##gff-version 3 O43293 UniProtKB Chain 1 454 . . . ID=PRO_0000085914;Note=Death-associated protein kinase 3 O43293 UniProtKB Domain 13 275 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O43293 UniProtKB Region 161 204 . . . Note=Activation segment;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96017 O43293 UniProtKB Region 427 441 . . . Note=Leucine-zipper;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9488481;Dbxref=PMID:9488481 O43293 UniProtKB Active site 139 139 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 O43293 UniProtKB Binding site 19 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O43293 UniProtKB Binding site 42 42 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 O43293 UniProtKB Binding site 94 94 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18239682,ECO:0007744|PDB:2J90;Dbxref=PMID:18239682 O43293 UniProtKB Binding site 96 96 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18239682,ECO:0007744|PDB:2J90;Dbxref=PMID:18239682 O43293 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18239682;Dbxref=PMID:18239682 O43293 UniProtKB Modified residue 180 180 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15611134,ECO:0000269|PubMed:17158456;Dbxref=PMID:15611134,PMID:17158456 O43293 UniProtKB Modified residue 225 225 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Modified residue 265 265 . . . Note=Phosphothreonine%3B by autocatalysis and ROCK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15611134,ECO:0000269|PubMed:17158456,ECO:0000269|PubMed:18239682;Dbxref=PMID:15611134,PMID:17158456,PMID:18239682 O43293 UniProtKB Modified residue 299 299 . . . Note=Phosphothreonine%3B by autocatalysis%2C DAPK1 and ROCK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15367680,ECO:0000269|PubMed:15611134,ECO:0000269|PubMed:17158456,ECO:0000269|PubMed:20854903;Dbxref=PMID:15367680,PMID:15611134,PMID:17158456,PMID:20854903 O43293 UniProtKB Modified residue 306 306 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15367680;Dbxref=PMID:15367680 O43293 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine%3B by autocatalysis and DAPK1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15367680,ECO:0000269|PubMed:15611134;Dbxref=PMID:15367680,PMID:15611134 O43293 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15367680,ECO:0007744|PubMed:23186163;Dbxref=PMID:15367680,PMID:23186163 O43293 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15367680;Dbxref=PMID:15367680 O43293 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15367680;Dbxref=PMID:15367680 O43293 UniProtKB Alternative sequence 313 322 . . . ID=VSP_042059;Note=In isoform 2. LPPNNSYADF->ASPIVAPVDA;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17126281;Dbxref=PMID:17126281 O43293 UniProtKB Alternative sequence 323 454 . . . ID=VSP_042060;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17126281;Dbxref=PMID:17126281 O43293 UniProtKB Natural variant 112 112 . . . ID=VAR_040438;Note=In a colorectal adenocarcinoma sample%3B somatic mutation%3B greatly reduces kinase activity%2C increases cell proliferation and cell survival. T->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17344846,ECO:0000269|PubMed:21487036;Dbxref=PMID:17344846,PMID:21487036 O43293 UniProtKB Natural variant 161 161 . . . ID=VAR_040439;Note=In an ovarian mucinous carcinoma sample%3B somatic mutation%3B greatly reduces kinase activity%2C increases cell proliferation and cell survival. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17344846,ECO:0000269|PubMed:21487036;Dbxref=PMID:17344846,PMID:21487036 O43293 UniProtKB Natural variant 216 216 . . . ID=VAR_040440;Note=In a lung neuroendocrine carcinoma sample%3B somatic mutation%3B greatly reduces kinase activity%2C increases cell proliferation%2C cell adhesion and cell survival. P->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17344846,ECO:0000269|PubMed:21487036;Dbxref=PMID:17344846,PMID:21487036 O43293 UniProtKB Mutagenesis 42 42 . . . Note=Loss of kinase activity at low concentrations of ATP. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17158456;Dbxref=PMID:17158456 O43293 UniProtKB Mutagenesis 161 161 . . . Note=Loss of kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17158456;Dbxref=PMID:17158456 O43293 UniProtKB Mutagenesis 180 180 . . . Note=Greatly reduced kinase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21487036;Dbxref=PMID:21487036 O43293 UniProtKB Mutagenesis 225 225 . . . Note=Loss of kinase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17158456;Dbxref=PMID:17158456 O43293 UniProtKB Mutagenesis 265 265 . . . Note=Loss of phosphorylation by ROCK1%2C catalytically inactive. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17158456;Dbxref=PMID:17158456 O43293 UniProtKB Mutagenesis 294 295 . . . Note=Cytoplasmic localization. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20854903;Dbxref=PMID:20854903 O43293 UniProtKB Mutagenesis 299 300 . . . Note=Predominantly nuclear localization. TT->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Mutagenesis 299 299 . . . Note=Loss of phosphorylation by ROCK1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17158456;Dbxref=PMID:17158456 O43293 UniProtKB Mutagenesis 299 299 . . . Note=Predominantly cytoplasmic localization%3B phosphomimetic. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Mutagenesis 427 427 . . . Note=Predominantly nuclear localization%3B when associated with A-434 and A-441. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Mutagenesis 434 434 . . . Note=Predominantly nuclear localization%3B when associated with A-427 and A-441. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Mutagenesis 441 441 . . . Note=Predominantly nuclear localization%3B when associated with A-427 and A-434. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611134;Dbxref=PMID:15611134 O43293 UniProtKB Helix 9 12 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 13 21 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 23 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Turn 33 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 38 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J90 O43293 UniProtKB Beta strand 53 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 58 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 79 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 86 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 101 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 113 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 150 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 171 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5A6N O43293 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5A6O O43293 UniProtKB Helix 181 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 186 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 197 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 222 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 238 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 246 253 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 266 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY O43293 UniProtKB Helix 273 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BHY