##gff-version 3 P13481 UniProtKB Chain 1 393 . . . ID=PRO_0000185697;Note=Cellular tumor antigen p53 P13481 UniProtKB DNA binding 102 292 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Region 1 320 . . . Note=Interaction with CCAR2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Region 1 83 . . . Note=Interaction with HRMT1L2;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 1 44 . . . Note=Transcription activation (acidic) P13481 UniProtKB Region 48 97 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Region 66 110 . . . Note=Interaction with WWOX;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 100 370 . . . Note=Interaction with HIPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 100 300 . . . Note=Required for interaction with ZNF385A;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 113 236 . . . Note=Required for interaction with FBXO42;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 116 292 . . . Note=Interaction with AXIN1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 256 294 . . . Note=Interaction with E4F1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 273 280 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 283 325 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Region 300 393 . . . Note=Interaction with CARM1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 319 360 . . . Note=Interaction with HIPK2;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 325 356 . . . Note=Oligomerization P13481 UniProtKB Region 352 393 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Region 359 363 . . . Note=Interaction with USP7;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Region 368 387 . . . Note=Basic (repression of DNA-binding) P13481 UniProtKB Motif 305 321 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Motif 339 350 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Motif 370 372 . . . Note=[KR]-[STA]-K motif P13481 UniProtKB Compositional bias 75 92 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Compositional bias 283 299 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Compositional bias 305 319 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Compositional bias 366 380 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P13481 UniProtKB Binding site 176 176 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Binding site 179 179 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Binding site 238 238 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Binding site 242 242 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Site 120 120 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine%3B by HIPK4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 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 P13481 UniProtKB Modified residue 18 18 . . . Note=Phosphothreonine%3B by CK1%2C VRK1 and VRK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine%3B by CHEK2%2C CK1 and PLK3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine%3B by CDK5 and CDK7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine%3B by MAPKAPK5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine%3B by CDK5%2C DYRK2%2C HIPK2 and PKC/PRKCG;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 55 55 . . . Note=Phosphothreonine%3B by TAF1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Modified residue 55 55 . . . Note=Phosphothreonine%3B by TAF1 and GRK5;Ontology_term=ECO:0000250;evidence=ECO:0000250 P13481 UniProtKB Modified residue 120 120 . . . Note=N6-acetyllysine%3B by KAT6A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 284 284 . . . Note=Phosphothreonine%3B by AURKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 305 305 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine%3B by AURKA%2C CDK1 and CDK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 321 321 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02340 P13481 UniProtKB Modified residue 333 333 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 335 335 . . . Note=Symmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 337 337 . . . Note=Symmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 370 370 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 370 370 . . . Note=N6-methyllysine%3B by SMYD2%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 372 372 . . . Note=N6-methyllysine%3B by SETD7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 373 373 . . . Note=N6%2CN6-dimethyllysine%3B by EHMT1 and EHMT2%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 373 373 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 381 381 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 382 382 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 382 382 . . . Note=N6-acetyllysine%3B by KAT6A%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 382 382 . . . Note=N6-methyllysine%3B by KMT5A%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine%3B by CK2%2C CDK2 and NUAK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 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 P13481 UniProtKB Cross-link 291 291 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Cross-link 292 292 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04637 P13481 UniProtKB Cross-link 386 386 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250