##gff-version 3
Q2NL51	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49840	
Q2NL51	UniProtKB	Chain	2	490	.	.	.	ID=PRO_0000280395;Note=Glycogen synthase kinase-3 alpha	
Q2NL51	UniProtKB	Domain	119	404	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q2NL51	UniProtKB	Region	1	97	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q2NL51	UniProtKB	Region	451	490	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q2NL51	UniProtKB	Compositional bias	452	490	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q2NL51	UniProtKB	Active site	244	244	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q2NL51	UniProtKB	Binding site	125	133	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q2NL51	UniProtKB	Binding site	148	148	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q2NL51	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49840	
Q2NL51	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49840	
Q2NL51	UniProtKB	Modified residue	21	21	.	.	.	Note=Phosphoserine%3B by PKB/AKT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15791206;Dbxref=PMID:15791206	
Q2NL51	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49840	
Q2NL51	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49840	
Q2NL51	UniProtKB	Modified residue	97	97	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49840	
Q2NL51	UniProtKB	Modified residue	279	279	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18265	
Q2NL51	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Loss of phosphorylation%3B No inhibition of activity and constitutively active. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15791206;Dbxref=PMID:15791206