##gff-version 3 P53349 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Chain 2 1493 . . . ID=PRO_0000086241;Note=Mitogen-activated protein kinase kinase kinase 1 P53349 UniProtKB Domain 1224 1489 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P53349 UniProtKB Zinc finger 333 361 . . . Note=SWIM-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00325 P53349 UniProtKB Zinc finger 438 487 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 P53349 UniProtKB Region 1 178 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Region 194 300 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Region 411 431 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Region 506 531 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Region 895 914 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Region 927 957 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Region 992 1066 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 53 74 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 159 178 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 411 427 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 927 942 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 995 1010 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 1020 1035 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Compositional bias 1051 1066 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53349 UniProtKB Active site 1350 1350 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P53349 UniProtKB Binding site 1230 1238 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P53349 UniProtKB Binding site 1253 1253 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P53349 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19144319,ECO:0007744|PubMed:21183079;Dbxref=PMID:19144319,PMID:21183079 P53349 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 280 280 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 287 287 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P53349 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 295 295 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 526 526 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 915 915 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 999 999 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 1024 1024 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13233 P53349 UniProtKB Modified residue 1381 1381 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9078260;Dbxref=PMID:9078260 P53349 UniProtKB Modified residue 1393 1393 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9078260;Dbxref=PMID:9078260 P53349 UniProtKB Mutagenesis 1381 1381 . . . Note=Fails to activate MAP2K1%2C MAP2K4%2C MAP2K7%2C CHUK and IKBKB. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14500727,ECO:0000269|PubMed:9078260;Dbxref=PMID:14500727,PMID:9078260 P53349 UniProtKB Mutagenesis 1381 1381 . . . Note=Loss of kinase activity and autophosphorylation. T->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14500727,ECO:0000269|PubMed:9078260;Dbxref=PMID:14500727,PMID:9078260 P53349 UniProtKB Mutagenesis 1381 1381 . . . Note=Reduced kinase activity and autophosphorylation. T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14500727,ECO:0000269|PubMed:9078260;Dbxref=PMID:14500727,PMID:9078260 P53349 UniProtKB Mutagenesis 1393 1393 . . . Note=Loss of kinase activity and autophosphorylation. Fails to activate MAP2K1%2C MAP2K4%2C MAP2K7%2C CHUK and IKBKB. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14500727,ECO:0000269|PubMed:9078260;Dbxref=PMID:14500727,PMID:9078260 P53349 UniProtKB Mutagenesis 1393 1393 . . . Note=Loss of kinase activity and autophosphorylation. T->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14500727,ECO:0000269|PubMed:9078260;Dbxref=PMID:14500727,PMID:9078260 P53349 UniProtKB Mutagenesis 1393 1393 . . . Note=Reduced kinase activity and autophosphorylation. T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14500727,ECO:0000269|PubMed:9078260;Dbxref=PMID:14500727,PMID:9078260 P53349 UniProtKB Mutagenesis 1394 1394 . . . Note=Loss of NF-kappa-B transcription factor activity and reduced ability to activate MAP2K1%2C MAP2K4%2C MAP2K7. No effect on AP-1 activity or activation of CHUK and IKBKB. Loss of binding to IKBKB. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Mutagenesis 1396 1396 . . . Note=Loss of AP-1 and NF-kappa-B transcription factor activity. Reduced ability to activate MAP2K1%2C MAP2K4%2C MAP2K7%2C CHUK and IKBKB. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Mutagenesis 1397 1397 . . . Note=Loss of AP-1 and NF-kappa-B transcription factor activity. Reduced ability to activate MAP2K1%2C MAP2K4%2C MAP2K7%2C CHUK and IKBKB. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Mutagenesis 1401 1401 . . . Note=Loss of AP-1 and NF-kappa-B transcription factor activity. Reduced ability to activate MAP2K1%2C MAP2K4%2C MAP2K7%2C CHUK and IKBKB. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Mutagenesis 1402 1402 . . . Note=Loss of AP-1 transcription factor activity and reduced ability to activate CHUK and IKBKB. No effect on NF-kappa-B activity or activation of MAP2K1%2C MAP2K4%2C MAP2K7. Loss of binding to MAP2K4. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Mutagenesis 1403 1403 . . . Note=Loss of AP-1 transcription factor activity%2C no effect on NF-kappa-B activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Mutagenesis 1404 1404 . . . Note=Loss of AP-1 and NF-kappa-B transcription factor activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500727;Dbxref=PMID:14500727 P53349 UniProtKB Sequence conflict 30 39 . . . Note=GGGALQGSGA->ALQGSG;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 103 103 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 257 257 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 307 307 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 413 413 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 559 559 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 883 883 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53349 UniProtKB Sequence conflict 1467 1467 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305