##gff-version 3 Q13127 UniProtKB Chain 1 1097 . . . ID=PRO_0000269547;Note=RE1-silencing transcription factor Q13127 UniProtKB Zinc finger 159 181 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 216 238 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 248 270 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 276 298 . . . Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 304 326 . . . Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 332 355 . . . Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 361 383 . . . Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 389 412 . . . Note=C2H2-type 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Zinc finger 1060 1082 . . . Note=C2H2-type 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q13127 UniProtKB Region 32 122 . . . Note=Interaction with SIN3A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734093;Dbxref=PMID:10734093 Q13127 UniProtKB Region 43 57 . . . Note=Interaction with SIN3B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16288918;Dbxref=PMID:16288918 Q13127 UniProtKB Region 83 103 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Region 127 159 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Region 145 418 . . . Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 Q13127 UniProtKB Region 201 212 . . . Note=Required for binding to the neuron-restrictive silencer element;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VIG1 Q13127 UniProtKB Region 452 642 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Region 774 837 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Region 853 938 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Region 961 1049 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Region 1009 1087 . . . Note=Interaction with RCOR1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10449787;Dbxref=PMID:10449787 Q13127 UniProtKB Compositional bias 143 159 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 452 478 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 479 493 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 494 574 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 575 591 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 806 836 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 910 938 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Compositional bias 1005 1021 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13127 UniProtKB Modified residue 864 864 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q13127 UniProtKB Modified residue 971 971 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O54963 Q13127 UniProtKB Alternative sequence 301 313 . . . ID=VSP_022064;Note=In isoform 2. ERPYKCELCPYSS->KRSFLVHKFSSLF;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7871435;Dbxref=PMID:7871435 Q13127 UniProtKB Alternative sequence 304 326 . . . ID=VSP_022067;Note=In isoform 4. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13127 UniProtKB Alternative sequence 314 1097 . . . ID=VSP_022065;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7871435;Dbxref=PMID:7871435 Q13127 UniProtKB Alternative sequence 329 329 . . . ID=VSP_022066;Note=In isoform 3. E->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13127 UniProtKB Alternative sequence 330 1097 . . . ID=VSP_022068;Note=In isoform 3. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13127 UniProtKB Natural variant 160 160 . . . ID=VAR_076333;Note=In WT6%3B inhibits transcriptional repression activity. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Natural variant 290 290 . . . ID=VAR_076334;Note=In WT6%3B inhibits transcriptional repression activity. N->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Natural variant 322 322 . . . ID=VAR_076335;Note=In WT6%3B inhibits transcriptional repression activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=dbSNP:rs869025312,PMID:26551668 Q13127 UniProtKB Natural variant 412 412 . . . ID=VAR_076336;Note=In WT6. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Natural variant 437 1097 . . . ID=VAR_079529;Note=In GINGF5. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28686854;Dbxref=PMID:28686854 Q13127 UniProtKB Natural variant 626 626 . . . ID=VAR_029795;Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs2228991,PMID:15489334 Q13127 UniProtKB Natural variant 692 692 . . . ID=VAR_029796;Note=E->D;Dbxref=dbSNP:rs2227902 Q13127 UniProtKB Natural variant 762 762 . . . ID=VAR_029797;Note=K->Q;Dbxref=dbSNP:rs2227903 Q13127 UniProtKB Natural variant 797 797 . . . ID=VAR_029798;Note=P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8568247;Dbxref=dbSNP:rs3796529,PMID:8568247 Q13127 UniProtKB Mutagenesis 91 91 . . . Note=Does not change transcriptional repression activity. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Mutagenesis 313 313 . . . Note=Lack of deubiquitination by USP7. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21258371;Dbxref=PMID:21258371 Q13127 UniProtKB Mutagenesis 420 420 . . . Note=Inhibits transcriptional repression activity. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Mutagenesis 512 522 . . . Note=No effect on nuclear localization. KFSKTKKSKRK->AFSKTADSMDA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16442230;Dbxref=PMID:16442230 Q13127 UniProtKB Mutagenesis 512 522 . . . Note=Reduced nuclear localization. KFSKTKKSKRK->GS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16442230;Dbxref=PMID:16442230 Q13127 UniProtKB Mutagenesis 512 522 . . . Note=No effect on nuclear localization. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16442230;Dbxref=PMID:16442230 Q13127 UniProtKB Mutagenesis 593 593 . . . Note=Does not change transcriptional repression activity. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Mutagenesis 642 642 . . . Note=Does not change transcriptional repression activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Mutagenesis 918 918 . . . Note=Does not change transcriptional repression activity. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26551668;Dbxref=PMID:26551668 Q13127 UniProtKB Mutagenesis 1009 1013 . . . Note=Loss of interaction with BTRC. Reduced ubiquitination. Decreased proteasomal degradation in G2. Decreased average time from nuclear envelope breakdown to anaphase onset. Increased number of lagging chromosomes and chromosome bridges in anaphase and prematurely separated sister chromatids. Reduced MAD2 levels. EGIHS->AGIHA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18354482;Dbxref=PMID:18354482 Q13127 UniProtKB Mutagenesis 1009 1009 . . . Note=Loss of interaction with BTRC. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18354482;Dbxref=PMID:18354482 Q13127 UniProtKB Mutagenesis 1013 1013 . . . Note=Loss of interaction with BTRC. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18354482;Dbxref=PMID:18354482 Q13127 UniProtKB Mutagenesis 1042 1042 . . . Note=No impact on deubiquitination by USP7. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21258371;Dbxref=PMID:21258371 Q13127 UniProtKB Sequence conflict 295 295 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13127 UniProtKB Sequence conflict 596 599 . . . Note=PQKE->SRNS;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13127 UniProtKB Sequence conflict 630 630 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13127 UniProtKB Helix 44 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CZY