##gff-version 3
Q6DJT9	UniProtKB	Chain	1	500	.	.	.	ID=PRO_0000295107;Note=Zinc finger protein PLAG1	
Q6DJT9	UniProtKB	Zinc finger	34	56	.	.	.	Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Zinc finger	62	86	.	.	.	Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Zinc finger	92	114	.	.	.	Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Zinc finger	121	143	.	.	.	Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Zinc finger	150	172	.	.	.	Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Zinc finger	185	207	.	.	.	Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Zinc finger	213	236	.	.	.	Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042	
Q6DJT9	UniProtKB	Region	1	30	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6DJT9	UniProtKB	Region	2	84	.	.	.	Note=Interaction with KPNA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11882654;Dbxref=PMID:11882654	
Q6DJT9	UniProtKB	Region	41	242	.	.	.	Note=Decreased nuclear import with localization in the nucleus but also in the cytoplasm	
Q6DJT9	UniProtKB	Region	243	500	.	.	.	Note=Activates transcription%3B Inhibition of nuclear import due to lack of NLS and KPNA2 interaction	
Q6DJT9	UniProtKB	Region	243	384	.	.	.	Note=Repression domain%3B contains 3 sumoylation motifs and massively decrease transcription activity	
Q6DJT9	UniProtKB	Region	365	388	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6DJT9	UniProtKB	Region	385	500	.	.	.	Note=Massively activates transcription	
Q6DJT9	UniProtKB	Motif	22	25	.	.	.	Note=Nuclear localization signal	
Q6DJT9	UniProtKB	Compositional bias	365	385	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6DJT9	UniProtKB	Cross-link	244	244	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
Q6DJT9	UniProtKB	Cross-link	263	263	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
Q6DJT9	UniProtKB	Alternative sequence	1	82	.	.	.	ID=VSP_045183;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q6DJT9	UniProtKB	Natural variant	458	458	.	.	.	ID=VAR_033212;Note=P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9020842;Dbxref=dbSNP:rs35883156,PMID:9020842	
Q6DJT9	UniProtKB	Mutagenesis	23	24	.	.	.	Note=Inhibition of KPNA2 interaction when mutation occurs in the NLS%3B decreased nuclear import with localization in the nucleus but also in the cytoplasm%3B Complete inhibition of nuclear import when associated with a lack of zinc-finger domains. RK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11882654;Dbxref=PMID:11882654	
Q6DJT9	UniProtKB	Mutagenesis	31	32	.	.	.	Note=No inhibition of KPNA2 interaction and no change in nuclear import. RK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11882654;Dbxref=PMID:11882654	
Q6DJT9	UniProtKB	Mutagenesis	92	92	.	.	.	Note=Prevents formation of functional zinc-finger 3%3B induces drastic decrease of DNA affinity and complete modification of DNA binding specificity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10646861;Dbxref=PMID:10646861	
Q6DJT9	UniProtKB	Mutagenesis	227	227	.	.	.	Note=Prevents formation of functional zinc-finger 7 and inhibits DNA binding%3B No proliferation and transformation of cultured cells. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10646861,ECO:0000269|PubMed:11888928;Dbxref=PMID:10646861,PMID:11888928	
Q6DJT9	UniProtKB	Mutagenesis	244	244	.	.	.	Note=Abolishes single and double sumoylation%3B nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity%3B when associated with R-263 and R-353. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15208321,ECO:0000269|PubMed:16207715;Dbxref=PMID:15208321,PMID:16207715	
Q6DJT9	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Decreases sumoylation%3B Abolishes double sumoylation only%3B Nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity%3B when associated with R-244 and R-353. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15208321,ECO:0000269|PubMed:16207715;Dbxref=PMID:15208321,PMID:16207715	
Q6DJT9	UniProtKB	Mutagenesis	339	339	.	.	.	Note=No effect on transcription activation capacity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9722527;Dbxref=PMID:9722527	
Q6DJT9	UniProtKB	Mutagenesis	340	340	.	.	.	Note=No effect on transcription activation capacity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9722527;Dbxref=PMID:9722527	
Q6DJT9	UniProtKB	Mutagenesis	353	353	.	.	.	Note=No effect on sumoylation. Increases transcriptional activity and inhibits repression domain activity%3B when associated with R-244 and R-263. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15208321,ECO:0000269|PubMed:16207715;Dbxref=PMID:15208321,PMID:16207715	
Q6DJT9	UniProtKB	Sequence conflict	276	276	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305