##gff-version 3
Q62622	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Chain	2	117	.	.	.	ID=PRO_0000190515;Note=Eukaryotic translation initiation factor 4E-binding protein 1	
Q62622	UniProtKB	Region	1	47	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62622	UniProtKB	Region	64	117	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62622	UniProtKB	Motif	53	59	.	.	.	Note=YXXXXLphi motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70445	
Q62622	UniProtKB	Motif	113	117	.	.	.	Note=TOS motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Compositional bias	1	15	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62622	UniProtKB	Compositional bias	33	47	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62622	UniProtKB	Compositional bias	78	97	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62622	UniProtKB	Compositional bias	98	117	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62622	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q62622	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60876	
Q62622	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphothreonine%3B by MTOR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine%3B by DYRK2%2C MAPK1%2C MAPK3 and MTOR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7939721;Dbxref=PMID:7939721	
Q62622	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphothreonine%3B by MTOR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	76	76	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	95	95	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60876	
Q62622	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60876	
Q62622	UniProtKB	Modified residue	100	100	.	.	.	Note=Phosphoserine%3B by DYRK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Cross-link	56	56	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13541	
Q62622	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Decreases phosphorylation by MAPK1 and MAPK3. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7939721;Dbxref=PMID:7939721	
Q62622	UniProtKB	Sequence conflict	19	19	.	.	.	Note=R->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62622	UniProtKB	Sequence conflict	69	69	.	.	.	Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q62622	UniProtKB	Sequence conflict	75	75	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305