##gff-version 3
P68366	UniProtKB	Chain	1	448	.	.	.	ID=PRO_0000048106;Note=Tubulin alpha-4A chain	
P68366	UniProtKB	Motif	1	4	.	.	.	Note=MREC motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Active site	254	254	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	11	11	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	71	71	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	71	71	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	140	140	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	144	144	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	145	145	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	179	179	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	206	206	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Binding site	228	228	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P68366	UniProtKB	Modified residue	40	40	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24906155;Dbxref=PMID:24906155	
P68366	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
P68366	UniProtKB	Modified residue	83	83	.	.	.	Note=3'-nitrotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68368	
P68366	UniProtKB	Modified residue	432	432	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BQE3	
P68366	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5XIF6	
P68366	UniProtKB	Alternative sequence	1	15	.	.	.	ID=VSP_055194;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
P68366	UniProtKB	Natural variant	145	145	.	.	.	ID=VAR_072714;Note=In ALS22. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25374358;Dbxref=dbSNP:rs730880029,PMID:25374358	
P68366	UniProtKB	Natural variant	215	215	.	.	.	ID=VAR_072715;Note=In ALS22%3B displays significantly different distribution in terms of incorporation into microtubules. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25374358;Dbxref=dbSNP:rs730880028,PMID:25374358	
P68366	UniProtKB	Natural variant	320	320	.	.	.	ID=VAR_072716;Note=In ALS22%3B displays significantly lower levels of dimer assembly. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25374358;Dbxref=dbSNP:rs730880025,PMID:25374358	
P68366	UniProtKB	Natural variant	320	320	.	.	.	ID=VAR_072717;Note=In ALS22%3B displays significantly lower levels of dimer assembly. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25374358;Dbxref=dbSNP:rs730880026,PMID:25374358	
P68366	UniProtKB	Natural variant	383	383	.	.	.	ID=VAR_072718;Note=In ALS22%3B displays significantly different distribution in terms of incorporation into microtubules%3B destabilizes the microtubule network. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25374358;Dbxref=dbSNP:rs368743618,PMID:25374358