##gff-version 3 Q16566 UniProtKB Chain 1 473 . . . ID=PRO_0000086106;Note=Calcium/calmodulin-dependent protein kinase type IV Q16566 UniProtKB Domain 46 300 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q16566 UniProtKB Region 305 321 . . . Note=Autoinhibitory domain Q16566 UniProtKB Region 306 323 . . . Note=PP2A-binding Q16566 UniProtKB Region 322 341 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q16566 UniProtKB Region 341 368 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16566 UniProtKB Region 445 473 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16566 UniProtKB Compositional bias 351 368 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16566 UniProtKB Active site 164 164 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q16566 UniProtKB Binding site 52 60 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q16566 UniProtKB Binding site 75 75 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q16566 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8702940;Dbxref=PMID:8702940 Q16566 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8702940;Dbxref=PMID:8702940 Q16566 UniProtKB Modified residue 200 200 . . . Note=Phosphothreonine%3B by CaMKK1 and CaMKK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15143065,ECO:0000269|PubMed:19506079,ECO:0000269|PubMed:8702940;Dbxref=PMID:15143065,PMID:19506079,PMID:8702940 Q16566 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13234 Q16566 UniProtKB Modified residue 341 341 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13234 Q16566 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q16566 UniProtKB Glycosylation 57 57 . . . Note=O-linked (GlcNAc) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Glycosylation 58 58 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Glycosylation 137 137 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Glycosylation 189 189 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Glycosylation 344 344 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Glycosylation 345 345 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Glycosylation 356 356 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Natural variant 150 150 . . . ID=VAR_040604;Note=In a lung adenocarcinoma sample%3B somatic mutation. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 Q16566 UniProtKB Natural variant 178 178 . . . ID=VAR_040605;Note=D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35548075,PMID:17344846 Q16566 UniProtKB Natural variant 465 465 . . . ID=VAR_040606;Note=Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56360861,PMID:17344846 Q16566 UniProtKB Natural variant 469 469 . . . ID=VAR_040607;Note=In a lung large cell carcinoma sample%3B somatic mutation. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs1239950009,PMID:17344846 Q16566 UniProtKB Mutagenesis 12 12 . . . Note=Loss of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8702940;Dbxref=PMID:8702940 Q16566 UniProtKB Mutagenesis 13 13 . . . Note=Loss of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8702940;Dbxref=PMID:8702940 Q16566 UniProtKB Mutagenesis 57 58 . . . Note=Loss of phosphorylation of CREB1. TS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Mutagenesis 75 75 . . . Note=Loss of activity%3B dominant negative form. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10617605;Dbxref=PMID:10617605 Q16566 UniProtKB Mutagenesis 189 189 . . . Note=Increases phosphorylation of CREB1 2-fold. Decreases total O-linked glycosylation 2-fold. Increases ATP-binding affinity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19506079;Dbxref=PMID:19506079 Q16566 UniProtKB Mutagenesis 200 200 . . . Note=Loss of activation by CaMKK1 or CaMKK2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8855261;Dbxref=PMID:8855261 Q16566 UniProtKB Mutagenesis 309 312 . . . Note=Fully active Ca2+/CaM-independent kinase%3B when associated with 320-A-A-321. HMDT->DEDD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961813;Dbxref=PMID:7961813 Q16566 UniProtKB Mutagenesis 320 321 . . . Note=Fully active Ca2+/CaM-independent kinase%3B when associated with 309-A--A-312. Loss of interaction with PPP2CA/PPP2CB. FN->DD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15143065,ECO:0000269|PubMed:7961813;Dbxref=PMID:15143065,PMID:7961813 Q16566 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 42 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 46 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 56 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Turn 66 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 71 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 91 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 111 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 126 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 138 157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 221 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 247 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Turn 263 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 271 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 285 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 291 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Turn 298 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O Q16566 UniProtKB Helix 311 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W4O