##gff-version 3 Q53EL6 UniProtKB Chain 1 469 . . . ID=PRO_0000256519;Note=Programmed cell death protein 4 Q53EL6 UniProtKB Domain 163 284 . . . Note=MI 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698 Q53EL6 UniProtKB Domain 326 449 . . . Note=MI 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698 Q53EL6 UniProtKB Region 1 38 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53EL6 UniProtKB Region 58 128 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53EL6 UniProtKB Motif 58 64 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q53EL6 UniProtKB Motif 70 76 . . . Note=Phosphodegron Q53EL6 UniProtKB Motif 241 250 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q53EL6 UniProtKB Compositional bias 11 27 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53EL6 UniProtKB Compositional bias 73 89 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53EL6 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q53EL6 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JID1 Q53EL6 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine%3B by PKB and RPS6KB1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16357133,ECO:0000269|PubMed:17053147,ECO:0007744|PubMed:24275569;Dbxref=PMID:16357133,PMID:17053147,PMID:24275569 Q53EL6 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q53EL6 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:23186163,PMID:24275569 Q53EL6 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163,PMID:24275569 Q53EL6 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163,PMID:24275569 Q53EL6 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q53EL6 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q53EL6 UniProtKB Modified residue 152 152 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:15592455;Dbxref=PMID:15592455 Q53EL6 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:23186163,PMID:24275569 Q53EL6 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:23186163,PMID:24275569 Q53EL6 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine%3B by PKB;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16357133,ECO:0007744|PubMed:15144186,ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:15144186,PMID:16357133,PMID:16964243,PMID:17081983,PMID:20068231,PMID:21406692,PMID:23186163 Q53EL6 UniProtKB Alternative sequence 1 15 . . . ID=VSP_045622;Note=In isoform 2. MDVENEQILNVNPAD->MTKY;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q53EL6 UniProtKB Natural variant 36 36 . . . ID=VAR_028901;Note=I->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:9759869,ECO:0000269|Ref.1,ECO:0000269|Ref.4,ECO:0007744|PubMed:20068231;Dbxref=dbSNP:rs7081726,PMID:14702039,PMID:15489334,PMID:20068231,PMID:9759869 Q53EL6 UniProtKB Natural variant 48 48 . . . ID=VAR_028902;Note=S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs11548765,PMID:15489334 Q53EL6 UniProtKB Natural variant 120 120 . . . ID=VAR_036375;Note=In a breast cancer sample%3B somatic mutation. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q53EL6 UniProtKB Mutagenesis 67 67 . . . Note=Loss of phosphorylation site. Reduces interaction with BTRC. Abolishes phosphorylation by PKB%3B when associated with A-457. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16357133,ECO:0000269|PubMed:17053147;Dbxref=PMID:16357133,PMID:17053147 Q53EL6 UniProtKB Mutagenesis 71 71 . . . Note=Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17053147;Dbxref=PMID:17053147 Q53EL6 UniProtKB Mutagenesis 76 76 . . . Note=Strongly reduced interaction with BTRC. Strongly reduced ubiquitination. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17053147;Dbxref=PMID:17053147 Q53EL6 UniProtKB Mutagenesis 174 174 . . . Note=Reduced inhibition of EIF4A1 helicase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 210 210 . . . Note=Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 249 249 . . . Note=Reduced interaction with EIF4A1. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 252 252 . . . Note=Strongly reduced interaction with EIF4A1. Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 253 253 . . . Note=Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Reduced inhibition of EIF4A1 helicase activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19153607,ECO:0000269|PubMed:19204291;Dbxref=PMID:19153607,PMID:19204291 Q53EL6 UniProtKB Mutagenesis 255 255 . . . Note=Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 333 333 . . . Note=No effect on inhibition of EIF4A1 and on inhibition of translation%3B when associated with A-340. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19204291;Dbxref=PMID:19204291 Q53EL6 UniProtKB Mutagenesis 337 337 . . . Note=No effect on inhibition of EIF4A1 and on inhibition of translation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19204291;Dbxref=PMID:19204291 Q53EL6 UniProtKB Mutagenesis 340 340 . . . Note=No effect on inhibition of EIF4A1 and on inhibition of translation%3B when associated with A-333. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19204291;Dbxref=PMID:19204291 Q53EL6 UniProtKB Mutagenesis 358 358 . . . Note=Strongly reduced interaction with EIF4A1. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 359 359 . . . Note=Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19204291;Dbxref=PMID:19204291 Q53EL6 UniProtKB Mutagenesis 361 361 . . . Note=Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19204291;Dbxref=PMID:19204291 Q53EL6 UniProtKB Mutagenesis 414 414 . . . Note=Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 418 418 . . . Note=Reduced interaction with EIF4A1. Strongly reduced inhibition of translation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 420 420 . . . Note=Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19153607;Dbxref=PMID:19153607 Q53EL6 UniProtKB Mutagenesis 457 457 . . . Note=Loss of phosphorylation site%2C and loss of nuclear accumulation. Abolishes phosphorylation by PKB%3B when associated with A-67. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16357133;Dbxref=PMID:16357133 Q53EL6 UniProtKB Sequence conflict 79 79 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 102 102 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 130 130 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 220 220 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 222 222 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 309 309 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 314 314 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Sequence conflict 440 440 . . . Note=S->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53EL6 UniProtKB Helix 161 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 181 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 195 198 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 199 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 213 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Turn 227 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 233 253 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 257 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 278 281 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Turn 282 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Helix 289 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RG8 Q53EL6 UniProtKB Beta strand 308 313 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KZT Q53EL6 UniProtKB Helix 324 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 344 354 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 357 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 360 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 378 393 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 398 418 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 422 435 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6 Q53EL6 UniProtKB Helix 441 445 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZU6