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

759-983 (ART domain)

Relief mechanism

Ligand binding, Others

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for Q9ZP54

Entry ID Method Resolution Chain Position Source
No available structures

71 variants for Q9ZP54

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH01933363 2 A>T No 1000Genomes
tmp_2_13359564_A_C 5 H>Q No 1000Genomes
tmp_2_13359516_T_G 21 K>N No 1000Genomes
ENSVATH05637827 31 N>K No 1000Genomes
tmp_2_13358651_G_T 60 T>K No 1000Genomes
tmp_2_13358636_G_A 65 S>L No 1000Genomes
tmp_2_13358491_C_A 87 V>F No 1000Genomes
ENSVATH05637798 93 S>N No 1000Genomes
ENSVATH05637797 98 S>G No 1000Genomes
ENSVATH05637796 100 G>S No 1000Genomes
ENSVATH14575303 101 T>I No 1000Genomes
tmp_2_13358433_G_A 106 T>I No 1000Genomes
ENSVATH00255729 111 K>E No 1000Genomes
ENSVATH00255729 111 K>Q No 1000Genomes
ENSVATH13494265 131 E>D No 1000Genomes
tmp_2_13358199_A_T 152 L>M No 1000Genomes
ENSVATH05637786 163 M>V No 1000Genomes
ENSVATH05637785 177 S>I No 1000Genomes
ENSVATH05637784 195 P>R No 1000Genomes
tmp_2_13358061_T_C 198 K>E No 1000Genomes
ENSVATH05637783 199 T>I No 1000Genomes
ENSVATH05637778 202 A>T No 1000Genomes
tmp_2_13357922_G_A 207 T>I No 1000Genomes
tmp_2_13357888_A_T 218 D>E No 1000Genomes
ENSVATH05637776 220 V>G No 1000Genomes
ENSVATH13494236 223 E>G No 1000Genomes
ENSVATH05637775 228 A>T No 1000Genomes
ENSVATH05637774 230 S>T No 1000Genomes
ENSVATH05637772 247 K>R No 1000Genomes
ENSVATH05637770 249 M>L No 1000Genomes
tmp_2_13357790_G_T 251 A>D No 1000Genomes
tmp_2_13357711_T_C,G 277 E>D No 1000Genomes
tmp_2_13357704_C_T 280 E>K No 1000Genomes
ENSVATH13494235 313 L>F No 1000Genomes
tmp_2_13357422_C_T 324 G>E No 1000Genomes
ENSVATH05637759 343 K>I No 1000Genomes
ENSVATH13494211 374 R>H No 1000Genomes
ENSVATH05637750 377 L>S No 1000Genomes
tmp_2_13356940_G_A 428 H>Y No 1000Genomes
ENSVATH05637739 444 T>I No 1000Genomes
ENSVATH05637734 472 K>R No 1000Genomes
ENSVATH13494174 479 F>L No 1000Genomes
tmp_2_13356607_T_G 481 K>Q No 1000Genomes
tmp_2_13356601_T_C 483 K>E No 1000Genomes
ENSVATH00255727 507 G>D No 1000Genomes
tmp_2_13356477_G_A 524 T>I No 1000Genomes
ENSVATH05637731 551 D>E No 1000Genomes
ENSVATH01933353 554 V>I No 1000Genomes
tmp_2_13356320_C_G,A 576 K>N No 1000Genomes
tmp_2_13356297_T_C 584 K>R No 1000Genomes
ENSVATH14575300 589 E>K No 1000Genomes
tmp_2_13356071_C_G,T 631 Q>H No 1000Genomes
tmp_2_13356058_G_T 636 L>I No 1000Genomes
ENSVATH05637720 639 S>P No 1000Genomes
ENSVATH05637713 686 E>K No 1000Genomes
tmp_2_13355652_C_G 709 S>T No 1000Genomes
ENSVATH01933351 718 S>F No 1000Genomes
tmp_2_13355594_A_T 728 D>E No 1000Genomes
ENSVATH05637711 729 D>N No 1000Genomes
ENSVATH05637704 768 H>N No 1000Genomes
ENSVATH05637703 774 L>V No 1000Genomes
tmp_2_13355340_C_T 782 R>Q No 1000Genomes
ENSVATH05637702 790 T>R No 1000Genomes
tmp_2_13355130_T_G 824 K>N No 1000Genomes
tmp_2_13355129_G_T 825 L>I No 1000Genomes
tmp_2_13354730_C_A 876 A>S No 1000Genomes
ENSVATH13494142 899 E>G No 1000Genomes
ENSVATH05637668 912 P>L No 1000Genomes
ENSVATH05637667 915 G>E No 1000Genomes
tmp_2_13354440_A_C 929 D>E No 1000Genomes
ENSVATH05637654 981 H>Q No 1000Genomes

