Q0JMY1

SS
Gene name
PARP2-B (Os01g0351100, LOC_Os01g24920, B1051E10.53, P0463A02.23)
Protein name
Poly [ADP-ribose] polymerase 2-B
Names
PARP-2-B , EC 2.4.2.30 , NAD, + ADP-ribosyltransferase 2-B , ADPRT-2-B , Poly[ADP-ribose] synthase 2-B , 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)

250-384 (RD domain) SS

Target domain

378-605 (ART domain)

Relief mechanism

Ligand binding, Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for Q0JMY1

Entry ID Method Resolution Chain Position Source
No available structures

No variants for Q0JMY1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0JMY1

No associated diseases with Q0JMY1

13 regional properties for Q0JMY1

Type Name Position InterPro Accession
domain PB1 domain 15 - 98 IPR000270
domain Protein kinase domain 252 - 518 IPR000719
domain AGC-kinase, C-terminal 519 - 590 IPR000961
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 130 - 182 IPR002219
active_site Serine/threonine-protein kinase, active site 372 - 384 IPR008271
binding_site Protein kinase, ATP binding site 258 - 285 IPR017441
domain Protein kinase, C-terminal 540 - 580 IPR017892
domain Diacylglycerol/phorbol-ester binding 128 - 142 IPR020454-1
domain Diacylglycerol/phorbol-ester binding 144 - 153 IPR020454-2
domain Diacylglycerol/phorbol-ester binding 157 - 168 IPR020454-3
domain Diacylglycerol/phorbol-ester binding 169 - 181 IPR020454-4
domain Protein kinase C, PB1 domain 16 - 98 IPR034877
domain PB1-like domain 15 - 98 IPR053793

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.

3 GO annotations of molecular function

Name Definition
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
Q5Z8Q9 PARP2-A Poly [ADP-ribose] polymerase 2-A 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
MQMIGGEMWT AAGRRLHQQR DLHAILRTAH RRCCTRPIGG GLDAPAAPPG DLRTLSGVGM
70 80 90 100 110 120
LIHQFKALLA PKKIYPWRSS HLQSLEVRRL HTAPSNAAAA AAVTDGGDQD KTKSAKDDDG
130 140 150 160 170 180
DDKVQCKKEK IVTATKKGAA VLDQYIPDNI KTAYHVLQVG DEIYDATMNQ TNVGGNNNKF
190 200 210 220 230 240
YIIQALESDA GGNFMVYSRW GRVGTRDIHW SYRKGSHCYA HKYTWLEMDY GEADKETNKK
250 260 270 280 290 300
TSSITNQLEE TKLETRTASF ISLICDISMM KQQMVEIGYN ADKLPLGKLS KSTILKGYDV
310 320 330 340 350 360
LKRISNVISG ADTDRTQLEQ LTGEFYSVIP HDFGFKKMSE FIIDTPQKLK AKLEMVEALS
370 380 390 400 410 420
EIEIAIKLLE DDSSDQDHPL YARYKQFCCD FTPLEVDSEE YSMIKTYLTN THGKTHTGYT
430 440 450 460 470 480
VDIVQIFKVS RLGEMERFQK FASAGNRMLL WHGSRLTNWA GILSQGLRIA PPEAPISGFM
490 500 510 520 530 540
FGKGVYFADM FSKSANYCCA SEACKSGVML LCEVALGEMN ELLYGDFGAD NLPNGKLSTK
550 560 570 580 590 600
GVGQTEPNIA ESKITDDGMV IPLGKPEKVP SRRGSLMYNE YIVYNVDQIR MRYILNVNFN
FKRWG