##gff-version 3 Q95UN8 UniProtKB Chain 1 1161 . . . ID=PRO_0000086269;Note=Mitogen-activated protein kinase kinase kinase Q95UN8 UniProtKB Domain 56 120 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 Q95UN8 UniProtKB Domain 142 402 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q95UN8 UniProtKB Region 426 447 . . . Note=Leucine-zipper 1 Q95UN8 UniProtKB Region 461 482 . . . Note=Leucine-zipper 2 Q95UN8 UniProtKB Region 560 615 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Region 658 678 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Region 790 830 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Region 988 1014 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Region 1045 1093 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Region 1137 1161 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Compositional bias 560 602 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Compositional bias 806 830 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Compositional bias 1062 1090 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q95UN8 UniProtKB Active site 264 264 . . . Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q02779,ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q95UN8 UniProtKB Binding site 148 156 . . . Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q02779,ECO:0000255|PROSITE-ProRule:PRU00159 Q95UN8 UniProtKB Binding site 169 169 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:12504027;Dbxref=PMID:12504027 Q95UN8 UniProtKB Modified residue 300 300 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q95UN8 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q95UN8 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897 Q95UN8 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16584 Q95UN8 UniProtKB Modified residue 685 685 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16584 Q95UN8 UniProtKB Modified residue 773 773 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16584 Q95UN8 UniProtKB Modified residue 792 792 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16584 Q95UN8 UniProtKB Modified residue 862 862 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897 Q95UN8 UniProtKB Modified residue 993 993 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16584 Q95UN8 UniProtKB Mutagenesis 169 169 . . . Note=Loss of kinase activity. Attenuates bsk activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504027;Dbxref=PMID:12504027 Q95UN8 UniProtKB Sequence conflict 327 327 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q95UN8 UniProtKB Sequence conflict 670 670 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q95UN8 UniProtKB Sequence conflict 908 908 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305