##gff-version 3
O14558	UniProtKB	Chain	1	160	.	.	.	ID=PRO_0000125939;Note=Heat shock protein beta-6	
O14558	UniProtKB	Domain	55	160	.	.	.	Note=SHSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00285	
O14558	UniProtKB	Region	1	72	.	.	.	Note=Involved in stabilization of the HSPB1:HSBP6 heterodimer;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27717639;Dbxref=PMID:27717639	
O14558	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:21334344,ECO:0007744|PubMed:24275569;Dbxref=PMID:21334344,PMID:24275569	
O14558	UniProtKB	Modified residue	66	66	.	.	.	Note=Deamidated glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97541	
O14558	UniProtKB	Natural variant	20	20	.	.	.	ID=VAR_077818;Note=Decreases phosphorylation at Ser-16%3B abolishes cardioprotective effects. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18790732;Dbxref=dbSNP:rs11549029,PMID:18790732	
O14558	UniProtKB	Mutagenesis	3	3	.	.	.	Note=Increases homodimer-based self-association properties%3B increases chaperone activity%3B when associated with G-5. I->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24382496;Dbxref=PMID:24382496	
O14558	UniProtKB	Mutagenesis	5	5	.	.	.	Note=Increases homodimer-based self-association properties%3B increases chaperone activity%3B when associated with G-3. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24382496;Dbxref=PMID:24382496	
O14558	UniProtKB	Mutagenesis	67	67	.	.	.	Note=No effect on homodimer-based self-association properties%3B no effect on chaperone activity. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24382496;Dbxref=PMID:24382496	
O14558	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Decreases heteromer formation with CRYAB. S->Q	
O14558	UniProtKB	Sequence conflict	64	66	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O14558	UniProtKB	Beta strand	3	5	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5LUM	
O14558	UniProtKB	Beta strand	7	9	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5LUM	
O14558	UniProtKB	Beta strand	69	71	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUS	
O14558	UniProtKB	Beta strand	74	79	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Helix	85	87	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Beta strand	88	93	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Beta strand	96	107	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Beta strand	109	122	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Helix	129	131	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Beta strand	133	136	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT	
O14558	UniProtKB	Beta strand	140	146	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JUT