##gff-version 3 P12004 UniProtKB Chain 1 261 . . . ID=PRO_0000149158;Note=Proliferating cell nuclear antigen P12004 UniProtKB DNA binding 61 80 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P12004 UniProtKB Region 7 100 . . . Note=Interaction with NUDT15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19419956;Dbxref=PMID:19419956 P12004 UniProtKB Modified residue 14 14 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19419956;Dbxref=PMID:19419956 P12004 UniProtKB Modified residue 77 77 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P12004 UniProtKB Modified residue 80 80 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P12004 UniProtKB Modified residue 211 211 . . . Note=Phosphotyrosine%3B by EGFR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17115032;Dbxref=PMID:17115032 P12004 UniProtKB Modified residue 248 248 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P12004 UniProtKB Cross-link 164 164 . . . 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:25755297,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25114211,PMID:25755297,PMID:25772364,PMID:28112733 P12004 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17108083,ECO:0000269|PubMed:17130289;Dbxref=PMID:17108083,PMID:17130289 P12004 UniProtKB Cross-link 254 254 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P12004 UniProtKB Natural variant 228 228 . . . ID=VAR_071871;Note=In ATLD2%3B a hypomorphic mutation affecting DNA repair in response to UV%3B results in significantly decreased interaction with FEN1%2C LIG1 and ERCC5. S->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24911150;Dbxref=dbSNP:rs369958038,PMID:24911150 P12004 UniProtKB Mutagenesis 13 13 . . . Note=Inhibits acetylation%2C recruitment to DNA damage sites%2C inducible ubiquitination and protein degradation%2C DNA replication and repair synthesis efficiencies%2C but homotrimer formation%2C nuclear recruitment to DNA damage sites%2C interactions with CREBBP%2C EP300 and POLD1 are similar as the wild-type%3B in association with R-14%3B R-20%3B R-77 and R-80. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 14 14 . . . Note=Inhibits acetylation%2C recruitment to DNA damage sites%2C inducible ubiquitination and protein degradation%2C DNA replication and repair synthesis efficiencies%2C but homotrimer formation%2C nuclear recruitment to DNA damage sites%2C interactions with CREBBP%2C EP300 and POLD1 are similar as the wild-type%3B in association with R-13%3B R-20%3B R-77 and R-80. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 20 20 . . . Note=Inhibits acetylation%2C recruitment to DNA damage sites%2C inducible ubiquitination and protein degradation%2C DNA replication and repair synthesis efficiencies%2C but homotrimer formation%2C nuclear recruitment to DNA damage sites%2C interactions with CREBBP%2C EP300 and POLD1 are similar as the wild-type%3B in association with R-13%3B R-14%3B R-77 and R-80. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 40 40 . . . Note=Complete loss of interaction with UHRF2. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11595739;Dbxref=PMID:11595739 P12004 UniProtKB Mutagenesis 43 45 . . . Note=No effect on POLD3-binding. Impairs binding to ALKBH2. SHV->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11595739,ECO:0000269|PubMed:26408825;Dbxref=PMID:11595739,PMID:26408825 P12004 UniProtKB Mutagenesis 77 77 . . . Note=Inhibits recruitment to DNA damage sites%2C but nuclear localization is similar as the wild-type%3B in association with A-80. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 77 77 . . . Note=Inhibits acetylation%2C recruitment to DNA damage sites%2C inducible ubiquitination and protein degradation%2C DNA replication and repair synthesis efficiencies%2C but homotrimer formation%2C nuclear recruitment to DNA damage sites%2C interactions with CREBBP%2C EP300 and POLD1 are similar as the wild-type%3B in association with R-13%3B R-14%3B R-20 and R-80. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 80 80 . . . Note=Inhibits recruitment to DNA damage sites%2C but nuclear localization is similar as the wild-type%3B in association with A-77. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 80 80 . . . Note=Inhibits acetylation%2C recruitment to DNA damage sites%2C inducible ubiquitination and protein degradation%2C DNA replication and repair synthesis efficiencies%2C but homotrimer formation%2C nuclear recruitment to DNA damage sites%2C interactions with CREBBP%2C EP300 and POLD1 are similar as the wild-type%3B in association with R-13%3B R-14%3B R-20 and R-77. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24939902;Dbxref=PMID:24939902 P12004 UniProtKB Mutagenesis 125 128 . . . Note=Strong decrease in POLD3-binding. Impairs binding to ALKBH2. QLGI->AAAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11595739,ECO:0000269|PubMed:26408825;Dbxref=PMID:11595739,PMID:26408825 P12004 UniProtKB Mutagenesis 128 128 . . . Note=Complete loss of interaction with UHRF2. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11595739;Dbxref=PMID:11595739 P12004 UniProtKB Mutagenesis 164 164 . . . Note=Abolishes ubiquitination. No effect on interaction with SHPRH. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17108083,ECO:0000269|PubMed:17130289,ECO:0000269|PubMed:18719106,ECO:0000269|PubMed:20129063;Dbxref=PMID:17108083,PMID:17130289,PMID:18719106,PMID:20129063 P12004 UniProtKB Mutagenesis 188 190 . . . Note=No effect on POLD3-binding. No effect on ALKBH2-binding. VDK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11595739,ECO:0000269|PubMed:26408825;Dbxref=PMID:11595739,PMID:26408825 P12004 UniProtKB Mutagenesis 211 211 . . . Note=Alters chromatin-associated PCNA stability and its function in DNA replication and repair. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17115032;Dbxref=PMID:17115032 P12004 UniProtKB Mutagenesis 250 250 . . . Note=Complete loss of interaction with UHRF2. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11595739;Dbxref=PMID:11595739 P12004 UniProtKB Mutagenesis 251 254 . . . Note=Decrease in POLD3-binding. LAPK->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11595739;Dbxref=PMID:11595739 P12004 UniProtKB Mutagenesis 252 252 . . . Note=Complete loss of interaction with UHRF2. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11595739;Dbxref=PMID:11595739 P12004 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 10 20 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 24 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 34 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 44 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 57 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 72 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 87 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VYM P12004 UniProtKB Beta strand 97 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F5Q P12004 UniProtKB Beta strand 111 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E0U P12004 UniProtKB Beta strand 134 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 141 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 156 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 166 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 176 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 191 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E0U P12004 UniProtKB Beta strand 196 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 203 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 209 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Helix 216 221 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 223 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 231 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1VYM P12004 UniProtKB Beta strand 235 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Turn 242 244 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 245 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1U7B P12004 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7KQ1