##gff-version 3 O15381 UniProtKB Chain 1 856 . . . ID=PRO_0000084588;Note=Nuclear valosin-containing protein-like O15381 UniProtKB Region 1 220 . . . Note=Interaction with RPL5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Region 84 175 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O15381 UniProtKB Region 197 236 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O15381 UniProtKB Region 267 474 . . . Note=Interaction with WDR74;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28416111;Dbxref=PMID:28416111 O15381 UniProtKB Region 496 523 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O15381 UniProtKB Motif 49 52 . . . Note=Nucleolar localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Motif 85 88 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Motif 218 232 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Compositional bias 110 162 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O15381 UniProtKB Compositional bias 199 221 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O15381 UniProtKB Compositional bias 496 512 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O15381 UniProtKB Binding site 305 312 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22226966;Dbxref=PMID:22226966 O15381 UniProtKB Binding site 622 629 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22226966;Dbxref=PMID:22226966 O15381 UniProtKB Modified residue 70 70 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBY8 O15381 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163 O15381 UniProtKB Modified residue 138 138 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163 O15381 UniProtKB Modified residue 156 156 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBY8 O15381 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBY8 O15381 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692;Dbxref=PMID:20068231,PMID:21406692 O15381 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 O15381 UniProtKB Cross-link 208 208 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 O15381 UniProtKB Alternative sequence 1 216 . . . ID=VSP_045334;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 O15381 UniProtKB Alternative sequence 1 106 . . . ID=VSP_007771;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:9286697;Dbxref=PMID:15489334,PMID:9286697 O15381 UniProtKB Alternative sequence 115 205 . . . ID=VSP_007772;Note=In isoform 3 and isoform 5. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334 O15381 UniProtKB Alternative sequence 320 320 . . . ID=VSP_045335;Note=In isoform 4. G->GAECSGMITAHCSFDFSGSNDPPASASQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 O15381 UniProtKB Natural variant 295 295 . . . ID=VAR_048109;Note=V->I;Dbxref=dbSNP:rs12084919 O15381 UniProtKB Natural variant 359 359 . . . ID=VAR_015890;Note=C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9286697;Dbxref=PMID:9286697 O15381 UniProtKB Natural variant 404 404 . . . ID=VAR_048110;Note=V->I;Dbxref=dbSNP:rs34631151 O15381 UniProtKB Mutagenesis 51 52 . . . Note=Loss of nucleolar localization and interaction with RPL5. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Mutagenesis 85 86 . . . Note=Decreased nuclear localization. Complete loss of nuclear localization%3B when associated with 218-A--A-220 and 230-A--A-232. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Mutagenesis 173 173 . . . Note=Abolishes binding to MTREX. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31358741;Dbxref=PMID:31358741 O15381 UniProtKB Mutagenesis 175 175 . . . Note=Impairs binding to MTREX. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31358741;Dbxref=PMID:31358741 O15381 UniProtKB Mutagenesis 176 176 . . . Note=Impairs the binding of MTREX. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31358741;Dbxref=PMID:31358741 O15381 UniProtKB Mutagenesis 218 220 . . . Note=Decreased nuclear localization%3B when associated with 230-A--A-232. Complete loss of nuclear localization%3B when associated with 85-A-A-86 and 230-A--A-232. KRK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Mutagenesis 230 232 . . . Note=Decreased nuclear localization when associated with 218-A--A-220. Complete loss of nuclear localization%3B when associated with 85-A-A-86 and 218-A--A-220. RKK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469983;Dbxref=PMID:15469983 O15381 UniProtKB Mutagenesis 311 311 . . . Note=Loss of ATP-binding. Significant reduction in interaction with TERT and in telomerase activity. Loss of interaction with MTREX. K->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:16782053,ECO:0000269|PubMed:22226966,ECO:0000305|PubMed:22226966;Dbxref=PMID:16782053,PMID:22226966 O15381 UniProtKB Mutagenesis 365 365 . . . Note=Decreases 60S ribosomes synthesis. Strongly decreases 60S ribosomal subunit synthesis%2C enhances interaction with WDR74 and increases association of WDR74 and MTREX as well as induces partial migration of WDR74 to the nucleoplasm%3B when associated with Q-682. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26166824,ECO:0000269|PubMed:26456651;Dbxref=PMID:26166824,PMID:26456651 O15381 UniProtKB Mutagenesis 628 628 . . . Note=Loss of ATP-binding. No effect on interaction with TERT%2C MTREX and RPL5 and on telomerase activity. Significant reduction in the level of the 60S ribosomal subunit. K->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:15469983,ECO:0000269|PubMed:16782053,ECO:0000269|PubMed:22226966,ECO:0000269|PubMed:26166824,ECO:0000305|PubMed:22226966;Dbxref=PMID:15469983,PMID:16782053,PMID:22226966,PMID:26166824 O15381 UniProtKB Mutagenesis 682 682 . . . Note=Decreases 60S ribosomes synthesis. Strongly decreases 60S ribosomal subunit synthesis%2C enhances interaction with WDR74 and increases association of WDR74 and MTREX as well as induces partial migration of WDR74 to the nucleoplasm%3B when associated with Q-365. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26166824,ECO:0000269|PubMed:26456651;Dbxref=PMID:26166824,PMID:26456651 O15381 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6RO1 O15381 UniProtKB Helix 585 597 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 599 602 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 604 609 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Beta strand 616 623 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 628 638 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Beta strand 642 647 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Turn 648 651 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 657 672 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Beta strand 675 681 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Turn 684 686 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 701 710 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Beta strand 718 725 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 727 729 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 732 735 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Beta strand 742 745 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 751 761 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Turn 762 769 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 776 780 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 784 786 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 790 808 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A O15381 UniProtKB Helix 825 832 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2X8A