##gff-version 3 Q01196 UniProtKB Chain 1 453 . . . ID=PRO_0000174655;Note=Runt-related transcription factor 1 Q01196 UniProtKB Domain 50 178 . . . Note=Runt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00399 Q01196 UniProtKB Region 1 26 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Region 80 84 . . . Note=Interaction with DNA Q01196 UniProtKB Region 135 143 . . . Note=Interaction with DNA Q01196 UniProtKB Region 168 177 . . . Note=Interaction with DNA Q01196 UniProtKB Region 171 195 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Region 209 252 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Region 291 371 . . . Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742995;Dbxref=PMID:11742995 Q01196 UniProtKB Region 307 400 . . . Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01196 UniProtKB Region 362 402 . . . Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17377532;Dbxref=PMID:17377532 Q01196 UniProtKB Region 404 445 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Compositional bias 171 186 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Compositional bias 222 252 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Compositional bias 404 441 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01196 UniProtKB Binding site 112 112 . . . . Q01196 UniProtKB Binding site 116 116 . . . . Q01196 UniProtKB Binding site 139 139 . . . . Q01196 UniProtKB Binding site 170 170 . . . . Q01196 UniProtKB Site 177 178 . . . Note=Breakpoint for translocation to form AML1-EMV-1 (or AML1-EAP) in CML and T-MDS%2C to form AML1-MTG8 (ETO) in AML-M2%2C to form AML1-CBFA2T3 in therapy-related myeloid malignancies%2C to form AML1-MECOM in CML and to form type I MACROD1-RUNX1 fusion protein Q01196 UniProtKB Site 241 242 . . . Note=Breakpoint for translocation to form AML1-EAP in T-MDS and CML%2C to form type II MACROD1-RUNX1 fusion protein and to form RUNX1-CBFA2T2 in acute myeloid leukemia;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20520637;Dbxref=PMID:20520637 Q01196 UniProtKB Modified residue 14 14 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:23186163 Q01196 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q01196 UniProtKB Modified residue 24 24 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q01196 UniProtKB Modified residue 43 43 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q01196 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q01196 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:23186163,PMID:24275569 Q01196 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine%3B by HIPK2;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18695000,ECO:0007744|PubMed:19690332;Dbxref=PMID:18695000,PMID:19690332 Q01196 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q01196 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q01196 UniProtKB Modified residue 273 273 . . . Note=Phosphothreonine%3B by HIPK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18695000;Dbxref=PMID:18695000 Q01196 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine%3B by HIPK2;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18695000,ECO:0007744|PubMed:19690332;Dbxref=PMID:18695000,PMID:19690332 Q01196 UniProtKB Modified residue 296 296 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q01196 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01196 UniProtKB Alternative sequence 1 105 . . . ID=VSP_005919;Note=In isoform AML-1L. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7651838,ECO:0000303|PubMed:9199349;Dbxref=PMID:7651838,PMID:9199349 Q01196 UniProtKB Alternative sequence 1 5 . . . ID=VSP_005917;Note=In isoform AML-1G. MRIPV->MASDSIFESFPSYPQCFMRECILGMNPSRDVH;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:7651838,ECO:0000303|PubMed:7891692;Dbxref=PMID:15489334,PMID:7651838,PMID:7891692 Q01196 UniProtKB Alternative sequence 1 5 . . . ID=VSP_005916;Note=In isoform AML-1H. MRIPV->MNPSRDVH;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 1 5 . . . ID=VSP_005918;Note=In isoform AML-1I. MRIPV->MPAAPRGPAQGEAAARTRSR;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 137 242 . . . ID=VSP_005920;Note=In isoform AML-1FC. VGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQD->VDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPI;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 178 224 . . . ID=VSP_005923;Note=In isoform AML-1FA. RHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRA->SKCIHLGLVHPPGWYTLQAGILRDHVSDSLGSTFPPGGWQAPVKPKS;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 178 188 . . . ID=VSP_005921;Note=In isoform AML-1FB. RHRQKLDDQTK->NSLTWPRYPHI;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 189 453 . . . ID=VSP_005922;Note=In isoform AML-1FB. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 225 453 . . . ID=VSP_005924;Note=In isoform AML-1FA. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 242 250 . . . ID=VSP_005926;Note=In isoform AML-1C. DTRQIQPSP->EEDTAPWRC;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1720541;Dbxref=PMID:1720541 Q01196 UniProtKB Alternative sequence 243 453 . . . ID=VSP_005925;Note=In isoform AML-1FC. