Q5Z8Q9

SS
Gene name
PARP2-A (Os01g0351200, LOC_Os01g24940, B1051E10.55, P0463A02.25)
Protein name
Poly [ADP-ribose] polymerase 2-A
Names
PARP-2-A , EC 2.4.2.30 , NAD, + ADP-ribosyltransferase 2-A , ADPRT-2-A , Poly[ADP-ribose] synthase 2-A , Protein ADP-ribosyltransferase PARP2 , EC 2.4.2.-
Species
Oryza sativa subsp. japonica (Rice)
KEGG Pathway
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)

308-440 (RD domain) SS

Target domain

434-660 (ART domain)

Relief mechanism

Ligand binding, Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for Q5Z8Q9

Entry ID Method Resolution Chain Position Source
No available structures

No variants for Q5Z8Q9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5Z8Q9

No associated diseases with Q5Z8Q9

11 regional properties for Q5Z8Q9

Type Name Position InterPro Accession
domain Protein kinase domain 626 - 887 IPR000719
domain Ephrin receptor ligand binding domain 29 - 210 IPR001090
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 626 - 883 IPR001245
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 186 - 206 IPR001426-1
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 247 - 267 IPR001426-2
domain Sterile alpha motif domain 907 - 974 IPR001660
domain Fibronectin type III 328 - 533 IPR003961
active_site Tyrosine-protein kinase, active site 747 - 759 IPR008266
binding_site Protein kinase, ATP binding site 632 - 658 IPR017441
domain Tyrosine-protein kinase, catalytic domain 626 - 883 IPR020635
domain Ephrin receptor, transmembrane domain 548 - 622 IPR027936

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.

4 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+ 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.

1 GO annotations of biological process

Name Definition
double-strand break repair The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.

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
P11103 Parp1 Poly [ADP-ribose] polymerase 1 Mus musculus (Mouse) SS
O88554 Parp2 Poly [ADP-ribose] polymerase 2 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
Q9ZP54 PARP1 Poly [ADP-ribose] polymerase 1 Arabidopsis thaliana (Mouse-ear cress) 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
MSARLRVEEL RAELQRRGLD ASGNKPVLVR RLDAAIRKEE EEEAAVSAAA KEEADAGGVV
70 80 90 100 110 120
DGEGNGEDKR KRKRRGDGED VDNSESDAAK LEGMSYRELQ ALAKSRGLAA NGSKKEVIER
130 140 150 160 170 180
LLCAPSDTDG GVQDKKKIAK GFADGDDRVE ECRKEKIVTA TRKGAAVLDQ HIPDHIKMTY
190 200 210 220 230 240
HVLQVWFLLK GDEIYDATMN QTNVGDNNNK FYIIQALESD AGGSFMVYNR WGRVGARGQD
250 260 270 280 290 300
KLHGPFSSRE QAIYEFEGKF HGKTNNHWSD RKSFECYARK YTWLEMDYGE ADRETNKKVS
310 320 330 340 350 360
PSTDQIKETK LETRIASFIS LICNISMMKQ QMVEIGYNSD KLPLGKLSKS TIFKGYDVLK
370 380 390 400 410 420
RISNVISRAD RRQLEQLTGE FYTVIPHDFG FKKMREFIID TPQKLKAKLE MVEALGEIEI
430 440 450 460 470 480
ATKLLEDDST DQDDPLYARY KQLSCDFTPL EVGSEEYSMI KTYLANTHGK THTSYTVDVV
490 500 510 520 530 540
QIFKVSRHGE MERFQKFATA GNRMLLWHGS RLTNWAGILS QGLRIAPPEA PVTGYMFGKG
550 560 570 580 590 600
VYFADMFSKS ANYCYASEAC RSGVLLLCEV ALGEMNELLN ADYDANNLPK GKLSTKGVGQ
610 620 630 640 650
TEPNTAESKI TDDGVVVPLG KPKAEPSKRG SLLYNEFIVY NVDQIRMRYV LHVSFNFKKR