##gff-version 3
Q24338	UniProtKB	Chain	1	425	.	.	.	ID=PRO_0000050972;Note=Polycomb protein esc	
Q24338	UniProtKB	Repeat	71	114	.	.	.	Note=WD 1	
Q24338	UniProtKB	Repeat	126	165	.	.	.	Note=WD 2	
Q24338	UniProtKB	Repeat	168	208	.	.	.	Note=WD 3	
Q24338	UniProtKB	Repeat	214	253	.	.	.	Note=WD 4	
Q24338	UniProtKB	Repeat	284	321	.	.	.	Note=WD 5	
Q24338	UniProtKB	Repeat	340	379	.	.	.	Note=WD 6	
Q24338	UniProtKB	Repeat	388	424	.	.	.	Note=WD 7	
Q24338	UniProtKB	Region	1	64	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q24338	UniProtKB	Compositional bias	21	39	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q24338	UniProtKB	Compositional bias	40	57	.	.	.	Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q24338	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897	
Q24338	UniProtKB	Mutagenesis	64	64	.	.	.	Note=In esc1%3B induces homeotic transformation%3B when associated with R-240. Y->F	
Q24338	UniProtKB	Mutagenesis	210	211	.	.	.	Note=Strongly reduces phosphorylation and the interaction with E(z). GG->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10757791;Dbxref=PMID:10757791	
Q24338	UniProtKB	Mutagenesis	216	218	.	.	.	Note=Strongly reduces phosphorylation and the interaction with E(z). RDE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10757791;Dbxref=PMID:10757791	
Q24338	UniProtKB	Mutagenesis	240	240	.	.	.	Note=In esc1%3B induces homeotic transformation%3B when associated with F-64. L->R