##gff-version 3 Q9JIH2 UniProtKB Chain 1 466 . . . ID=PRO_0000204869;Note=Nuclear pore complex protein Nup50 Q9JIH2 UniProtKB Repeat 76 77 . . . Note=1 Q9JIH2 UniProtKB Repeat 112 113 . . . Note=2 Q9JIH2 UniProtKB Repeat 225 226 . . . Note=3 Q9JIH2 UniProtKB Repeat 271 272 . . . Note=4 Q9JIH2 UniProtKB Repeat 301 302 . . . Note=5 Q9JIH2 UniProtKB Domain 333 466 . . . Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164 Q9JIH2 UniProtKB Region 1 22 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Region 76 302 . . . Note=5 X 2 AA repeats of F-G Q9JIH2 UniProtKB Region 128 150 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Region 143 205 . . . Note=Binding to CDKN1B Q9JIH2 UniProtKB Region 200 257 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Region 316 343 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Compositional bias 200 217 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Compositional bias 225 241 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Compositional bias 242 256 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9JIH2 UniProtKB Modified residue 8 8 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q9JIH2 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Modified residue 82 82 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Modified residue 126 126 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q9JIH2 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Modified residue 234 234 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9JIH2 UniProtKB Modified residue 246 246 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Modified residue 448 448 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q9JIH2 UniProtKB Cross-link 351 351 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UKX7 Q9JIH2 UniProtKB Sequence conflict 127 135 . . . Note=KISSPKCNN->VSNPKTNGD;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 158 158 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 314 314 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 321 321 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 324 324 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 439 441 . . . Note=LPA->IKV;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 451 451 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Sequence conflict 462 464 . . . Note=EKK->QKT;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9JIH2 UniProtKB Turn 12 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C1M Q9JIH2 UniProtKB Helix 32 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C1M