##gff-version 3
P61599	UniProtKB	Chain	1	178	.	.	.	ID=PRO_0000074534;Note=N-alpha-acetyltransferase 20	
P61599	UniProtKB	Domain	2	157	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
P61599	UniProtKB	Alternative sequence	103	178	.	.	.	ID=VSP_045644;Note=In isoform 2. KGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEPDEDAYDMRKALSRDTEKKSIIPLPHPVRPEDIE->YEESTFQGY;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
P61599	UniProtKB	Natural variant	4	4	.	.	.	ID=VAR_088425;Note=In MRT73%3B decreases interaction with NAA25%3B may reduce protein capacity to acetylate Met-Glu N-terminal peptides%3B does not affect protein stability. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37191084;Dbxref=dbSNP:rs752372862,PMID:37191084	
P61599	UniProtKB	Natural variant	34	178	.	.	.	ID=VAR_088426;Note=In MRT73. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37191084;Dbxref=dbSNP:rs755734957,PMID:37191084	
P61599	UniProtKB	Natural variant	54	54	.	.	.	ID=VAR_086809;Note=In MRT73%3B decreased complex formation with NAA25 and decreased N-acetylation catalytic activity in vitro for all 4 types of substrates%3B does not affect protein stability. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34230638;Dbxref=dbSNP:rs2146464332,PMID:34230638	
P61599	UniProtKB	Natural variant	80	80	.	.	.	ID=VAR_086810;Note=In MRT73%3B strong decrease in N-acetylation catalytic activity in vitro for substrates Met-Glu%2C Met-Asn and Met-Gln%2C but not Met-Asp%3B does not affect protein stability. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34230638;Dbxref=dbSNP:rs768029717,PMID:34230638	
P61599	UniProtKB	Sequence conflict	47	47	.	.	.	Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P61599	UniProtKB	Beta strand	4	6	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	11	14	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Turn	15	18	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	21	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Helix	28	37	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	44	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	51	53	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Turn	65	68	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	85	87	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Helix	88	102	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	111	113	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Helix	117	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	129	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX	
P61599	UniProtKB	Beta strand	147	153	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7STX