##gff-version 3 P0CG47 UniProtKB Chain 1 76 . . . ID=PRO_0000396174;Note=Ubiquitin P0CG47 UniProtKB Chain 77 152 . . . ID=PRO_0000396175;Note=Ubiquitin P0CG47 UniProtKB Chain 153 228 . . . ID=PRO_0000396176;Note=Ubiquitin P0CG47 UniProtKB Propeptide 229 229 . . . ID=PRO_0000396177 P0CG47 UniProtKB Domain 1 76 . . . Note=Ubiquitin-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 P0CG47 UniProtKB Domain 77 152 . . . Note=Ubiquitin-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 P0CG47 UniProtKB Domain 153 228 . . . Note=Ubiquitin-like 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 P0CG47 UniProtKB Site 54 54 . . . Note=Interacts with activating enzyme P0CG47 UniProtKB Site 68 68 . . . Note=Essential for function P0CG47 UniProtKB Site 72 72 . . . Note=Interacts with activating enzyme P0CG47 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine%3B by PINK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24660806,ECO:0000269|PubMed:24751536,ECO:0000269|PubMed:24784582,ECO:0000269|PubMed:25527291;Dbxref=PMID:24660806,PMID:24751536,PMID:24784582,PMID:25527291 P0CG47 UniProtKB Modified residue 66 66 . . . Note=(Microbial infection) ADP-ribosylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32330457;Dbxref=PMID:32330457 P0CG47 UniProtKB Modified residue 76 76 . . . Note=ADP-ribosylglycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Cross-link 6 6 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16443603;Dbxref=PMID:16443603 P0CG47 UniProtKB Cross-link 11 11 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:16543144;Dbxref=PMID:16443603,PMID:16543144 P0CG47 UniProtKB Cross-link 27 27 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15466860;Dbxref=PMID:15466860 P0CG47 UniProtKB Cross-link 29 29 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543144,ECO:0000269|PubMed:25752573,ECO:0000269|PubMed:25752577,ECO:0000269|PubMed:34239127;Dbxref=PMID:16543144,PMID:25752573,PMID:25752577,PMID:34239127 P0CG47 UniProtKB Cross-link 33 33 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25752577;Dbxref=PMID:25752577 P0CG47 UniProtKB Cross-link 48 48 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:16543144;Dbxref=PMID:16443603,PMID:16543144 P0CG47 UniProtKB Cross-link 63 63 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543144,ECO:0000269|PubMed:18719106;Dbxref=PMID:16543144,PMID:18719106 P0CG47 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) P0CG47 UniProtKB Natural variant 76 229 . . . ID=VAR_066248;Note=In UBB(+1)%3B loss of polyubiquitination%3B impairs the ubiquitin-proteasome pathway%3B refractory to disassembly by DUBs%3B slow degradation by UCHL3. GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC->YADLREDPDRQDHHPGSGAQ P0CG47 UniProtKB Mutagenesis 48 48 . . . Note=No effect on HLTF-mediated polyubiquitination of PCNA. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18719106;Dbxref=PMID:18719106 P0CG47 UniProtKB Mutagenesis 63 63 . . . Note=Abolishes HLTF-mediated polyubiquitination of PCNA. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18719106;Dbxref=PMID:18719106 P0CG47 UniProtKB Mutagenesis 65 65 . . . Note=Prevents phosphorylation in case of mitophagy. Decreased localization of PRKN to mitochondria. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24660806,ECO:0000269|PubMed:24751536,ECO:0000269|PubMed:24784582;Dbxref=PMID:24660806,PMID:24751536,PMID:24784582 P0CG47 UniProtKB Mutagenesis 65 65 . . . Note=Phosphomimetic mutant that binds and activates PRKN. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24751536;Dbxref=PMID:24751536 P0CG47 UniProtKB Mutagenesis 65 65 . . . Note=Phosphomimetic mutant that binds and activates PRKN. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24751536;Dbxref=PMID:24751536 P0CG47 UniProtKB Mutagenesis 68 68 . . . Note=Loss of DTX3L-mediated polyubiquitination of histone H3 and H4. H->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Mutagenesis 72 72 . . . Note=No effect on ADP-ribosylation. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Mutagenesis 72 72 . . . Note=No effect on ADP-ribosylation%2C when associated with K-74. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Mutagenesis 74 74 . . . Note=No effect on ADP-ribosylation. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Mutagenesis 74 74 . . . Note=No effect on ADP-ribosylation%2C when associated with K-72. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Mutagenesis 76 76 . . . Note=Loss of ADP-ribosylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28525742;Dbxref=PMID:28525742 P0CG47 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MYH P0CG47 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Helix 99 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Beta strand 117 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Beta strand 142 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RBR P0CG47 UniProtKB Beta strand 154 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NBB P0CG47 UniProtKB Beta strand 164 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Beta strand 171 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XPK P0CG47 UniProtKB Helix 175 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Beta strand 200 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UV5 P0CG47 UniProtKB Beta strand 206 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GO7 P0CG47 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Beta strand 218 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5NVG P0CG47 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EFW