##gff-version 3
P05213	UniProtKB	Chain	1	451	.	.	.	ID=PRO_0000048121;Note=Tubulin alpha-1B chain	
P05213	UniProtKB	Chain	1	450	.	.	.	ID=PRO_0000437387;Note=Detyrosinated tubulin alpha-1B chain;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:26446751,ECO:0000305|PubMed:27102488,ECO:0000305|PubMed:29146868;Dbxref=PMID:26446751,PMID:27102488,PMID:29146868	
P05213	UniProtKB	Region	432	451	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P05213	UniProtKB	Motif	1	4	.	.	.	Note=MREC motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Active site	254	254	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	11	11	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	71	71	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	71	71	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	140	140	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	144	144	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	145	145	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	179	179	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	206	206	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Binding site	228	228	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Site	451	451	.	.	.	Note=Involved in polymerization	
P05213	UniProtKB	Modified residue	40	40	.	.	.	Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Modified residue	40	40	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Modified residue	282	282	.	.	.	Note=3'-nitrotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68373	
P05213	UniProtKB	Modified residue	339	339	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68373	
P05213	UniProtKB	Modified residue	443	443	.	.	.	Note=5-glutamyl polyglutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Modified residue	445	445	.	.	.	Note=5-glutamyl polyglutamate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1967194;Dbxref=PMID:1967194	
P05213	UniProtKB	Modified residue	451	451	.	.	.	Note=3'-nitrotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q71U36	
P05213	UniProtKB	Cross-link	326	326	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Cross-link	370	370	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68363	
P05213	UniProtKB	Sequence conflict	55	55	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05213	UniProtKB	Sequence conflict	114	114	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05213	UniProtKB	Sequence conflict	119	119	.	.	.	Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05213	UniProtKB	Sequence conflict	135	136	.	.	.	Note=FL->LF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05213	UniProtKB	Sequence conflict	340	340	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305