##gff-version 3 P53668 UniProtKB Chain 1 647 . . . ID=PRO_0000075804;Note=LIM domain kinase 1 P53668 UniProtKB Domain 25 75 . . . Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 P53668 UniProtKB Domain 84 137 . . . Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 P53668 UniProtKB Domain 165 258 . . . Note=PDZ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00143 P53668 UniProtKB Domain 339 604 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P53668 UniProtKB Region 256 319 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53668 UniProtKB Compositional bias 272 317 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P53668 UniProtKB Active site 460 460 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P53668 UniProtKB Binding site 345 353 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P53668 UniProtKB Binding site 368 368 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P53668 UniProtKB Modified residue 210 210 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P53668 UniProtKB Modified residue 229 229 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53667 P53668 UniProtKB Modified residue 298 298 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P53668 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53667 P53668 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53667 P53668 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P53668 UniProtKB Modified residue 323 323 . . . Note=Phosphoserine%3B by MAPKAPK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53667 P53668 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53667 P53668 UniProtKB Modified residue 508 508 . . . Note=Phosphothreonine%3B by ROCK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25107909;Dbxref=PMID:25107909 P53668 UniProtKB Mutagenesis 460 460 . . . Note=Abrogates kinase activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15056216;Dbxref=PMID:15056216 P53668 UniProtKB Sequence conflict 200 201 . . . Note=RV->EC;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53668 UniProtKB Sequence conflict 269 271 . . . Note=DPS->GSQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53668 UniProtKB Sequence conflict 326 327 . . . Note=VV->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 P53668 UniProtKB Sequence conflict 523 523 . . . Note=G->P;Ontology_term=ECO:0000305;evidence=ECO:0000305