##gff-version 3
P04911	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400	
P04911	UniProtKB	Chain	2	132	.	.	.	ID=PRO_0000055326;Note=Histone H2A.1	
P04911	UniProtKB	Motif	129	130	.	.	.	Note=[ST]-Q motif	
P04911	UniProtKB	Site	120	120	.	.	.	Note=Not ubiquitinated;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:2201907;Dbxref=PMID:10642555,PMID:2201907	
P04911	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400	
P04911	UniProtKB	Modified residue	5	5	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10082517;Dbxref=PMID:10082517	
P04911	UniProtKB	Modified residue	8	8	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:11545749;Dbxref=PMID:10082517,PMID:11545749	
P04911	UniProtKB	Modified residue	14	14	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22389435;Dbxref=PMID:22389435	
P04911	UniProtKB	Modified residue	22	22	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22389435;Dbxref=PMID:22389435	
P04911	UniProtKB	Modified residue	106	106	.	.	.	Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239	
P04911	UniProtKB	Modified residue	120	120	.	.	.	Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22389435;Dbxref=PMID:22389435	
P04911	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
P04911	UniProtKB	Cross-link	127	127	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
P04911	UniProtKB	Mutagenesis	120	121	.	.	.	Note=No effect. No effect%3B when associated with R-124 and R-127. KK->RR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:2201907;Dbxref=PMID:10642555,PMID:2201907	
P04911	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Causes hypersensitivity to DNA-damage-inducing agents and impairs sporulation. S->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781691;Dbxref=PMID:15781691	
P04911	UniProtKB	Mutagenesis	124	124	.	.	.	Note=No effect%3B when associated with R-120%3B R-121 and R-127. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642555;Dbxref=PMID:10642555	
P04911	UniProtKB	Mutagenesis	127	127	.	.	.	Note=No effect%3B when associated with R-120%3B R-121 and R-124. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642555;Dbxref=PMID:10642555	
P04911	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Causes hypersensitivity to DNA-damage-inducing agents. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
P04911	UniProtKB	Mutagenesis	129	129	.	.	.	Note=No effect. S->E%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636	
P04911	UniProtKB	Helix	19	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Helix	29	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Beta strand	41	45	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Helix	48	74	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Beta strand	78	80	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Helix	82	90	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Helix	93	99	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WNN	
P04911	UniProtKB	Beta strand	102	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ID3	
P04911	UniProtKB	Turn	105	107	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7ON1	
P04911	UniProtKB	Helix	115	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1ID3