##gff-version 3 O92531 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26664 O92531 UniProtKB Chain 2 3016 . . . ID=PRO_0000450931;Note=Genome polyprotein O92531 UniProtKB Chain 2 191 . . . ID=PRO_0000045724;Note=Core protein precursor;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Chain 2 177 . . . ID=PRO_0000045725;Note=Mature core protein O92531 UniProtKB Propeptide 178 191 . . . ID=PRO_0000045726;Note=ER anchor for the core protein%2C removed in mature form by host signal peptidase O92531 UniProtKB Chain 192 383 . . . ID=PRO_0000045727;Note=Envelope glycoprotein E1 O92531 UniProtKB Chain 384 748 . . . ID=PRO_0000045728;Note=Envelope glycoprotein E2 O92531 UniProtKB Chain 749 811 . . . ID=PRO_0000045729;Note=Viroporin p7 O92531 UniProtKB Chain 812 1028 . . . ID=PRO_0000045730;Note=Protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O92531 UniProtKB Chain 1029 1659 . . . ID=PRO_0000045731;Note=Serine protease/helicase NS3 O92531 UniProtKB Chain 1660 1713 . . . ID=PRO_0000045732;Note=Non-structural protein 4A O92531 UniProtKB Chain 1714 1974 . . . ID=PRO_0000045733;Note=Non-structural protein 4B O92531 UniProtKB Chain 1975 2425 . . . ID=PRO_0000045734;Note=Non-structural protein 5A O92531 UniProtKB Chain 2426 3016 . . . ID=PRO_0000045735;Note=RNA-directed RNA polymerase O92531 UniProtKB Topological domain 2 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Topological domain 190 358 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Topological domain 380 727 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 728 748 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Topological domain 749 759 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 760 780 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Topological domain 781 784 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 785 805 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Topological domain 806 815 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 816 836 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Topological domain 837 883 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Transmembrane 884 904 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Topological domain 905 930 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Transmembrane 931 951 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Topological domain 952 1659 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Transmembrane 1660 1680 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Topological domain 1681 1807 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Transmembrane 1808 1828 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Topological domain 1829 1830 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 1831 1851 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Topological domain 1852 1852 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Transmembrane 1853 1873 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Topological domain 1874 1883 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Transmembrane 1884 1904 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Topological domain 1905 1974 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Intramembrane 1975 2004 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Topological domain 2005 2995 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Transmembrane 2996 3016 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Domain 905 1028 . . . Note=Peptidase C18;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O92531 UniProtKB Domain 1029 1210 . . . Note=Peptidase S29;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Domain 1219 1371 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 O92531 UniProtKB Domain 2639 2757 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 O92531 UniProtKB Region 2 75 . . . Note=Disordered;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 2 59 . . . Note=Interaction with DDX3X;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG65 O92531 UniProtKB Region 2 58 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Region 2 23 . . . Note=Interaction with STAT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Region 112 152 . . . Note=Important for endoplasmic reticulum and mitochondrial localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Region 122 173 . . . Note=Interaction with APOA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29846 O92531 UniProtKB Region 164 167 . . . Note=Important for lipid droplets localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 265 296 . . . Note=Important for fusion;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 385 411 . . . Note=HVR1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 474 478 . . . Note=HVR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 480 493 . . . Note=CD81-binding 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Region 544 551 . . . Note=CD81-binding 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Region 662 673 . . . Note=PKR/eIF2-alpha phosphorylation homology domain (PePHD) O92531 UniProtKB Region 906 1208 . . . Note=Protease NS2-3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Region 931 951 . . . Note=Interaction with host SCPS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Region 1488 1500 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Region 1681 1692 . . . Note=NS3-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 2122 2335 . . . Note=Transcriptional activation;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Region 2122 2210 . . . Note=FKBP8-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Region 2137 2141 . . . Note=Interaction with non-structural protein 4A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Region 2191 2443 . . . Note=Interaction with host SKP2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Region 2212 2277 . . . Note=Interaction with EIF2AK2/PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Region 2212 2251 . . . Note=ISDR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Region 2251 2309 . . . Note=NS4B-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Region 2302 2379 . . . Note=V3 O92531 UniProtKB Region 2353 2414 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O92531 UniProtKB Motif 5 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Motif 38 43 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Motif 66 71 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Motif 1318 1321 . . . Note=DECH box;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Motif 2325 2328 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Motif 2330 2338 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Compositional bias 47 61 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O92531 UniProtKB Compositional bias 2355 2375 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O92531 UniProtKB Active site 954 954 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O92531 UniProtKB Active site 974 974 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O92531 UniProtKB Active site 995 995 . . . Note=For protease NS2 activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O92531 UniProtKB Active site 1085 1085 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Active site 1109 1109 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Active site 1167 1167 . . . Note=Charge relay system%3B for serine protease NS3 activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Binding site 1125 1125 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Binding site 1127 1127 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Binding site 1173 1173 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Binding site 1177 1177 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01166 O92531 UniProtKB Binding site 1232 1239 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 O92531 UniProtKB Binding site 1239 1239 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Binding site 1319 1319 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Binding site 2013 2013 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Binding site 2031 2031 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Binding site 2033 2033 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Binding site 2054 2054 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Binding site 2645 2645 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Binding site 2743 2743 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Binding site 2744 2744 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26663 O92531 UniProtKB Site 177 178 . . . Note=Cleavage%3B by host signal peptide peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Site 191 192 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Site 383 384 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Site 748 749 . . . Note=Cleavage%3B by host signal peptidase O92531 UniProtKB Site 811 812 . . . Note=Cleavage%3B by host signal peptidase O92531 UniProtKB Site 1028 1029 . . . Note=Cleavage%3B by protease NS2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01030 O92531 UniProtKB Site 1659 1660 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Site 1713 1714 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Site 1974 1975 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Site 2425 2426 . . . Note=Cleavage%3B by serine protease NS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q913V3 O92531 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O92531 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O92531 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01403 O92531 UniProtKB Modified residue 2196 2196 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Modified residue 2199 2199 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Modified residue 2203 2203 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Modified residue 2206 2206 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WMX2 O92531 UniProtKB Modified residue 2209 2209 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Modified residue 2212 2212 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99IB8 O92531 UniProtKB Modified residue 2454 2454 . . . Note=Phosphoserine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26662 O92531 UniProtKB Lipidation 924 924 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Lipidation 1974 1974 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 416 416 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 422 422 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 429 429 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Glycosylation 475 475 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Glycosylation 532 532 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Glycosylation 556 556 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 O92531 UniProtKB Glycosylation 625 625 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Glycosylation 647 647 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 428 552 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 451 458 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 486 494 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 503 508 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 564 569 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 583 587 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 599 622 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 609 646 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Disulfide bond 654 679 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958 O92531 UniProtKB Cross-link 2353 2353 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27958