##gff-version 3
Q9QZQ8	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000227904;Note=Core histone macro-H2A.1	
Q9QZQ8	UniProtKB	Domain	2	117	.	.	.	Note=Histone H2A	
Q9QZQ8	UniProtKB	Domain	184	367	.	.	.	Note=Macro;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00490	
Q9QZQ8	UniProtKB	Region	128	180	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9QZQ8	UniProtKB	Compositional bias	140	160	.	.	.	Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9QZQ8	UniProtKB	Binding site	203	203	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	204	204	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	226	226	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	275	275	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	312	312	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	313	313	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	314	314	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Binding site	316	316	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A0D2UG83	
Q9QZQ8	UniProtKB	Modified residue	7	7	.	.	.	Note=N6-lactoyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0C0S5	
Q9QZQ8	UniProtKB	Modified residue	9	9	.	.	.	Note=N6-lactoyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0C0S5	
Q9QZQ8	UniProtKB	Modified residue	18	18	.	.	.	Note=N6-methyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Modified residue	116	116	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q9QZQ8	UniProtKB	Modified residue	123	123	.	.	.	Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Modified residue	123	123	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q9QZQ8	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19144319,ECO:0007744|PubMed:21183079;Dbxref=PMID:19144319,PMID:21183079	
Q9QZQ8	UniProtKB	Modified residue	170	170	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q9QZQ8	UniProtKB	Modified residue	173	173	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q9QZQ8	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q9QZQ8	UniProtKB	Cross-link	116	116	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Cross-link	117	117	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Cross-link	123	123	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Cross-link	167	167	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Cross-link	189	189	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Cross-link	320	320	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75367	
Q9QZQ8	UniProtKB	Alternative sequence	198	226	.	.	.	ID=VSP_061611;Note=In isoform 2. QVVQADIASIDSDAVVHPTNTDFYTGGEV->NLIHSEISNLAGFEVEAIINPTNADIDLKDDL	
Q9QZQ8	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Abolished ability to bind poly-ADP-ribose and inhibit PARP1. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28991266;Dbxref=PMID:28991266