##gff-version 3 P09874 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|Ref.12,ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P09874 UniProtKB Chain 2 1014 . . . ID=PRO_0000211320;Note=Poly [ADP-ribose] polymerase 1 P09874 UniProtKB Chain 2 214 . . . ID=PRO_0000456361;Note=Poly [ADP-ribose] polymerase 1%2C processed N-terminus;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7596430;Dbxref=PMID:7596430 P09874 UniProtKB Chain 215 1014 . . . ID=PRO_0000456362;Note=Poly [ADP-ribose] polymerase 1%2C processed C-terminus;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7596430;Dbxref=PMID:7596430 P09874 UniProtKB Domain 225 359 . . . Note=PADR1 zinc-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01351 P09874 UniProtKB Domain 385 476 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 P09874 UniProtKB Domain 542 638 . . . Note=WGR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01321 P09874 UniProtKB Domain 662 779 . . . Note=PARP alpha-helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00398 P09874 UniProtKB Domain 788 1014 . . . Note=PARP catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00397 P09874 UniProtKB Zinc finger 9 93 . . . Note=PARP-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00264 P09874 UniProtKB Zinc finger 113 203 . . . Note=PARP-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00264 P09874 UniProtKB Region 198 233 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09874 UniProtKB Region 290 332 . . . Note=Zinc ribbon;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01351 P09874 UniProtKB Region 361 385 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09874 UniProtKB Region 373 524 . . . Note=Automodification domain;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:19764761;Dbxref=PMID:19764761 P09874 UniProtKB Motif 207 209 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1505517;Dbxref=PMID:1505517 P09874 UniProtKB Motif 221 226 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1505517;Dbxref=PMID:1505517 P09874 UniProtKB Compositional bias 366 385 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09874 UniProtKB Active site 988 988 . . . Note=For poly [ADP-ribose] polymerase activity;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:32028527,ECO:0000305|PubMed:7852410,ECO:0000305|PubMed:9315851;Dbxref=PMID:32028527,PMID:7852410,PMID:9315851 P09874 UniProtKB Binding site 21 21 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3OD8,ECO:0007744|PDB:3ODA,ECO:0007744|PDB:4AV1,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:21233213,PMID:22582261,PMID:22683995 P09874 UniProtKB Binding site 24 24 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3OD8,ECO:0007744|PDB:3ODA,ECO:0007744|PDB:4AV1,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:21233213,PMID:22582261,PMID:22683995 P09874 UniProtKB Binding site 53 53 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3OD8,ECO:0007744|PDB:3ODA,ECO:0007744|PDB:4AV1,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:21233213,PMID:22582261,PMID:22683995 P09874 UniProtKB Binding site 56 56 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3OD8,ECO:0007744|PDB:3ODA,ECO:0007744|PDB:4AV1,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:21233213,PMID:22582261,PMID:22683995 P09874 UniProtKB Binding site 125 125 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3ODC,ECO:0007744|PDB:3ODE,ECO:0007744|PDB:4AV1;Dbxref=PMID:21233213,PMID:22683995 P09874 UniProtKB Binding site 128 128 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3ODC,ECO:0007744|PDB:3ODE,ECO:0007744|PDB:4AV1;Dbxref=PMID:21233213,PMID:22683995 P09874 UniProtKB Binding site 159 159 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3ODC,ECO:0007744|PDB:3ODE,ECO:0007744|PDB:4AV1;Dbxref=PMID:21233213,PMID:22683995 P09874 UniProtKB Binding site 162 162 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00264,ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22683995,ECO:0007744|PDB:3ODC,ECO:0007744|PDB:3ODE,ECO:0007744|PDB:4AV1;Dbxref=PMID:21233213,PMID:22683995 P09874 UniProtKB Binding site 295 295 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU01351,ECO:0000269|PubMed:18055453,ECO:0000269|PubMed:22582261,ECO:0007744|PDB:2RIQ,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:18055453,PMID:22582261 P09874 UniProtKB Binding site 298 298 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU01351,ECO:0000269|PubMed:18055453,ECO:0000269|PubMed:22582261,ECO:0007744|PDB:2RIQ,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:18055453,PMID:22582261 P09874 UniProtKB Binding site 311 311 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU01351,ECO:0000269|PubMed:18055453,ECO:0000269|PubMed:22582261,ECO:0007744|PDB:2RIQ,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:18055453,PMID:22582261 P09874 UniProtKB Binding site 321 321 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU01351,ECO:0000269|PubMed:18055453,ECO:0000269|PubMed:22582261,ECO:0007744|PDB:2RIQ,ECO:0007744|PDB:4DQY,ECO:0007744|PDB:4OPX,ECO:0007744|PDB:4OQA,ECO:0007744|PDB:4OQB;Dbxref=PMID:18055453,PMID:22582261 P09874 UniProtKB Binding site 862 864 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGN5 P09874 UniProtKB Binding site 871 871 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGN5 P09874 UniProtKB Binding site 878 878 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGN5 P09874 UniProtKB Binding site 904 904 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGN5 P09874 UniProtKB Site 214 215 . . . Note=Cleavage%3B by caspase-3 and