##gff-version 3 P51617 UniProtKB Chain 1 712 . . . ID=PRO_0000086030;Note=Interleukin-1 receptor-associated kinase 1 P51617 UniProtKB Domain 27 106 . . . Note=Death P51617 UniProtKB Domain 212 521 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P51617 UniProtKB Region 105 187 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Region 110 211 . . . Note=ProST region P51617 UniProtKB Region 532 591 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Region 613 660 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Region 690 712 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Compositional bias 134 151 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Compositional bias 163 179 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Compositional bias 538 556 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Compositional bias 572 590 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Compositional bias 646 660 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51617 UniProtKB Active site 340 340 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P51617 UniProtKB Binding site 218 226 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P51617 UniProtKB Binding site 239 239 . . . . P51617 UniProtKB Binding site 342 345 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P51617 UniProtKB Binding site 358 358 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P51617 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine%3B by PKC/PRKCI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684752;Dbxref=PMID:14684752 P51617 UniProtKB Modified residue 131 131 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 P51617 UniProtKB Modified residue 209 209 . . . Note=Phosphothreonine%3B by IRAK4;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14625308;Dbxref=PMID:14625308 P51617 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P51617 UniProtKB Modified residue 375 375 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P51617 UniProtKB Modified residue 387 387 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14625308;Dbxref=PMID:14625308 P51617 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P51617 UniProtKB Cross-link 134 134 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18347055;Dbxref=PMID:18347055 P51617 UniProtKB Cross-link 180 180 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18347055;Dbxref=PMID:18347055 P51617 UniProtKB Alternative sequence 45 45 . . . ID=VSP_011849;Note=In isoform 3. F->FGGWRRAAGGREARGLLAPTPDAPRPA;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P51617 UniProtKB Alternative sequence 435 513 . . . ID=VSP_041950;Note=In isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16024789;Dbxref=PMID:15489334,PMID:16024789 P51617 UniProtKB Alternative sequence 478 492 . . . ID=VSP_011850;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P51617 UniProtKB Alternative sequence 513 542 . . . ID=VSP_011851;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11397809,ECO:0000303|PubMed:15489334;Dbxref=PMID:11397809,PMID:15489334 P51617 UniProtKB Natural variant 194 194 . . . ID=VAR_051629;Note=R->H;Dbxref=dbSNP:rs11465830 P51617 UniProtKB Natural variant 196 196 . . . ID=VAR_051630;Note=F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8599092;Dbxref=dbSNP:rs1059702,PMID:8599092 P51617 UniProtKB Natural variant 203 203 . . . ID=VAR_051631;Note=C->S;Dbxref=dbSNP:rs10127175 P51617 UniProtKB Natural variant 398 398 . . . ID=VAR_040573;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56340948,PMID:17344846 P51617 UniProtKB Natural variant 412 412 . . . ID=VAR_040574;Note=In a glioblastoma multiforme sample%3B somatic mutation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P51617 UniProtKB Natural variant 421 421 . . . ID=VAR_040575;Note=In a breast pleomorphic lobular carcinoma sample%3B somatic mutation. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P51617 UniProtKB Natural variant 532 532 . . . ID=VAR_040576;Note=S->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17344846,ECO:0000269|PubMed:8599092;Dbxref=dbSNP:rs1059703,PMID:17344846,PMID:8599092 P51617 UniProtKB Natural variant 619 619 . . . ID=VAR_040577;Note=G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34112487,PMID:17344846 P51617 UniProtKB Natural variant 625 625 . . . ID=VAR_040578;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35638718,PMID:17344846 P51617 UniProtKB Natural variant 638 638 . . . ID=VAR_040579;Note=R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56082801,PMID:17344846 P51617 UniProtKB Natural variant 690 690 . . . ID=VAR_040580;Note=In a lung adenocarcinoma sample%3B somatic mutation. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P51617 UniProtKB Mutagenesis 209 209 . . . Note=Completely abolishes auto-phosphorylation in the kinase domain. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14625308;Dbxref=PMID:14625308 P51617 UniProtKB Mutagenesis 239 239 . . . Note=Loss of kinase activity. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15084582;Dbxref=PMID:15084582 P51617 UniProtKB Mutagenesis 340 340 . . . Note=Loss of kinase activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18691762;Dbxref=PMID:18691762 P51617 UniProtKB Mutagenesis 387 387 . . . Note=Loss of kinase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14625308;Dbxref=PMID:14625308 P51617 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 202 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 217 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 222 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 234 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 249 265 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 274 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 283 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 296 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 304 307 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 312 331 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 332 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 345 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 354 356 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 393 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 403 419 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 423 427 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Beta strand 430 433 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 434 436 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 437 445 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 464 466 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 467 476 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 487 500 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 505 507 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 511 521 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN P51617 UniProtKB Helix 522 524 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BFN