS | VQNLIKLIFD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IDSMNKTLME | FHIDMDKMPL | GKLSAHQIQS | AYRVVKEIYN | VLECGSNTAK | LIDATNRFYT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LIPHNFGVQL | PTLIETHQQI | EDLRQMLDSL | AEIEVAYSII | KSEDVSDACN | PLDNHYAQIK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TQLVALDKNS | EEFSILSQYV | KNTHASTHKS | YDLKIVDVFK | VSRQGEARRF | KPFKKLHNRK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LLWHGSRLTN | FVGILSHGLR | IAPPEAPPTG | YMFGKGIYFA | DMVSKSANYC | CTSQQNSTGL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| MLLSEVALGD | MMECTSAKYI | NKLSNNKHSC | FGRGRTMPDP | TKSYIRSDGV | EIPYGETITD |
| 970 | 980 | 990 | |||
| EHLKSSLLYN | EYIVYDVAQV | NIQYLFRMEF | KYSY |