caspase-7;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10497198,ECO:0000269|PubMed:22464733,ECO:0000269|PubMed:7596430;Dbxref=PMID:10497198,PMID:22464733,PMID:7596430 P09874 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|Ref.12,ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P09874 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 P09874 UniProtKB Modified residue 97 97 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09874 UniProtKB Modified residue 105 105 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09874 UniProtKB Modified residue 131 131 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09874 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P09874 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:23186163;Dbxref=PMID:17525332,PMID:23186163 P09874 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P09874 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P09874 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P09874 UniProtKB Modified residue 364 364 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P09874 UniProtKB Modified residue 368 368 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 P09874 UniProtKB Modified residue 387 387 . . . Note=PolyADP-ribosyl aspartic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19764761;Dbxref=PMID:19764761 P09874 UniProtKB Modified residue 407 407 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 413 413 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 435 435 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 437 437 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 444 444 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 445 445 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 448 448 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 456 456 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 471 471 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 484 484 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 488 488 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19764761;Dbxref=PMID:19764761 P09874 UniProtKB Modified residue 491 491 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19764761;Dbxref=PMID:19764761 P09874 UniProtKB Modified residue 499 499 . . . Note=ADP-ribosylserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28190768,ECO:0000269|PubMed:29954836,ECO:0000269|PubMed:33186521,ECO:0000269|PubMed:34210965,ECO:0000269|PubMed:34625544;Dbxref=PMID:28190768,PMID:29954836,PMID:33186521,PMID:34210965,PMID:34625544 P09874 UniProtKB Modified residue 504 504 . . . Note=ADP-ribosylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29954836;Dbxref=PMID:29954836 P09874 UniProtKB Modified residue 507 507 . . . Note=ADP-ribosylserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28190768,ECO:0000269|PubMed:29954836,ECO:0000269|PubMed:34210965,ECO:0000269|PubMed:34625544;Dbxref=PMID:28190768,PMID:29954836,PMID:34210965,PMID:34625544 P09874 UniProtKB Modified residue 513 513 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 514 514 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 519 519 . . . Note=ADP-ribosylserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28190768,ECO:0000269|PubMed:29954836,ECO:0000269|PubMed:34210965,ECO:0000269|PubMed:34625544;Dbxref=PMID:28190768,PMID:29954836,PMID:34210965,PMID:34625544 P09874 UniProtKB Modified residue 520 520 . . . Note=PolyADP-ribosyl glutamic acid;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09874 UniProtKB Modified residue 521 521 . . . Note=N6-(ADP-ribosyl)lysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21680843,ECO:0000269|PubMed:27568560;Dbxref=PMID:21680843,PMID:27568560 P09874 UniProtKB Modified residue 594 594 . . . Note=Phosphothreonine%3B by PRKDC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35460603;Dbxref=PMID:35460603 P09874 UniProtKB Modified residue 600 600 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09874 UniProtKB Modified residue 621 621 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09874 UniProtKB Modified residue 782 782 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 P09874 UniProtKB Modified residue 786 786 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P09874 UniProtKB Cross-link 192 192 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P09874 UniProtKB Cross-link 203 203 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211 P09874 UniProtKB Cross-link 203 203 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25772364,PMID:28112733 P09874 UniProtKB Cross-link 249 249 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P09874 UniProtKB Cross-link 467 467 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25772364,PMID:28112733 P09874 UniProtKB Cross-link 486 486 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211 P09874 UniProtKB Cross-link 486 486 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25114211,ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25114211,PMID:25218447,PMID:25772364,PMID:28112733 P09874 UniProtKB Cross-link 512 512 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:25755297,PMID:25772364,PMID:28112733 P09874 UniProtKB Cross-link 528 528 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P09874 UniProtKB Cross-link 748 748 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211 P09874 UniProtKB Cross-link 748 748 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733 P09874 UniProtKB Natural variant 54 54 . . . ID=VAR_050460;Note=F->L;Dbxref=dbSNP:rs3738708 P09874 UniProtKB Natural variant 188 188 . . . ID=VAR_014714;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5;Dbxref=dbSNP:rs1805409 P09874 UniProtKB Natural variant 334 334 . . . ID=VAR_019171;Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5;Dbxref=dbSNP:rs3219057 P09874 UniProtKB Natural variant 377 377 . . . ID=VAR_050461;Note=P->S;Dbxref=dbSNP:rs2230484 P09874 UniProtKB Natural variant 383 383 . . . ID=VAR_019172;Note=S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5;Dbxref=dbSNP:rs3219062 P09874 UniProtKB Natural variant 488 488 . . . ID=VAR_035852;Note=In a breast cancer sample%3B somatic mutation. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 P09874 UniProtKB Natural variant 762 762 . . . ID=VAR_014715;Note=V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|Ref.5;Dbxref=dbSNP:rs1136410,PMID:15489334 P09874 UniProtKB Natural variant 940 940 . . . ID=VAR_019173;Note=K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2891139,ECO:0000269|Ref.5;Dbxref=dbSNP:rs3219145,PMID:2891139 P09874 UniProtKB Mutagenesis 18 18 . . . Note=Abolished DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 25 25 . . . Note=Does not affect translocation into the cytosol. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35460603;Dbxref=PMID:35460603 P09874 UniProtKB Mutagenesis 34 34 . . . Note=Abolished DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 34 34 . . . Note=Abolished binding to DNA strand breaks. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683995;Dbxref=PMID:22683995 P09874 UniProtKB Mutagenesis 40 40 . . . Note=Does not affect DNA-binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 41 41 . . . Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 42 42 . . . Note=No effect. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 43 43 . . . Note=No effect. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 43 43 . . . Note=Strongly decreased homodimerization. M->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683995;Dbxref=PMID:22683995 P09874 UniProtKB Mutagenesis 44 48 . . . Note=Abolished DNA-binding. FDGKV->ADGKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 44 44 . . . Note=Abolished DNA-binding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 44 44 . . . Note=Strongly decreased homodimerization. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683995;Dbxref=PMID:22683995 P09874 UniProtKB Mutagenesis 45 45 . . . Note=Does not affect DNA-binding. Decreased poly-ADP-ribosyltransferase activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21233213,ECO:0000269|PubMed:22582261;Dbxref=PMID:21233213,PMID:22582261 P09874 UniProtKB Mutagenesis 119 120 . . . Note=Abolished prolonged residence (trapping) to chromatin. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35013556;Dbxref=PMID:35013556 P09874 UniProtKB Mutagenesis 122 122 . . . Note=Strongly decreased DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 138 138 . . . Note=Abolished binding to DNA strand breaks. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683995;Dbxref=PMID:22683995 P09874 UniProtKB Mutagenesis 151 154 . . . Note=Abolished DNA-binding. LGMI->AGMA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21233213;Dbxref=PMID:21233213 P09874 UniProtKB Mutagenesis 214 214 . . . Note=Abolished cleavage by caspase-7 (CASP7). D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22464733;Dbxref=PMID:22464733 P09874 UniProtKB Mutagenesis 241 241 . . . Note=Does not affect auto-poly-ADP-ribosylation. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 246 246 . . . Note=Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626479;Dbxref=PMID:22582261,PMID:26626479 P09874 UniProtKB Mutagenesis 298 298 . . . Note=Decreased stability leading to impaired oly-ADP-ribosyltransferase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18055453;Dbxref=PMID:18055453 P09874 UniProtKB Mutagenesis 314 314 . . . Note=Does not affect auto-poly-ADP-ribosylation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 315 315 . . . Note=Does not affect auto-poly-ADP-ribosylation. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 316 316 . . . Note=Strongly reduced poly-ADP-ribosyltransferase and ability to regulate chromatin compaction. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 317 317 . . . Note=Does not affect auto-poly-ADP-ribosylation. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 318 318 . . . Note=Strongly reduced poly-ADP-ribosyltransferase activity. Able to bind damaged DNA%2C however%2C defects in the interdomain communication prevent unfolding of the PARP alpha-helical domain%2C blocking catalytic activation. W->A%2CR%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20388712,ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626479,ECO:0000269|PubMed:26626480,ECO:0000269|PubMed:32241924;Dbxref=PMID:20388712,PMID:22582261,PMID:26626479,PMID:26626480,PMID:32241924 P09874 UniProtKB Mutagenesis 318 318 . . . Note=Does not affect auto-poly-ADP-ribosylation. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 319 319 . . . Note=Does not affect auto-poly-ADP-ribosylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 320 320 . . . Note=Does not affect auto-poly-ADP-ribosylation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 325 325 . . . Note=Does not affect translocation into the cytosol. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35460603;Dbxref=PMID:35460603 P09874 UniProtKB Mutagenesis 348 350 . . . Note=Does not affect auto-poly-ADP-ribosylation. LKV->DKD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 357 357 . . . Note=Does not affect auto-poly-ADP-ribosylation. