##gff-version 3 P54274 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231;Dbxref=PMID:19413330,PMID:20068231 P54274 UniProtKB Chain 2 439 . . . ID=PRO_0000197129;Note=Telomeric repeat-binding factor 1 P54274 UniProtKB Domain 375 432 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 P54274 UniProtKB DNA binding 403 428 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 P54274 UniProtKB Region 1 36 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Region 58 268 . . . Note=TRFH mediates dimerization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202258;Dbxref=PMID:18202258 P54274 UniProtKB Region 265 378 . . . Note=Interaction with RLIM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19164295;Dbxref=PMID:19164295 P54274 UniProtKB Region 266 311 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Region 326 375 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Motif 337 356 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P54274 UniProtKB Compositional bias 18 36 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Compositional bias 281 295 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Compositional bias 296 311 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Compositional bias 332 360 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P54274 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231;Dbxref=PMID:19413330,PMID:20068231 P54274 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:20068231,PMID:23186163 P54274 UniProtKB Modified residue 219 219 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11375976;Dbxref=PMID:11375976 P54274 UniProtKB Cross-link 213 213 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P54274 UniProtKB Cross-link 325 325 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P54274 UniProtKB Cross-link 366 366 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P54274 UniProtKB Alternative sequence 296 315 . . . ID=VSP_003303;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:9326950,ECO:0000303|PubMed:9391075;Dbxref=PMID:15489334,PMID:9326950,PMID:9391075 P54274 UniProtKB Mutagenesis 74 74 . . . Note=Abolishes dimerization and telomere binding%3B when associated with P-75. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11545737;Dbxref=PMID:11545737 P54274 UniProtKB Mutagenesis 75 75 . . . Note=Abolishes dimerization and telomere binding%3B when associated with D-74. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11545737;Dbxref=PMID:11545737 P54274 UniProtKB Mutagenesis 77 77 . . . Note=Abolishes telomere binding. W->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11545737;Dbxref=PMID:11545737 P54274 UniProtKB Mutagenesis 81 81 . . . Note=Abolishes telomere binding. F->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11545737;Dbxref=PMID:11545737 P54274 UniProtKB Mutagenesis 90 90 . . . Note=Diminishes telomere binding. F->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11545737;Dbxref=PMID:11545737 P54274 UniProtKB Mutagenesis 115 115 . . . Note=Loss of interaction with FBXO4. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20159592;Dbxref=PMID:20159592 P54274 UniProtKB Mutagenesis 120 120 . . . Note=Loss of interaction with FBXO4. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20159592;Dbxref=PMID:20159592 P54274 UniProtKB Mutagenesis 219 219 . . . Note=Loss of phosphorylation%3B induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11375976;Dbxref=PMID:11375976 P54274 UniProtKB Mutagenesis 219 219 . . . Note=Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants). S->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11375976;Dbxref=PMID:11375976 P54274 UniProtKB Sequence conflict 14 14 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P54274 UniProtKB Sequence conflict 338 338 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P54274 UniProtKB Helix 63 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Helix 95 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L82 P54274 UniProtKB Helix 117 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Beta strand 143 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Helix 150 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Helix 167 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Helix 190 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Beta strand 203 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L82 P54274 UniProtKB Helix 211 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Helix 226 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Helix 233 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Beta strand 252 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1H6O P54274 UniProtKB Helix 255 265 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BQO P54274 UniProtKB Beta strand 377 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ITY P54274 UniProtKB Helix 385 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1W0T P54274 UniProtKB Helix 403 409 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1W0T P54274 UniProtKB Beta strand 410 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0A P54274 UniProtKB Helix 417 428 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1W0T