##gff-version 3
P01959	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6030605;Dbxref=PMID:6030605	
P01959	UniProtKB	Chain	2	142	.	.	.	ID=PRO_0000052624;Note=Hemoglobin subunit alpha	
P01959	UniProtKB	Peptide	96	104	.	.	.	ID=PRO_0000455869;Note=Hemopressin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01946	
P01959	UniProtKB	Binding site	59	59	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00238	
P01959	UniProtKB	Binding site	88	88	.	.	.	Note=Proximal binding residue;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00238	
P01959	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P69905	
P01959	UniProtKB	Modified residue	8	8	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P69905	
P01959	UniProtKB	Modified residue	12	12	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	17	17	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P69905	
P01959	UniProtKB	Modified residue	17	17	.	.	.	Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	41	41	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P69905	
P01959	UniProtKB	Modified residue	103	103	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	125	125	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	135	135	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	138	138	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Modified residue	139	139	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01942	
P01959	UniProtKB	Sequence conflict	132	132	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P01959	UniProtKB	Helix	5	18	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	19	21	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	22	36	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	38	43	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	54	72	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	74	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	82	88	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Turn	89	92	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	97	113	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Turn	115	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Helix	120	136	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H	
P01959	UniProtKB	Turn	137	141	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S0H