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Alternative sequence 251 453 . . . ID=VSP_005927;Note=In isoform AML-1C. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1720541;Dbxref=PMID:1720541 Q01196 UniProtKB Alternative sequence 258 453 . . . ID=VSP_005928;Note=In isoform AML-1E. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8490181;Dbxref=PMID:8490181 Q01196 UniProtKB Alternative sequence 440 453 . . . ID=VSP_005929;Note=In isoform AML-1A. APSARLEEAVWRPY->GGASCSRQARRDPGPWARTPSWGRGRPTDRISL;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7651838,ECO:0000303|PubMed:7835892;Dbxref=PMID:7651838,PMID:7835892 Q01196 UniProtKB Natural variant 139 139 . . . ID=VAR_012128;Note=In FPDMM. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508512;Dbxref=dbSNP:rs1060499616,PMID:10508512 Q01196 UniProtKB Natural variant 174 174 . . . ID=VAR_012129;Note=In FPDMM%3B impaired phosphorylation. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10508512,ECO:0000269|PubMed:18695000;Dbxref=dbSNP:rs74315450,PMID:10508512,PMID:18695000 Q01196 UniProtKB Natural variant 431 431 . . . ID=VAR_013177;Note=S->R;Dbxref=dbSNP:rs1055308 Q01196 UniProtKB Natural variant 433 433 . . . ID=VAR_013178;Note=S->R;Dbxref=dbSNP:rs1055309 Q01196 UniProtKB Mutagenesis 67 67 . . . Note=Loss of heterodimerization and reduced EP300 phosphorylation induction. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18695000;Dbxref=PMID:18695000 Q01196 UniProtKB Mutagenesis 80 80 . . . Note=Strongly reduces DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 83 83 . . . Note=Strongly reduces DNA-binding. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11276260,ECO:0000269|PubMed:18695000;Dbxref=PMID:11276260,PMID:18695000 Q01196 UniProtKB Mutagenesis 83 83 . . . Note=Strongly reduces DNA-binding%2C impaired phosphorylation and reduced EP300 phosphorylation induction. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11276260,ECO:0000269|PubMed:18695000;Dbxref=PMID:11276260,PMID:18695000 Q01196 UniProtKB Mutagenesis 84 84 . . . Note=No effect on DNA binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 106 106 . . . Note=Disrupts interaction of AML1-MTG8/ETO with CBFB%2C no effect on AML1-MTG8/ETO-mediated transformation activity. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19202074;Dbxref=PMID:19202074 Q01196 UniProtKB Mutagenesis 107 107 . . . Note=Loss of heterodimerization. Disrupts interactionof AML1-MTG8/ETO with CBFB%2C no effect on AML1-MTG8/ETO-mediated transformation activity. A->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10404214,ECO:0000269|PubMed:19202074;Dbxref=PMID:10404214,PMID:19202074 Q01196 UniProtKB Mutagenesis 108 108 . . . Note=Loss of heterodimerization and impaired phosphorylation. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10404214,ECO:0000269|PubMed:18695000;Dbxref=PMID:10404214,PMID:18695000 Q01196 UniProtKB Mutagenesis 135 135 . . . Note=Strongly reduces DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 139 139 . . . Note=Strongly reduces DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 140 140 . . . Note=Disrupts AML1-MTG8/ETODNA-binding%2C decreases AML1-MTG8/ETO transforming activity. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19202074;Dbxref=PMID:19202074 Q01196 UniProtKB Mutagenesis 142 142 . . . Note=Strongly reduces DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 145 453 . . . Note=No DNA-binding. Missing Q01196 UniProtKB Mutagenesis 167 167 . . . Note=Reduces DNA-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 169 169 . . . Note=Strongly reduces DNA-binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 171 171 . . . Note=Strongly reduces DNA-binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 174 174 . . . Note=Strongly reduces DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 177 177 . . . Note=Strongly reduces DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11276260;Dbxref=PMID:11276260 Q01196 UniProtKB Mutagenesis 249 249 . . . Note=Reduced phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18695000;Dbxref=PMID:18695000 Q01196 UniProtKB Mutagenesis 273 273 . . . Note=Reduced phosphorylation%3B when associated with A-276. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18695000;Dbxref=PMID:18695000 Q01196 UniProtKB Mutagenesis 276 276 . . . Note=Reduced phosphorylation%3B when associated with A-273. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18695000;Dbxref=PMID:18695000 Q01196 UniProtKB Sequence conflict 412 412 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01196 UniProtKB Helix 54 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CMO Q01196 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 70 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CMO Q01196 UniProtKB Beta strand 90 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 102 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1H9D Q01196 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 146 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 154 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1E50 Q01196 UniProtKB Beta strand 158 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LJM Q01196 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CMO