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 358 359 . . . Note=Does not affect auto-poly-ADP-ribosylation. PP->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20388712;Dbxref=PMID:20388712 P09874 UniProtKB Mutagenesis 394 394 . . . Note=Strongly decreased ability of the BRCT domain to bind intact DNA%3B when associated with Q-418. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34919819;Dbxref=PMID:34919819 P09874 UniProtKB Mutagenesis 405 409 . . . Note=Strongly decreased ability of the BRCT domain to bind intact DNA. KDEVK->QDEVQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34919819;Dbxref=PMID:34919819 P09874 UniProtKB Mutagenesis 418 425 . . . Note=Strongly decreased ability of the BRCT domain to bind intact DNA. KLTGTANK->QLTGTANQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34919819;Dbxref=PMID:34919819 P09874 UniProtKB Mutagenesis 418 418 . . . Note=Strongly decreased ability of the BRCT domain to bind intact DNA%3B when associated with Q-394. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34919819;Dbxref=PMID:34919819 P09874 UniProtKB Mutagenesis 441 442 . . . Note=Strongly decreased ability of the BRCT domain to bind intact DNA. KK->QQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34919819;Dbxref=PMID:34919819 P09874 UniProtKB Mutagenesis 490 493 . . . Note=Strongly reduced interaction with TIMELESS. VEVV->GEVQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26344098;Dbxref=PMID:26344098 P09874 UniProtKB Mutagenesis 499 499 . . . Note=Abolishes automodification on serine following interaction with HPF1%2C leading to delay dissociation from chromatin%3B when associated with A-507 and A-519. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28190768,ECO:0000269|PubMed:34210965,ECO:0000269|PubMed:34625544;Dbxref=PMID:28190768,PMID:34210965,PMID:34625544 P09874 UniProtKB Mutagenesis 507 507 . . . Note=Abolishes automodification on serine following interaction with HPF1%2C leading to delay dissociation from chromatin%3B when associated with A-499 and A-519. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28190768,ECO:0000269|PubMed:34210965,ECO:0000269|PubMed:34625544;Dbxref=PMID:28190768,PMID:34210965,PMID:34625544 P09874 UniProtKB Mutagenesis 519 519 . . . Note=Abolishes automodification on serine following interaction with HPF1%2C leading to delay dissociation from chromatin%3B when associated with A-499 and A-507. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28190768,ECO:0000269|PubMed:34210965,ECO:0000269|PubMed:34625544;Dbxref=PMID:28190768,PMID:34210965,PMID:34625544 P09874 UniProtKB Mutagenesis 567 567 . . . Note=Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. N->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626479;Dbxref=PMID:22582261,PMID:26626479 P09874 UniProtKB Mutagenesis 589 589 . . . Note=Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. Abolished ability to mediate DNA intrastrand transfer (named 'monkey-bar mechanism'). W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626479;Dbxref=PMID:22582261,PMID:26626479 P09874 UniProtKB Mutagenesis 591 591 . . . Note=Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626479;Dbxref=PMID:22582261,PMID:26626479 P09874 UniProtKB Mutagenesis 594 594 . . . Note=Abolished phosphorylation by PRKDC%2C inhibiting translocation into the cytosol. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35460603;Dbxref=PMID:35460603 P09874 UniProtKB Mutagenesis 633 633 . . . Note=Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626479;Dbxref=PMID:22582261,PMID:26626479 P09874 UniProtKB Mutagenesis 698 701 . . . Note=Increased auto-poly-ADP-ribosylation. LGKL->AGKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22582261;Dbxref=PMID:22582261 P09874 UniProtKB Mutagenesis 713 713 . . . Note=Increased auto-poly-ADP-ribosylation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22582261;Dbxref=PMID:22582261 P09874 UniProtKB Mutagenesis 713 713 . . . Note=Leads to constitutive activity in absence of DNA damage due to unfolding of the PARP alpha-helical domain%2C relieving autoinhibition. L->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22582261,ECO:0000269|PubMed:26626480;Dbxref=PMID:22582261,PMID:26626480 P09874 UniProtKB Mutagenesis 763 770 . . . Note=Able to bind BAD inhibitor in absence of DNA. EMLDNLLD->AMLANLLA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29487285;Dbxref=PMID:29487285 P09874 UniProtKB Mutagenesis 765 765 . . . Note=Increased auto-poly-ADP-ribosylation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22582261;Dbxref=PMID:22582261 P09874 UniProtKB Mutagenesis 766 770 . . . Note=Able to bind EB-47 or BAD inhibitors in absence of DNA. Released from DNA strand break independently of EB-47 or BAD inhibitors. DNLLD->ANLLA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29487285,ECO:0000269|PubMed:32241924;Dbxref=PMID:29487285,PMID:32241924 P09874 UniProtKB Mutagenesis 768 768 . . . Note=Increased auto-poly-ADP-ribosylation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22582261;Dbxref=PMID:22582261 P09874 UniProtKB Mutagenesis 774 774 . . . Note=Increased DNA-independent poly-ADP-ribosyltransferase activity. A->S%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 797 797 . . . Note=1.5%25 of wild-type activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 826 826 . . . Note=Strongly reduced serine ADP-ribosylation%2C caused by abolished interaction with HPF1. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32028527;Dbxref=PMID:32028527 P09874 UniProtKB Mutagenesis 826 826 . . . Note=Decreased polymerase activity%2C leading to the production of short poly-ADP-ribose chains. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34795260;Dbxref=PMID:34795260 P09874 UniProtKB Mutagenesis 850 851 . . . Note=Abolished interaction with TIMELESS. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26344098;Dbxref=PMID:26344098 P09874 UniProtKB Mutagenesis 862 862 . . . Note=Poly-ADP-ribosyltransferase activity is impaired while mono-ADP-ribosyltransferase activity is not affected%3B produces a mixture of short and mono ADP-ribose chains. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7852410;Dbxref=PMID:7852410 P09874 UniProtKB Mutagenesis 865 865 . . . Note=Increased affinity for DNA damage sites. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34795260;Dbxref=PMID:34795260 P09874 UniProtKB Mutagenesis 868 868 . . . Note=4%25 of wild-type activity. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 870 870 . . . Note=Increased DNA-independent poly-ADP-ribosyltransferase activity. A->S%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 871 871 . . . Note=Increased DNA-independent poly-ADP-ribosyltransferase activity. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 871 871 . . . Note=Does not affect DNA-independent poly-ADP-ribosyltransferase activity. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 882 882 . . . Note=Does not affect DNA-independent poly-ADP-ribosyltransferase activity. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 883 887 . . . Note=Does not affect DNA-independent poly-ADP-ribosyltransferase activity. EAPVT->ASSVA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 883 883 . . . Note=Does not affect ADP-ribosyltransferase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7852410;Dbxref=PMID:7852410 P09874 UniProtKB Mutagenesis 885 885 . . . Note=Does not affect DNA-independent poly-ADP-ribosyltransferase activity. P->G%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26626480;Dbxref=PMID:26626480 P09874 UniProtKB Mutagenesis 890 890 . . . Note=<0.5%25 of wild-type activity. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 893 893 . . . Note=Abolishes enzymatic activity. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 897 897 . . . Note=10%25 of wild-type activity. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 899 899 . . . Note=0.6%25 of wild-type activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 908 908 . . . Note=<0.5%25 of wild-type activity. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 923 923 . . . Note=Does not affect ADP-ribosyltransferase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7852410;Dbxref=PMID:7852410 P09874 UniProtKB Mutagenesis 926 926 . . . Note=1.5%25 of wild-type activity. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 931 931 . . . Note=Does not affect ADP-ribosyltransferase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7852410;Dbxref=PMID:7852410 P09874 UniProtKB Mutagenesis 986 986 . . . Note=14%25 of wild-type activity and increased branching 15-fold. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 988 988 . . . Note=Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected%3B only monomers are added. Disrupts interaction with CHD1L and ability to recruit PARP2 to DNA damage sites. E->A%2CD%2CQ%2CK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29220653,ECO:0000269|PubMed:30104678,ECO:0000269|PubMed:32028527,ECO:0000269|PubMed:7852410,ECO:0000269|PubMed:9315851;Dbxref=PMID:29220653,PMID:30104678,PMID:32028527,PMID:7852410,PMID:9315851 P09874 UniProtKB Mutagenesis 993 993 . . . Note=Abolished interaction with TIMELESS. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26344098;Dbxref=PMID:26344098 P09874 UniProtKB Mutagenesis 1003 1003 . . . Note=1.5%25 of wild-type activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315851;Dbxref=PMID:9315851 P09874 UniProtKB Mutagenesis 1013 1014 . . . Note=Strongly reduced serine ADP-ribosylation%2C caused by abolished interaction with HPF1. LW->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32028527;Dbxref=PMID:32028527 P09874 UniProtKB Sequence conflict 17 17 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Sequence conflict 70 70 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Sequence conflict 212 212 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Sequence conflict 613 613 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Sequence conflict 827 827 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Sequence conflict 908 908 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Sequence conflict 980 980 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09874 UniProtKB Turn 2 5 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L30 P09874 UniProtKB Beta strand 8 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L30 P09874 UniProtKB Beta strand 32 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Beta strand 42 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Helix 54 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Helix 67 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Helix 74 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Helix 79 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OD8 P09874 UniProtKB Beta strand 102 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N8A P09874 UniProtKB Beta strand 113 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Beta strand 137 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Beta strand 148 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Helix 160 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Helix 167 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Turn 174 