##gff-version 3
O88764	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000085916;Note=Death-associated protein kinase 3	
O88764	UniProtKB	Domain	13	275	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
O88764	UniProtKB	Region	161	204	.	.	.	Note=Activation segment;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96017	
O88764	UniProtKB	Region	390	448	.	.	.	Note=Interaction with CDC5L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11884640;Dbxref=PMID:11884640	
O88764	UniProtKB	Region	418	448	.	.	.	Note=Required for interaction with ATF4 but not with PAWR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10602480;Dbxref=PMID:10602480	
O88764	UniProtKB	Region	422	436	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	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	
O88764	UniProtKB	Binding site	19	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
O88764	UniProtKB	Binding site	42	42	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
O88764	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphothreonine%3B by ROCK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine%3B by autocatalysis and DAPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	307	307	.	.	.	Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Modified residue	321	321	.	.	.	Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43293	
O88764	UniProtKB	Alternative sequence	1	1	.	.	.	ID=VSP_042061;Note=In isoform 2. M->MIDSSCVPRILQKDSAMM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O88764	UniProtKB	Mutagenesis	42	42	.	.	.	Note=Loss of kinase activity%2C loss of PAWR-linked translocation into the cytoplasm%3B maintains nuclear localization but loss of localization to PML-NB. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10602474,ECO:0000269|PubMed:10602480;Dbxref=PMID:10602474,PMID:10602480	
O88764	UniProtKB	Mutagenesis	294	294	.	.	.	Note=Causes dissociation from promyelocytic leukemia oncogenic bodies and increased blebbing-inducing potency%3B when associated with T-300. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17953487;Dbxref=PMID:17953487	
O88764	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Causes dissociation from promyelocytic leukemia oncogenic bodies and increased blebbing-inducing potency%3B when associated with T-299. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17953487;Dbxref=PMID:17953487	
O88764	UniProtKB	Mutagenesis	406	407	.	.	.	Note=Cytoplasmic localization. RR->AL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10602474;Dbxref=PMID:10602474