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

412-637 (ART domain)

Relief mechanism

Ligand binding, Others

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for Q11207

Entry ID Method Resolution Chain Position Source
No available structures

67 variants for Q11207

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_4_1050114_A_G 4 K>R No 1000Genomes
ENSVATH00454935 12 L>S No 1000Genomes
ENSVATH02622055 13 K>Q No 1000Genomes
ENSVATH02622056 22 T>A No 1000Genomes
ENSVATH00454938 24 V>I No 1000Genomes
tmp_4_1050180_C_T 26 A>V No 1000Genomes
ENSVATH02622058 27 V>A No 1000Genomes
ENSVATH13882229 51 R>I No 1000Genomes
ENSVATH02622062 52 N>D No 1000Genomes
tmp_4_1050341_C_A 54 S>Y No 1000Genomes
ENSVATH02622063 55 N>D No 1000Genomes
ENSVATH02622065 58 Y>* No 1000Genomes
ENSVATH02622064 58 Y>D No 1000Genomes
ENSVATH10534286 66 I>S No 1000Genomes
ENSVATH00454940 82 I>S No 1000Genomes
tmp_4_1050454_A_G 92 K>E No 1000Genomes
ENSVATH06424120 98 R>K No 1000Genomes
ENSVATH06424120 98 R>T No 1000Genomes
ENSVATH06424121 108 N>K No 1000Genomes
ENSVATH02622067 111 V>A No 1000Genomes
tmp_4_1050613_G_A 118 D>N No 1000Genomes
ENSVATH02622075 119 E>G No 1000Genomes
ENSVATH02622076 124 N>D No 1000Genomes
ENSVATH00454941 124 N>S No 1000Genomes
ENSVATH02622077 130 E>D No 1000Genomes
ENSVATH02622088 168 V>I No 1000Genomes
tmp_4_1050879_A_G 176 T>A No 1000Genomes
ENSVATH02622090 187 V>I No 1000Genomes
ENSVATH02622095 199 Y>F No 1000Genomes
tmp_4_1051148_G_T 205 W>L No 1000Genomes
ENSVATH02622096 221 D>N No 1000Genomes
ENSVATH06424130 225 R>H No 1000Genomes
tmp_4_1051252_A_T 240 N>Y No 1000Genomes
tmp_4_1051282_C_T 250 P>S No 1000Genomes
tmp_4_1051557_C_T 276 P>L No 1000Genomes
tmp_4_1051604_C_G 292 R>G No 1000Genomes
tmp_4_1051610_G_A 294 A>T No 1000Genomes
ENSVATH06424139 295 K>M No 1000Genomes
tmp_4_1051625_C_T 299 L>F No 1000Genomes
ENSVATH13882232 320 L>V No 1000Genomes
ENSVATH06424143 323 G>S No 1000Genomes
tmp_4_1051921_G_A 326 S>N No 1000Genomes
ENSVATH00454949 328 S>P No 1000Genomes
tmp_4_1051938_A_G 332 K>E No 1000Genomes
ENSVATH06424148 339 R>G No 1000Genomes
ENSVATH02622136 347 Y>F No 1000Genomes
ENSVATH10534373 361 T>S No 1000Genomes
ENSVATH00454952 376 V>L No 1000Genomes
tmp_4_1052557_T_G 409 L>V No 1000Genomes
tmp_4_1052689_A_G 422 N>D No 1000Genomes
ENSVATH06424174 431 D>N No 1000Genomes
ENSVATH06424178 469 A>T No 1000Genomes
tmp_4_1052942_G_C 470 D>H No 1000Genomes
ENSVATH10534442 474 Q>L No 1000Genomes
tmp_4_1053233_G_A 502 R>Q No 1000Genomes
tmp_4_1053242_C_T 505 P>L No 1000Genomes
tmp_4_1053329_C_T 534 A>V No 1000Genomes
ENSVATH02622175 535 N>S No 1000Genomes
tmp_4_1053334_A_C 536 T>P No 1000Genomes
tmp_4_1053337_G_T 537 G>C No 1000Genomes
tmp_4_1053340_G_A 538 A>T No 1000Genomes
ENSVATH06424187 546 C>S No 1000Genomes
ENSVATH13882285 568 P>L No 1000Genomes
tmp_4_1053743_G_C 595 V>L No 1000Genomes
ENSVATH06424193 614 E>G No 1000Genomes
tmp_4_1053903_T_A,C 619 N>K No 1000Genomes
ENSVATH00454964 625 M>T No 1000Genomes

No associated diseases with Q11207

3 regional properties for Q11207

Type Name Position InterPro Accession
domain Pyruvate kinase, barrel 19 - 345 IPR015793
domain Pyruvate kinase, C-terminal 380 - 497 IPR015795
active_site Pyruvate kinase, active site 235 - 247 IPR018209

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

2 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.
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.

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.

3 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.
double-strand break repair via nonhomologous end joining The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
protein poly-ADP-ribosylation The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain.

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
Q9UGN5 PARP2 Poly [ADP-ribose] polymerase 2 Homo sapiens (Human) EV
Q9Y6F1 PARP3 Protein mono-ADP-ribosyltransferase PARP3 Homo sapiens (Human) PR
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
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
Q5RHR0 parp1 Poly [ADP-ribose] polymerase 1 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MANKLKVDEL RLKLAERGLS TTGVKAVLVE RLEEAIAEDT KKEESKSKRK RNSSNDTYES
70 80 90 100 110 120
NKLIAIGEFR GMIVKELREE AIKRGLDTTG TKKDLLERLC NDANNVSNAP VKSSNGTDEA
130 140 150 160 170 180
EDDNNGFEEE KKEEKIVTAT KKGAAVLDQW IPDEIKSQYH VLQRGDDVYD AILNQTNVRD
190 200 210 220 230 240
NNNKFFVLQV LESDSKKTYM VYTRWGRVGV KGQSKLDGPY DSWDRAIEIF TNKFNDKTKN
250 260 270 280 290 300
YWSDRKEFIP HPKSYTWLEM DYGKEENDSP VNNDIPSSSS EVKPEQSKLD TRVAKFISLI
310 320 330 340 350 360
CNVSMMAQHM MEIGYNANKL PLGKISKSTI SKGYEVLKRI SEVIDRYDRT RLEELSGEFY
370 380 390 400 410 420
TVIPHDFGFK KMSQFVIDTP QKLKQKIEMV EALGEIELAT KLLSVDPGLQ DDPLYYHYQQ
430 440 450 460 470 480
LNCGLTPVGN DSEEFSMVAN YMENTHAKTH SGYTVEIAQL FRASRAVEAD RFQQFSSSKN
490 500 510 520 530 540
RMLLWHGSRL TNWAGILSQG LRIAPPEAPV TGYMFGKGVY FADMFSKSAN YCYANTGAND
550 560 570 580 590 600
GVLLLCEVAL GDMNELLYSD YNADNLPPGK LSTKGVGKTA PNPSEAQTLE DGVVVPLGKP
610 620 630
VERSCSKGML LYNEYIVYNV EQIKMRYVIQ VKFNYKH