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Helix 177 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Helix 189 198 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ODC P09874 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L31 P09874 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N8A P09874 UniProtKB Helix 226 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Helix 258 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Turn 273 275 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JVN P09874 UniProtKB Helix 276 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Turn 296 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Beta strand 302 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Beta strand 308 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Beta strand 314 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Beta strand 324 327 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Helix 337 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Helix 342 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RIQ P09874 UniProtKB Turn 389 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Helix 405 414 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Beta strand 418 420 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Beta strand 427 431 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Helix 434 438 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Helix 441 448 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Beta strand 452 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Helix 458 464 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Helix 469 472 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Turn 473 475 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SCZ P09874 UniProtKB Helix 535 537 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Turn 540 542 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Beta strand 543 545 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Beta strand 548 550 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S68 P09874 UniProtKB Beta strand 554 561 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Turn 562 565 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Beta strand 566 581 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Beta strand 583 591 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Beta strand 597 606 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Helix 607 622 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Beta strand 639 641 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S6H P09874 UniProtKB Helix 667 676 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Helix 679 688 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Turn 693 695 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Helix 698 700 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Helix 703 721 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Helix 726 739 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Beta strand 745 747 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7ONS P09874 UniProtKB Beta strand 752 754 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UK0 P09874 UniProtKB Helix 755 779 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Beta strand 785 787 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4R6E P09874 UniProtKB Helix 790 796 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 799 803 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 806 808 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RCW P09874 UniProtKB Helix 809 820 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 824 826 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Beta strand 829 841 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 844 848 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 849 851 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 853 855 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GN7 P09874 UniProtKB Beta strand 857 863 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 866 868 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 869 875 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 882 884 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VKQ P09874 UniProtKB Helix 886 888 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AAC P09874 UniProtKB Beta strand 889 891 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WOK P09874 UniProtKB Beta strand 893 900 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 901 905 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 906 908 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 912 914 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7KK5 P09874 UniProtKB Beta strand 916 925 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 928 934 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 938 940 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VKK P09874 UniProtKB Beta strand 947 950 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 952 956 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 958 960 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 962 964 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 967 969 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 974 976 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 983 986 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 988 993 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Helix 994 996 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH P09874 UniProtKB Beta strand 997 1009 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NRH