##gff-version 3 O14578 UniProtKB Chain 1 2027 . . . ID=PRO_0000085908;Note=Citron Rho-interacting kinase O14578 UniProtKB Domain 97 360 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O14578 UniProtKB Domain 361 431 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 O14578 UniProtKB Domain 1443 1563 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 O14578 UniProtKB Domain 1591 1881 . . . Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795 O14578 UniProtKB Zinc finger 1362 1411 . . . Note=Phorbol-ester/DAG-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 O14578 UniProtKB Region 1091 1302 . . . Note=Interaction with Rho/Rac O14578 UniProtKB Region 1290 1310 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14578 UniProtKB Region 1322 1351 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14578 UniProtKB Region 1905 2012 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14578 UniProtKB Coiled coil 453 1297 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O14578 UniProtKB Motif 1953 1958 . . . Note=SH3-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14578 UniProtKB Compositional bias 1913 1927 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14578 UniProtKB Compositional bias 1951 1999 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14578 UniProtKB Active site 221 221 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 O14578 UniProtKB Binding site 103 111 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O14578 UniProtKB Binding site 126 126 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O14578 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 O14578 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:19690332,PMID:23186163 O14578 UniProtKB Modified residue 440 440 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 O14578 UniProtKB Modified residue 480 480 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O14578 UniProtKB Modified residue 582 582 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O14578 UniProtKB Modified residue 1196 1196 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49025 O14578 UniProtKB Modified residue 1721 1721 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 O14578 UniProtKB Modified residue 1940 1940 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O14578 UniProtKB Modified residue 1993 1993 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O14578 UniProtKB Modified residue 2013 2013 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O14578 UniProtKB Alternative sequence 1 467 . . . ID=VSP_014507;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10231032;Dbxref=PMID:10231032 O14578 UniProtKB Alternative sequence 481 482 . . . ID=VSP_012434;Note=In isoform 2. EV->GG;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 O14578 UniProtKB Alternative sequence 483 2027 . . . ID=VSP_012435;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 O14578 UniProtKB Alternative sequence 694 694 . . . ID=VSP_043301;Note=In isoform 4. E->EERRHSLENKVKRLETMERRENRLKDDIQTKSQQIQQMADKIL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15983625;Dbxref=PMID:15983625 O14578 UniProtKB Alternative sequence 1239 1253 . . . ID=VSP_014508;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10231032;Dbxref=PMID:10231032 O14578 UniProtKB Alternative sequence 1919 1919 . . . ID=VSP_014509;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10231032;Dbxref=PMID:10231032 O14578 UniProtKB Natural variant 7 7 . . . ID=VAR_040417;Note=G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs36054900,PMID:17344846 O14578 UniProtKB Natural variant 9 9 . . . ID=VAR_040418;Note=R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56193743,PMID:17344846 O14578 UniProtKB Natural variant 106 106 . . . ID=VAR_077442;Note=In MCPH17%3B impairs kinase activity%3B exhibits abnormal mitotic cytokinesis%3B exhibits multipolar spindles%3B increases the neurons apoptotic process. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27453578;Dbxref=dbSNP:rs886037892,PMID:27453578 O14578 UniProtKB Natural variant 126 126 . . . ID=VAR_077443;Note=In MCPH17%3B impairs kinase activity%3B exhibits abnormal mitotic cytokinesis%3B exhibits multipolar spindles%3B increases the neurons apoptotic process. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27453578;Dbxref=dbSNP:rs886037893,PMID:27453578 O14578 UniProtKB Natural variant 183 183 . . . ID=VAR_040419;Note=L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 O14578 UniProtKB Natural variant 230 230 . . . ID=VAR_077444;Note=In MCPH17%3B impairs kinase activity%3B exhibits abnormal mitotic cytokinesis%3B exhibits multipolar spindles%3B increases the neurons apoptotic process. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27453578;Dbxref=dbSNP:rs886037894,PMID:27453578 O14578 UniProtKB Sequence conflict 12 12 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14578 UniProtKB Sequence conflict 56 56 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14578 UniProtKB Sequence conflict 218 218 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305