##gff-version 3 O54949 UniProtKB Chain 1 527 . . . ID=PRO_0000186337;Note=Serine/threonine-protein kinase NLK O54949 UniProtKB Domain 138 427 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O54949 UniProtKB Region 1 304 . . . Note=Required for interaction with TAB2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194509;Dbxref=PMID:20194509 O54949 UniProtKB Region 1 125 . . . Note=Sufficient for interaction with DAPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UBE8 O54949 UniProtKB Region 22 72 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O54949 UniProtKB Region 90 139 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O54949 UniProtKB Region 124 416 . . . Note=Sufficient for interaction with DAPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UBE8 O54949 UniProtKB Region 428 527 . . . Note=Required for homodimerization and kinase activation and localization to the nucleus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21118996;Dbxref=PMID:21118996 O54949 UniProtKB Region 434 527 . . . Note=Required for interaction with TAB2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194509;Dbxref=PMID:20194509 O54949 UniProtKB Motif 298 300 . . . Note=TQE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15082531,ECO:0000269|PubMed:21118996,ECO:0000269|PubMed:9448268;Dbxref=PMID:15082531,PMID:21118996,PMID:9448268 O54949 UniProtKB Compositional bias 25 53 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O54949 UniProtKB Active site 264 264 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 O54949 UniProtKB Binding site 144 152 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O54949 UniProtKB Binding site 167 167 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 O54949 UniProtKB Modified residue 298 298 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:21118996,ECO:0007744|PubMed:21183079;Dbxref=PMID:21118996,PMID:21183079 O54949 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UBE8 O54949 UniProtKB Mutagenesis 167 167 . . . Note=Abrogates kinase activity and autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce ubiquitination and degradation of LEF1 and repress canonical Wnt/beta-catenin signaling. Abrogates ability to induce MYB degradation%2C and reduces ability to repress MYBL1 and MYBL2. K->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391247,ECO:0000269|PubMed:12556497,ECO:0000269|PubMed:15082531,ECO:0000269|PubMed:16055500,ECO:0000269|PubMed:20118921,ECO:0000269|PubMed:20194509,ECO:0000269|PubMed:21118996,ECO:0000269|PubMed:9448268;Dbxref=PMID:10391247,PMID:12556497,PMID:15082531,PMID:16055500,PMID:20118921,PMID:20194509,PMID:21118996,PMID:9448268 O54949 UniProtKB Mutagenesis 298 298 . . . Note=Abrogates autophosphorylation. T->D%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15082531,ECO:0000269|PubMed:21118996,ECO:0000269|PubMed:9448268;Dbxref=PMID:15082531,PMID:21118996,PMID:9448268 O54949 UniProtKB Mutagenesis 298 298 . . . Note=Abrogates autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce MYB degradation. T->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15082531,ECO:0000269|PubMed:21118996,ECO:0000269|PubMed:9448268;Dbxref=PMID:15082531,PMID:21118996,PMID:9448268 O54949 UniProtKB Mutagenesis 437 437 . . . Note=Retains kinase activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391247,ECO:0000269|PubMed:21118996;Dbxref=PMID:10391247,PMID:21118996 O54949 UniProtKB Mutagenesis 437 437 . . . Note=Abrogates homodimerization and intermolecular autophosphorylation%2C with consequent loss of kinase activity. Loss of nuclear localization. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391247,ECO:0000269|PubMed:21118996;Dbxref=PMID:10391247,PMID:21118996 O54949 UniProtKB Sequence conflict 69 69 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305