##gff-version 3
Q91V92	UniProtKB	Chain	1	1091	.	.	.	ID=PRO_0000102782;Note=ATP-citrate synthase	
Q91V92	UniProtKB	Domain	4	265	.	.	.	Note=ATP-grasp	
Q91V92	UniProtKB	Region	442	478	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q91V92	UniProtKB	Compositional bias	442	458	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q91V92	UniProtKB	Active site	750	750	.	.	.	Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	58	58	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	66	66	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	67	67	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	109	109	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	111	111	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	118	118	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	216	216	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	257	257	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	260	260	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	262	262	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	309	309	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	346	346	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	348	348	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	364	364	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	379	379	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Binding site	769	779	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q91V92	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q91V92	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16638	
Q91V92	UniProtKB	Modified residue	451	451	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16638	
Q91V92	UniProtKB	Modified residue	455	455	.	.	.	Note=Phosphoserine%3B by PKA and PKB/AKT1 or PKB/AKT2 or BCKDK;Ontology_term=ECO:0000250,ECO:0007744;evidence=ECO:0000250|UniProtKB:P53396,ECO:0007744|PubMed:19131326;Dbxref=PMID:19131326	
Q91V92	UniProtKB	Modified residue	459	459	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	530	530	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	536	536	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	544	544	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	653	653	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q91V92	UniProtKB	Modified residue	672	672	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17947660,ECO:0007744|PubMed:18034455;Dbxref=PMID:17947660,PMID:18034455	
Q91V92	UniProtKB	Modified residue	829	829	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	938	938	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	958	958	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	968	968	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q91V92	UniProtKB	Modified residue	1067	1067	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53396	
Q91V92	UniProtKB	Modified residue	1090	1090	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q91V92	UniProtKB	Cross-link	530	530	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34491895;Dbxref=PMID:34491895	
Q91V92	UniProtKB	Cross-link	536	536	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34491895;Dbxref=PMID:34491895	
Q91V92	UniProtKB	Cross-link	544	544	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34491895;Dbxref=PMID:34491895	
Q91V92	UniProtKB	Mutagenesis	530	530	.	.	.	Note=Abolished ubiquitination by the BCR(KLHL25)complex%2C leading to imapired differentiation of inducible regulatory T (iTreg) cells%3B when associated with R-536 and R-544. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34491895;Dbxref=PMID:34491895	
Q91V92	UniProtKB	Mutagenesis	536	536	.	.	.	Note=Abolished ubiquitination by the BCR(KLHL25)complex%2C leading to imapired differentiation of inducible regulatory T (iTreg) cells%3B when associated with R-530 and R-544. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34491895;Dbxref=PMID:34491895	
Q91V92	UniProtKB	Mutagenesis	544	544	.	.	.	Note=Abolished ubiquitination by the BCR(KLHL25)complex%2C leading to imapired differentiation of inducible regulatory T (iTreg) cells%3B when associated with R-530 and R-536. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34491895;Dbxref=PMID:34491895