##gff-version 3 P15927 UniProtKB Chain 1 270 . . . ID=PRO_0000097270;Note=Replication protein A 32 kDa subunit P15927 UniProtKB DNA binding 74 148 . . . Note=OB P15927 UniProtKB Region 21 41 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15927 UniProtKB Region 187 270 . . . Note=Interaction with RAD52%2C TIPIN%2C UNG and XPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081631;Dbxref=PMID:11081631 P15927 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:9139719,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231;Dbxref=PMID:19413330,PMID:20068231,PMID:9139719 P15927 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21731742,ECO:0000269|PubMed:26474068;Dbxref=PMID:21731742,PMID:26474068 P15927 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21731742,ECO:0000269|PubMed:26474068;Dbxref=PMID:21731742,PMID:26474068 P15927 UniProtKB Modified residue 21 21 . . . Note=Phosphothreonine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21558276,ECO:0000269|PubMed:26474068,ECO:0000269|PubMed:9139719,ECO:0000269|PubMed:9295339;Dbxref=PMID:21558276,PMID:26474068,PMID:9139719,PMID:9295339 P15927 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine%3B by CDK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:1318195,ECO:0000269|PubMed:8246944,ECO:0000269|PubMed:9295339,ECO:0007744|PubMed:20068231;Dbxref=PMID:1318195,PMID:20068231,PMID:8246944,PMID:9295339 P15927 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:1318195,ECO:0000269|PubMed:8246944,ECO:0000269|PubMed:9139719,ECO:0000269|PubMed:9295339,ECO:0007744|PubMed:20068231;Dbxref=PMID:1318195,PMID:20068231,PMID:8246944,PMID:9139719,PMID:9295339 P15927 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26474068,ECO:0000269|PubMed:9139719,ECO:0000269|PubMed:9295339;Dbxref=PMID:26474068,PMID:9139719,PMID:9295339 P15927 UniProtKB Cross-link 37 37 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26474068;Dbxref=PMID:26474068 P15927 UniProtKB Cross-link 38 38 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26474068;Dbxref=PMID:26474068 P15927 UniProtKB Alternative sequence 1 4 . . . ID=VSP_017201;Note=In isoform 2. MWNS->MGRGDRNKRSIR;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15927 UniProtKB Alternative sequence 1 4 . . . ID=VSP_017202;Note=In isoform 3. MWNS->MWNSNDGGAGWRRKRIAGGFSKRASLGSERRVVAGEEGRERSWGVWGSPAGRRRGRLGRLGQCLKGRSLREPAGFSEAWDVAQALILLFKTG;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15927 UniProtKB Natural variant 14 14 . . . ID=VAR_023300;Note=Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs28988896 P15927 UniProtKB Natural variant 15 15 . . . ID=VAR_023301;Note=G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs28988897 P15927 UniProtKB Natural variant 203 203 . . . ID=VAR_023302;Note=N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs28904899 P15927 UniProtKB Mutagenesis 4 4 . . . Note=Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks%3B when associated with A-8. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21731742;Dbxref=PMID:21731742 P15927 UniProtKB Mutagenesis 8 8 . . . Note=Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks%3B when associated with A-4. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20154705,ECO:0000269|PubMed:21731742;Dbxref=PMID:20154705,PMID:21731742 P15927 UniProtKB Mutagenesis 8 8 . . . Note=Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage%3B when associated with D-33. No effect on cell-cycle progression%2C nor DNA synthesis in undamaged cells%3B when associated with D-23%3B D-29 and D-33. Impaired DNA double strand breaks repair%3B when associated with D-23%3B D-29 and D-33. Extended DNA damage-induced G2-M checkpoint%3B when associated with D-23%3B D-29 and D-33. Preferentially interacts with RAD51%3B when associated with D-23%3B D-29 and D-33. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20154705,ECO:0000269|PubMed:21731742;Dbxref=PMID:20154705,PMID:21731742 P15927 UniProtKB Mutagenesis 23 23 . . . Note=No effect on DNA synthesis following DNA damage%3B when associated with D-29. No effect on cell-cycle progression%2C nor DNA synthesis in undamaged cells%3B when associated with D-8%3B D-29 and D-33. Impaired DNA double strand breaks repair%3B when associated with D-8%3B D-29 and D-33. Extended DNA damage-induced G2-M checkpoint%3B when associated with D-8%3B D-29 and D-33. Preferentially interacts with RAD51%3B when associated with D-8%3B D-29 and D-33. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20154705;Dbxref=PMID:20154705 P15927 UniProtKB Mutagenesis 29 29 . . . Note=Reduces phosphorylation by CDK1. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20154705,ECO:0000269|PubMed:9139719;Dbxref=PMID:20154705,PMID:9139719 P15927 UniProtKB Mutagenesis 29 29 . . . Note=No effect on DNA synthesis following DNA damage%3B when associated with D-23. No effect on cell-cycle progression%2C nor DNA synthesis in undamaged cells%3B when associated with D-8%3B D-23 and D-33. Impaired DNA double strand breaks repair%3B when associated with D-8%3B D-23 and D-33. Extended DNA damage-induced G2-M checkpoint%3B when associated with D-8%3B D-23 and D-33. Preferentially interacts with RAD51%3B when associated with D-8%3B D-23 and D-33. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20154705,ECO:0000269|PubMed:9139719;Dbxref=PMID:20154705,PMID:9139719 P15927 UniProtKB Mutagenesis 33 33 . . . Note=Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage%3B when associated with D-8. No effect on cell-cycle progression%2C nor DNA synthesis in undamaged cells%3B when associated with D-8%3B D-23 and D-29. Impaired DNA double strand breaks repair%3B when associated with D-8%3B D-23 and D-29. Extended DNA damage-induced G2-M checkpoint%3B when associated with D-8%3B D-23 and D-29. Preferentially interacts with RAD51%3B when associated with D-8%3B D-23 and D-29. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20154705;Dbxref=PMID:20154705 P15927 UniProtKB Mutagenesis 37 38 . . . Note=Impaired ubiquitination without affecting homologous recombination. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26474068;Dbxref=PMID:26474068 P15927 UniProtKB Mutagenesis 248 248 . . . Note=Abolishes interaction with RFWD3%2C leading to impair DNA interstrand cross-links (ICL) repair. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28575657;Dbxref=PMID:28575657 P15927 UniProtKB Mutagenesis 252 252 . . . Note=Abolishes interaction with RFWD3%2C leading to impair DNA interstrand cross-links (ICL) repair. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28575657;Dbxref=PMID:28575657 P15927 UniProtKB Mutagenesis 253 253 . . . Note=Does not affect interaction with RFWD3. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28575657;Dbxref=PMID:28575657 P15927 UniProtKB Mutagenesis 254 254 . . . Note=Abolishes interaction with RFWD3%2C leading to impair DNA interstrand cross-links (ICL) repair. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28575657;Dbxref=PMID:28575657 P15927 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1L1O P15927 UniProtKB Helix 51 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QUQ P15927 UniProtKB Beta strand 73 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 87 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 125 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Beta strand 138 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Helix 153 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KDF P15927 UniProtKB Helix 207 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4OU0 P15927 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DPU P15927 UniProtKB Helix 227 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4OU0 P15927 UniProtKB Helix 239 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4OU0 P15927 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4OU0 P15927 UniProtKB Beta strand 263 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4OU0