##gff-version 3
P01100	UniProtKB	Chain	1	380	.	.	.	ID=PRO_0000076465;Note=Protein c-Fos	
P01100	UniProtKB	Domain	137	200	.	.	.	Note=BZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
P01100	UniProtKB	Region	119	138	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P01100	UniProtKB	Region	139	159	.	.	.	Note=Basic motif%3B required for the activation of phospholipid synthesis%2C but not for CDS1-binding	
P01100	UniProtKB	Region	165	193	.	.	.	Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978	
P01100	UniProtKB	Region	354	380	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P01100	UniProtKB	Compositional bias	357	380	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P01100	UniProtKB	Modified residue	10	10	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17160021,ECO:0000269|PubMed:22105363;Dbxref=PMID:17160021,PMID:22105363	
P01100	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17160021,ECO:0000269|PubMed:22105363;Dbxref=PMID:17160021,PMID:22105363	
P01100	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01101	
P01100	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphothreonine%3B by MAPK1 and MAPK3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134156;Dbxref=PMID:12134156	
P01100	UniProtKB	Modified residue	331	331	.	.	.	Note=Phosphothreonine%3B by MAPK1 and MAPK3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134156;Dbxref=PMID:12134156	
P01100	UniProtKB	Modified residue	362	362	.	.	.	Note=Phosphoserine%3B by MAPK1%2C MAPK3 and RPS6KA3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7588633;Dbxref=PMID:7588633	
P01100	UniProtKB	Modified residue	374	374	.	.	.	Note=Phosphoserine%3B by MAPK1 and MAPK3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12134156,ECO:0000269|PubMed:7588633;Dbxref=PMID:12134156,PMID:7588633	
P01100	UniProtKB	Cross-link	113	113	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
P01100	UniProtKB	Cross-link	128	128	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733	
P01100	UniProtKB	Cross-link	265	265	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:25772364,PMID:28112733	
P01100	UniProtKB	Alternative sequence	1	114	.	.	.	ID=VSP_055560;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
P01100	UniProtKB	Alternative sequence	132	167	.	.	.	ID=VSP_055561;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
P01100	UniProtKB	Mutagenesis	10	10	.	.	.	Note=Loss of activation of phospholipid synthesis%3B when associated with E-30. Y->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17160021,ECO:0000269|PubMed:22105363;Dbxref=PMID:17160021,PMID:22105363	
P01100	UniProtKB	Mutagenesis	10	10	.	.	.	Note=Overall loss of Tyr-phosphorylation%2C including that of Y-30 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17160021,ECO:0000269|PubMed:22105363;Dbxref=PMID:17160021,PMID:22105363	
P01100	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Loss of activation of phospholipid synthesis%3B when associated with E-10. Y->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17160021,ECO:0000269|PubMed:22105363;Dbxref=PMID:17160021,PMID:22105363	
P01100	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Overall loss of Tyr-phosphorylation%2C including that of Y-10 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17160021,ECO:0000269|PubMed:22105363;Dbxref=PMID:17160021,PMID:22105363	
P01100	UniProtKB	Mutagenesis	106	106	.	.	.	Note=No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17160021;Dbxref=PMID:17160021	
P01100	UniProtKB	Mutagenesis	128	128	.	.	.	Note=No change in sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055710;Dbxref=PMID:16055710	
P01100	UniProtKB	Mutagenesis	192	192	.	.	.	Note=No change in sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055710;Dbxref=PMID:16055710	
P01100	UniProtKB	Mutagenesis	232	232	.	.	.	Note=Decreased sumoylation levels. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055710;Dbxref=PMID:16055710	
P01100	UniProtKB	Mutagenesis	265	265	.	.	.	Note=Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055710;Dbxref=PMID:16055710	
P01100	UniProtKB	Mutagenesis	325	325	.	.	.	Note=No change in sumoylation levels. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055710;Dbxref=PMID:16055710	
P01100	UniProtKB	Mutagenesis	331	331	.	.	.	Note=No change in sumoylation levels. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055710;Dbxref=PMID:16055710	
P01100	UniProtKB	Mutagenesis	337	337	.	.	.	Note=No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17160021;Dbxref=PMID:17160021	
P01100	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability%3B when associated with A-374. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16055710,ECO:0000269|PubMed:7588633;Dbxref=PMID:16055710,PMID:7588633	
P01100	UniProtKB	Mutagenesis	362	362	.	.	.	Note=Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels%3B when associated with D-374. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16055710,ECO:0000269|PubMed:7588633;Dbxref=PMID:16055710,PMID:7588633	
P01100	UniProtKB	Mutagenesis	374	374	.	.	.	Note=No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability%3B when associated with A-362. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16055710,ECO:0000269|PubMed:7588633;Dbxref=PMID:16055710,PMID:7588633	
P01100	UniProtKB	Mutagenesis	374	374	.	.	.	Note=Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels%3B when associated with D-362. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16055710,ECO:0000269|PubMed:7588633;Dbxref=PMID:16055710,PMID:7588633	
P01100	UniProtKB	Sequence conflict	133	144	.	.	.	Note=SPEEEEKRRIRR->ISRRRREKENPK;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P01100	UniProtKB	Helix	141	191	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1A02