No associated diseases with Q9ZP54

2 regional properties for Q9ZP54

Type Name Position InterPro Accession
domain Ubiquitin-like domain 16 - 93 IPR000626
domain Rad60/SUMO-like domain 18 - 86 IPR022617

Functions

Description
EC Number 2.4.2.30 Pentosyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

6 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).
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
nucleotidyltransferase activity Catalysis of the transfer of a nucleotidyl group to a reactant.
zinc ion binding Binding to a zinc ion (Zn).

6 GO annotations of biological process

Name Definition
DNA ADP-ribosylation The covalent attachment of an ADP-ribosyl group to a residue in double-stranded DNA.
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.
protein poly-ADP-ribosylation The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain.
response to abscisic acid Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an abscisic acid stimulus.
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

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
P09874 PARP1 Poly [ADP-ribose] polymerase 1 Homo sapiens (Human) SS
Q9Y6F1 PARP3 Protein mono-ADP-ribosyltransferase PARP3 Homo sapiens (Human) PR
Q9UGN5 PARP2 Poly [ADP-ribose] polymerase 2 Homo sapiens (Human) EV
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
Q5RHR0 parp1 Poly [ADP-ribose] polymerase 1 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MASPHKPWRA EYAKSSRSSC KTCKSVINKE NFRLGKLVQS THFDGIMPMW NHASCILKKT
70 80 90 100 110 120
KQIKSVDDVE GIESLRWEDQ QKIRKYVESG AGSNTSTSTG TSTSSTANNA KLEYGIEVSQ
130 140 150 160 170 180
TSRAGCRKCS EKILKGEVRI FSKPEGPGNK GLMWHHAKCF LEMSSSTELE SLSGWRSIPD
190 200 210 220 230 240
SDQEALLPLV KKALPAAKTE TAEARQTNSR AGTKRKNDSV DNEKSKLAKS SFDMSTSGAL
250 260 270 280 290 300
QPCSKEKEME AQTKELWDLK DDLKKYVTSA ELREMLEVNE QSTRGSELDL RDKCADGMMF
310 320 330 340 350 360
GPLALCPMCS GHLSFSGGLY RCHGYISEWS KCSHSTLDPD RIKGKWKIPD ETENQFLLKW
370 380 390 400 410 420
NKSQKSVKPK RILRPVLSGE TSQGQGSKDA TDSSRSERLA DLKVSIAGNT KERQPWKKRI
430 440 450 460 470 480
EEAGAEFHAN VKKGTSCLVV CGLTDIRDAE MRKARRMKVA IVREDYLVDC FKKQRKLPFD
490 500 510 520 530 540
KYKIEDTSES LVTVKVKGRS AVHEASGLQE HCHILEDGNS IYNTTLSMSD LSTGINSYYI
550 560 570 580 590 600
LQIIQEDKGS DCYVFRKWGR VGNEKIGGNK VEEMSKSDAV HEFKRLFLEK TGNTWESWEQ
610 620 630 640 650 660
KTNFQKQPGK FLPLDIDYGV NKQVAKKEPF QTSSNLAPSL IELMKMLFDV ETYRSAMMEF
670 680 690 700 710 720
EINMSEMPLG KLSKHNIQKG FEALTEIQRL LTESDPQPTM KESLLVDASN RFFTMIPSIH
730 740 750 760 770 780
PHIIRDEDDF KSKVKMLEAL QDIEIASRIV GFDVDSTESL DDKYKKLHCD ISPLPHDSED
790 800 810 820 830 840
YRLIEKYLNT THAPTHTEWS LELEEVFALE REGEFDKYAP HREKLGNKML LWHGSRLTNF
850 860 870 880 890 900
VGILNQGLRI APPEAPATGY MFGKGIYFAD LVSKSAQYCY TCKKNPVGLM LLSEVALGEI
910 920 930 940 950 960
HELTKAKYMD KPPRGKHSTK GLGKKVPQDS EFAKWRGDVT VPCGKPVSSK VKASELMYNE
970 980
YIVYDTAQVK LQFLLKVRFK HKR