##gff-version 3 Q99638 UniProtKB Chain 1 391 . . . ID=PRO_0000225000;Note=Cell cycle checkpoint control protein RAD9A Q99638 UniProtKB Region 51 91 . . . Note=Possesses 3'-5' exonuclease activity Q99638 UniProtKB Region 266 391 . . . Note=Sufficient for interaction with ABL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11971963;Dbxref=PMID:11971963 Q99638 UniProtKB Region 268 301 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99638 UniProtKB Region 319 391 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99638 UniProtKB Modified residue 28 28 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11971963;Dbxref=PMID:11971963 Q99638 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12709442;Dbxref=PMID:12709442 Q99638 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:12709442,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231;Dbxref=PMID:12709442,PMID:18669648,PMID:19690332,PMID:20068231 Q99638 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:12709442,ECO:0007744|PubMed:23186163;Dbxref=PMID:12709442,PMID:23186163 Q99638 UniProtKB Modified residue 341 341 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12709442,ECO:0000269|PubMed:20545769;Dbxref=PMID:12709442,PMID:20545769 Q99638 UniProtKB Modified residue 375 375 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:12709442,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231;Dbxref=PMID:12709442,PMID:17081983,PMID:19690332,PMID:20068231 Q99638 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:12709442,ECO:0007744|PubMed:17081983;Dbxref=PMID:12709442,PMID:17081983 Q99638 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:12709442,ECO:0000269|PubMed:17575048,ECO:0000269|PubMed:20545769,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:12709442,PMID:17081983,PMID:17575048,PMID:18669648,PMID:19690332,PMID:20068231,PMID:20545769,PMID:21406692,PMID:23186163 Q99638 UniProtKB Natural variant 3 3 . . . ID=VAR_025410;Note=C->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs11575913 Q99638 UniProtKB Natural variant 71 71 . . . ID=VAR_051724;Note=L->Q;Dbxref=dbSNP:rs2422490 Q99638 UniProtKB Natural variant 100 100 . . . ID=VAR_025411;Note=S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs2066492 Q99638 UniProtKB Natural variant 239 239 . . . ID=VAR_025412;Note=H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs17880039 Q99638 UniProtKB Natural variant 307 307 . . . ID=VAR_025413;Note=M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs17882466 Q99638 UniProtKB Mutagenesis 28 28 . . . Note=Abolishes phosphorylation by ABL1. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11971963;Dbxref=PMID:11971963 Q99638 UniProtKB Mutagenesis 272 272 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-277%3B A-328%3B A-341%3B A-375%3B A-380 and A-387. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12709442;Dbxref=PMID:12709442 Q99638 UniProtKB Mutagenesis 277 277 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-272%3B A-328%3B A-341%3B A-375%3B A-380 and A-387. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12709442;Dbxref=PMID:12709442 Q99638 UniProtKB Mutagenesis 328 328 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-272%3B A-277%3B A-341%3B A-375%3B A-380 and A-387. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12709442;Dbxref=PMID:12709442 Q99638 UniProtKB Mutagenesis 341 341 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-272%3B A-277%3B A-328%3B A-375%3B A-380 and A-387. Abolished phosphorylation by CK2%2C preventing interaction with TOPBP1%3B when associated with A-387. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12709442,ECO:0000269|PubMed:20545769;Dbxref=PMID:12709442,PMID:20545769 Q99638 UniProtKB Mutagenesis 341 341 . . . Note=Mimics phosphorylation%2C leading to weak but significant interaction with TOPBP1%3B when associated with E-387. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20545769;Dbxref=PMID:20545769 Q99638 UniProtKB Mutagenesis 375 375 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-272%3B A-277%3B A-328%3B A-341%3B A-380 and A-387. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12709442;Dbxref=PMID:12709442 Q99638 UniProtKB Mutagenesis 380 380 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-272%3B A-277%3B A-328%3B A-341%3B A-375 and A-387. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12709442;Dbxref=PMID:12709442 Q99638 UniProtKB Mutagenesis 387 387 . . . Note=Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex%3B when associated with A-272%3B A-277%3B A-328%3B A-341%3B A-375 and A-380. Abolished phosphorylation by CK2%2C preventing interaction with TOPBP1%3B when associated with A-341. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12709442,ECO:0000269|PubMed:20545769;Dbxref=PMID:12709442,PMID:20545769 Q99638 UniProtKB Mutagenesis 387 387 . . . Note=Mimics phosphorylation%2C leading to weak but significant interaction with TOPBP1%3B when associated with E-341. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20545769;Dbxref=PMID:20545769 Q99638 UniProtKB Sequence conflict 12 12 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99638 UniProtKB Sequence conflict 130 130 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99638 UniProtKB Beta strand 2 6 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 9 21 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 25 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 35 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6J8Y Q99638 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3A1J Q99638 UniProtKB Beta strand 73 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 77 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 87 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 94 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 103 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GGR Q99638 UniProtKB Beta strand 107 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 142 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 149 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 165 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Turn 172 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 187 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GGR Q99638 UniProtKB Beta strand 194 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Helix 219 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 235 240 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 241 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GGR Q99638 UniProtKB Beta strand 247 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 254 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8GNN Q99638 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3G65 Q99638 UniProtKB Beta strand 382 384 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6HM5