##gff-version 3 P10361 UniProtKB Chain 1 391 . . . ID=PRO_0000185712;Note=Cellular tumor antigen p53 P10361 UniProtKB DNA binding 100 290 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Region 1 318 . . . Note=Interaction with CCAR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Region 1 47 . . . Note=Transcription activation (acidic) P10361 UniProtKB Region 64 108 . . . Note=Interaction with WWOX;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 65 90 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10361 UniProtKB Region 98 368 . . . Note=Interaction with HIPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 98 298 . . . Note=Required for interaction with ZNF385A;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 111 234 . . . Note=Required for interaction with FBXO42;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 114 290 . . . Note=Interaction with AXIN1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 254 292 . . . Note=Interaction with E4F1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 271 278 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 281 324 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10361 UniProtKB Region 317 358 . . . Note=Interaction with HIPK2;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 323 354 . . . Note=Oligomerization P10361 UniProtKB Region 350 391 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10361 UniProtKB Region 357 361 . . . Note=Interaction with USP7;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Region 366 385 . . . Note=Basic (repression of DNA-binding) P10361 UniProtKB Motif 303 319 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Motif 337 348 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Motif 368 370 . . . Note=[KR]-[STA]-K motif P10361 UniProtKB Compositional bias 281 298 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10361 UniProtKB Compositional bias 304 318 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10361 UniProtKB Compositional bias 350 366 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10361 UniProtKB Binding site 174 174 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Binding site 177 177 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Binding site 236 236 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Binding site 240 240 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Site 118 118 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine%3B by HIPK4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine%3B by CDK5%2C PRPK%2C AMPK%2C NUAK1 and ATM;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 18 18 . . . Note=Phosphothreonine%3B by CK1%2C VRK1 and VRK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine%3B by CHEK2%2C CK1 and PLK3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine%3B by MAPKAPK5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 118 118 . . . Note=N6-acetyllysine%3B by KAT6A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 282 282 . . . Note=Phosphothreonine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 303 303 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine%3B by AURKA%2C CDK1 and CDK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 319 319 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02340 P10361 UniProtKB Modified residue 331 331 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 333 333 . . . Note=Symmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 335 335 . . . Note=Symmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 368 368 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 368 368 . . . Note=N6-methyllysine%3B by SMYD2%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 370 370 . . . Note=N6-methyllysine%3B by SETD7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 371 371 . . . Note=N6%2CN6-dimethyllysine%3B by EHMT1 and EHMT2%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 371 371 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 379 379 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 380 380 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 380 380 . . . Note=N6-acetyllysine%3B by KAT6A%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 380 380 . . . Note=N6-methyllysine%3B by KMT5A%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Modified residue 390 390 . . . Note=Phosphoserine%3B by CK2%2C CDK2 and NUAK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Cross-link 24 24 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Cross-link 289 289 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Cross-link 290 290 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P10361 UniProtKB Cross-link 384 384 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250 P10361 UniProtKB Natural variant 103 103 . . . Note=G->S P10361 UniProtKB Natural variant 256 256 . . . Note=E->G P10361 UniProtKB Sequence conflict 174 174 . . . Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305