##gff-version 3
Q99P99	UniProtKB	Chain	1	1077	.	.	.	ID=PRO_0000281034;Note=Histone deacetylase 4	
Q99P99	UniProtKB	Region	117	312	.	.	.	Note=Interaction with MEF2A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Region	132	167	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Region	204	225	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Region	239	327	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Region	508	530	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Region	542	582	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Region	623	646	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Region	653	1077	.	.	.	Note=Histone deacetylase;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Region	1052	1077	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Coiled coil	66	169	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99P99	UniProtKB	Motif	348	353	.	.	.	Note=PxLPxI/L motif%3B mediates interaction with ANKRA2 and 14-3-3 proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56524	
Q99P99	UniProtKB	Motif	1044	1077	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Compositional bias	132	166	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Compositional bias	204	224	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Compositional bias	239	278	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Compositional bias	290	327	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Compositional bias	515	530	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Compositional bias	1061	1077	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99P99	UniProtKB	Active site	796	796	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Binding site	665	665	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Binding site	667	667	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Binding site	673	673	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Binding site	744	744	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q99P99	UniProtKB	Modified residue	209	209	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6NZM9	
Q99P99	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphoserine%3B by CaMK4 and SIK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56524	
Q99P99	UniProtKB	Modified residue	349	349	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56524	
Q99P99	UniProtKB	Modified residue	466	466	.	.	.	Note=Phosphoserine%3B by CaMK4 and SIK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56524	
Q99P99	UniProtKB	Modified residue	563	563	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q99P99	UniProtKB	Modified residue	630	630	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q99P99	UniProtKB	Modified residue	631	631	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56524	
Q99P99	UniProtKB	Cross-link	557	557	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250