##gff-version 3
P11275	UniProtKB	Chain	1	478	.	.	.	ID=PRO_0000086094;Note=Calcium/calmodulin-dependent protein kinase type II subunit alpha	
P11275	UniProtKB	Domain	13	271	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P11275	UniProtKB	Region	290	300	.	.	.	Note=Calmodulin-binding	
P11275	UniProtKB	Region	310	320	.	.	.	Note=Interaction with BAALC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15659234;Dbxref=PMID:15659234	
P11275	UniProtKB	Region	314	341	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P11275	UniProtKB	Compositional bias	322	341	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P11275	UniProtKB	Active site	135	135	.	.	.	Note=Proton acceptor	
P11275	UniProtKB	Binding site	19	27	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P11275	UniProtKB	Binding site	42	42	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P11275	UniProtKB	Modified residue	13	13	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11798	
P11275	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P11275	UniProtKB	Modified residue	286	286	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2842767;Dbxref=PMID:2842767	
P11275	UniProtKB	Modified residue	330	330	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11798	
P11275	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11798	
P11275	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11798	
P11275	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11798	
P11275	UniProtKB	Modified residue	337	337	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11798	
P11275	UniProtKB	Modified residue	404	404	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P11275	UniProtKB	Mutagenesis	432	435	.	.	.	Note=Loss of interaction with MPDZ. IRIT->MGTA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15312654;Dbxref=PMID:15312654	
P11275	UniProtKB	Sequence conflict	301	301	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P11275	UniProtKB	Helix	295	309	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CDM