##gff-version 3
Q00899	UniProtKB	Chain	1	414	.	.	.	ID=PRO_0000047191;Note=Transcriptional repressor protein YY1	
Q00899	UniProtKB	Zinc finger	296	320	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q00899	UniProtKB	Zinc finger	325	347	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q00899	UniProtKB	Zinc finger	353	377	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q00899	UniProtKB	Zinc finger	383	407	.	.	.	Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q00899	UniProtKB	Region	1	170	.	.	.	Note=Interaction with the SMAD1/SMAD4 complex;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Region	32	83	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q00899	UniProtKB	Region	159	203	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q00899	UniProtKB	Region	257	341	.	.	.	Note=Involved in nuclear matrix association;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Region	295	414	.	.	.	Note=Binding to DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Region	333	371	.	.	.	Note=Involved in repression of activated transcription;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Region	371	397	.	.	.	Note=Involved in masking transactivation domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Compositional bias	39	55	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q00899	UniProtKB	Compositional bias	66	83	.	.	.	Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q00899	UniProtKB	Binding site	298	298	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	303	303	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	316	316	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	320	320	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	327	327	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	330	330	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	343	343	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	347	347	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	355	355	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	360	360	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	373	373	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	377	377	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	385	385	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	390	390	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	403	403	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Binding site	407	407	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Site	121	122	.	.	.	Note=Cleavage%3B by caspase-7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Modified residue	247	247	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q00899	UniProtKB	Modified residue	378	378	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	182	182	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	183	183	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	208	208	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	230	230	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	286	286	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	288	288	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	409	409	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Cross-link	411	411	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25490	
Q00899	UniProtKB	Sequence conflict	219	219	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q00899	UniProtKB	Sequence conflict	375	375	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305