##gff-version 3
Q9BXH1	UniProtKB	Chain	1	193	.	.	.	ID=PRO_0000143083;Note=Bcl-2-binding component 3%2C isoforms 1/2	
Q9BXH1	UniProtKB	Region	1	28	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9BXH1	UniProtKB	Region	71	138	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9BXH1	UniProtKB	Motif	137	151	.	.	.	Note=BH3	
Q9BXH1	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q9BXH1	UniProtKB	Alternative sequence	1	92	.	.	.	ID=VSP_012238;Note=In isoform 2. MARARQEGSSPEPVEGLARDGPRPFPLGRLVPSAVSCGLCEPGLAAAPAAPTLLPAAYLCAPTAPPAVTAALGGSRWPGGPRSRPRGPRPDG->MKFGMGSAQACPCQVPRAASTTWVPCQICG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11463392;Dbxref=PMID:11463392	
Q9BXH1	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Impairs p53/TP53-dependent apoptosis. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23340338;Dbxref=PMID:23340338	
Q9BXH1	UniProtKB	Mutagenesis	141	143	.	.	.	Note=Abolishes BLC2-binding. Impairs growth inhibitory activity. No effect on mitochondrial subcellular location. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11463392;Dbxref=PMID:11463392	
Q9BXH1	UniProtKB	Helix	133	150	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UUL	
Q9BXH1	UniProtKB	Turn	151	154	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P0S