##gff-version 3
Q64321	UniProtKB	Chain	1	544	.	.	.	ID=PRO_0000047720;Note=Zinc finger and BTB domain-containing protein 7B	
Q64321	UniProtKB	Domain	34	115	.	.	.	Note=BTB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00037	
Q64321	UniProtKB	Zinc finger	350	372	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q64321	UniProtKB	Zinc finger	378	400	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q64321	UniProtKB	Zinc finger	406	428	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q64321	UniProtKB	Zinc finger	434	458	.	.	.	Note=C2H2-type 4%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q64321	UniProtKB	Region	171	221	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64321	UniProtKB	Region	244	314	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64321	UniProtKB	Region	348	404	.	.	.	Note=Required for interaction with and acetylation by EP300;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Region	465	493	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64321	UniProtKB	Region	507	544	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64321	UniProtKB	Compositional bias	185	201	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64321	UniProtKB	Modified residue	150	150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15156	
Q64321	UniProtKB	Modified residue	210	210	.	.	.	Note=N6-acetyllysine%3B by EP300%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Modified residue	216	216	.	.	.	Note=N6-acetyllysine%3B by EP300%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Modified residue	339	339	.	.	.	Note=N6-acetyllysine%3B by EP300%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Modified residue	373	373	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15156	
Q64321	UniProtKB	Cross-link	210	210	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Cross-link	216	216	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Cross-link	339	339	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Natural variant	102	102	.	.	.	Note=In helpless. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23105140;Dbxref=PMID:23105140	
Q64321	UniProtKB	Natural variant	389	389	.	.	.	Note=In HD%3B disrupts sequence-specific DNA-binding%3B no effect on homodimerization or interaction with HDAC4 and HDAC5. R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15729333,ECO:0000269|PubMed:22730529,ECO:0000269|PubMed:24880459;Dbxref=PMID:15729333,PMID:22730529,PMID:24880459	
Q64321	UniProtKB	Mutagenesis	21	21	.	.	.	Note=Fails to repress CD8 expression. Abolishes interaction with HDAC4 and HDAC5. No effect on homodimerization and DNA binding. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22730529;Dbxref=PMID:22730529	
Q64321	UniProtKB	Mutagenesis	27	28	.	.	.	Note=Fails to repress CD8 expression. Abolishes interaction with HDAC4 and HDAC5. No effect on homodimerization and DNA binding. QR->AL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22730529;Dbxref=PMID:22730529	
Q64321	UniProtKB	Mutagenesis	207	207	.	.	.	Note=No effect on acetylation levels. Slightly decreases acetylation levels%3B when associated with R-210. Slightly decreases acetylation levels%3B when associated with R-216. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Slightly decreases acetylation levels. No effect on protein stability. Slightly decreases acetylation levels%3B when associated with R-207. Slightly decreases acetylation levels and increases protein stability%3B when associated with R-216. Increases protein stability%3B when associated with R-339. Decreases acetylation levels%3B when associated with R-216 and R-343. Abolishes acetylation levels and ubiquitination and highly increases protein stability%3B when associated with R-216 and R-339. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Slightly decreases acetylation levels. No effect on protein stability. Slightly decreases acetylation levels%3B when associated with R-207. Slightly decreases acetylation levels and increases protein stability%3B when associated with R-210. Increases protein stability%3B when associated with R-339. Decreases acetylation levels%3B when associated with R-210 and R-343. Abolishes acetylation levels and ubiquitination and highly increases protein stability%3B when associated with R-210 and R-339. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Mutagenesis	339	339	.	.	.	Note=Slightly decreases acetylation levels. Slightly increases protein stability. Slightly decreases acetylation levels%3B when associated with R-343. Increases protein stability%3B when associated with R-210 or R-216. Abolishes acetylation levels and ubiquitination and highly increases protein stability%3B when associated with R-210 and R-216. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Mutagenesis	343	343	.	.	.	Note=No effect on acetylation levels. Slightly decreases acetylation levels%3B when associated with R-339. Decreases acetylation levels%3B when associated with R-210 and R-216. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810990;Dbxref=PMID:20810990	
Q64321	UniProtKB	Sequence conflict	268	268	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305