##gff-version 3 P06401 UniProtKB Chain 1 933 . . . ID=PRO_0000053693;Note=Progesterone receptor P06401 UniProtKB Domain 679 913 . . . Note=NR LBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01189 P06401 UniProtKB DNA binding 567 639 . . . Note=Nuclear receptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P06401 UniProtKB Zinc finger 567 587 . . . Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P06401 UniProtKB Zinc finger 603 627 . . . Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P06401 UniProtKB Region 1 566 . . . Note=Modulating%2C Pro-Rich P06401 UniProtKB Region 1 164 . . . Note=AF3%3B mediates transcriptional activation (in isoform B);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Region 1 157 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Region 165 305 . . . Note=Mediates transcriptional transrepression (in isoform A);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9407067;Dbxref=PMID:9407067 P06401 UniProtKB Region 195 241 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Region 331 351 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Region 415 452 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Region 456 546 . . . Note=AF1%3B mediates transcriptional activation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1587864;Dbxref=PMID:1587864 P06401 UniProtKB Region 687 933 . . . Note=AF2%3B mediates transcriptional activation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1587864;Dbxref=PMID:1587864 P06401 UniProtKB Motif 55 59 . . . Note=LXXL motif 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Motif 115 119 . . . Note=LXXL motif 2;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Motif 183 187 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P06401 UniProtKB Compositional bias 68 84 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Compositional bias 120 135 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Compositional bias 415 431 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P06401 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11110801;Dbxref=PMID:11110801 P06401 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7476977,ECO:0000269|PubMed:8702648;Dbxref=PMID:7476977,PMID:8702648 P06401 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11110801,ECO:0000269|PubMed:8702648;Dbxref=PMID:11110801,PMID:8702648 P06401 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11110801;Dbxref=PMID:11110801 P06401 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11110801,ECO:0000269|PubMed:15798179,ECO:0000269|PubMed:7476977,ECO:0000269|PubMed:8702648,ECO:0000269|PubMed:9171245,ECO:0007744|PubMed:23186163;Dbxref=PMID:11110801,PMID:15798179,PMID:23186163,PMID:7476977,PMID:8702648,PMID:9171245 P06401 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10628747,ECO:0000269|PubMed:11110801,ECO:0000269|PubMed:15798179,ECO:0000269|PubMed:9171245;Dbxref=PMID:10628747,PMID:11110801,PMID:15798179,PMID:9171245 P06401 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11110801;Dbxref=PMID:11110801 P06401 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine%3B by MAPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10628747,ECO:0000269|PubMed:10655479,ECO:0000269|PubMed:15798179,ECO:0000269|PubMed:17173941,ECO:0000269|PubMed:17717077,ECO:0000269|PubMed:18202149,ECO:0000269|PubMed:8702648;Dbxref=PMID:10628747,PMID:10655479,PMID:15798179,PMID:17173941,PMID:17717077,PMID:18202149,PMID:8702648 P06401 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11110801,ECO:0000269|PubMed:18202149,ECO:0000269|PubMed:8702648;Dbxref=PMID:11110801,PMID:18202149,PMID:8702648 P06401 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine%3B by CDK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15572662,ECO:0000269|PubMed:18202149,ECO:0000269|PubMed:9171245;Dbxref=PMID:15572662,PMID:18202149,PMID:9171245 P06401 UniProtKB Modified residue 676 676 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11110801;Dbxref=PMID:11110801 P06401 UniProtKB Cross-link 7 7 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17020914;Dbxref=PMID:17020914 P06401 UniProtKB Cross-link 388 388 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate P06401 UniProtKB Cross-link 388 388 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17347654;Dbxref=PMID:17347654 P06401 UniProtKB Cross-link 531 531 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17020914;Dbxref=PMID:17020914 P06401 UniProtKB Alternative sequence 1 594 . . . ID=VSP_046942;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P06401 UniProtKB Alternative sequence 1 164 . . . ID=VSP_003706;Note=In isoform A. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P06401 UniProtKB Alternative sequence 1 16 . . . ID=VSP_047454;Note=In isoform 4. MTELKAKGPRAPHVAG->MEFIYIYMNFFFFFSV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12644308;Dbxref=PMID:12644308 P06401 UniProtKB Alternative sequence 17 635 . . . ID=VSP_047455;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12644308;Dbxref=PMID:12644308 P06401 UniProtKB Alternative sequence 636 737 . . . ID=VSP_053543;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.4 P06401 UniProtKB Natural variant 50 50 . . . ID=VAR_019221;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571143 P06401 UniProtKB Natural variant 120 120 . . . ID=VAR_019222;Note=A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571144 P06401 UniProtKB Natural variant 186 186 . . . ID=VAR_019223;Note=P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571145 P06401 UniProtKB Natural variant 301 301 . . . ID=VAR_019224;Note=M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571146 P06401 UniProtKB Natural variant 344 344 . . . ID=VAR_016117;Note=S->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2328727,ECO:0000269|Ref.8;Dbxref=dbSNP:rs3740753,PMID:2328727 P06401 UniProtKB Natural variant 347 347 . . . ID=VAR_025555;Note=C->S;Dbxref=dbSNP:rs11571147 P06401 UniProtKB Natural variant 444 444 . . . ID=VAR_019225;Note=A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571150 P06401 UniProtKB Natural variant 529 529 . . . ID=VAR_019226;Note=V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571151 P06401 UniProtKB Natural variant 536 536 . . . ID=VAR_019227;Note=Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571152 P06401 UniProtKB Natural variant 625 625 . . . ID=VAR_014627;Note=R->I;Dbxref=dbSNP:rs2020874 P06401 UniProtKB Natural variant 651 651 . . . ID=VAR_019228;Note=L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11571222 P06401 UniProtKB Natural variant 660 660 . . . ID=VAR_016118;Note=V->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12644308,ECO:0000269|PubMed:3551956,ECO:0000269|Ref.3;Dbxref=dbSNP:rs1042838,PMID:12644308,PMID:3551956 P06401 UniProtKB Natural variant 865 865 . . . ID=VAR_014628;Note=S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs2020880 P06401 UniProtKB Mutagenesis 7 7 . . . Note=Some loss of sumoylation%3B when associated with R-531. Complete loss of sumoylation%3B when associated with R-388 and R-531. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17020914;Dbxref=PMID:17020914 P06401 UniProtKB Mutagenesis 55 55 . . . Note=Reduces transcriptional activation%3B when associated with A-58 and A-59. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 58 58 . . . Note=Reduces transcriptional activation%3B when associated with A-55 and A-59. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 59 59 . . . Note=Reduces transcriptional activation%3B when associated with A-55 and A-58. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 115 115 . . . Note=Reduces transcriptional activation%3B when associated with A-118 and A-119. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 118 118 . . . Note=Reduces transcriptional activation%3B when associated with A-115 and A-119. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 119 119 . . . Note=Reduces transcriptional activation%3B when associated with A-115 and A-118. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 140 140 . . . Note=Reduces transcriptional activation. W->A%2CF%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11546784;Dbxref=PMID:11546784 P06401 UniProtKB Mutagenesis 294 294 . . . Note=No effect on interaction with CUEDC2. Impaired progesterone-induced transcriptional activity. No CUEDC2- nor progestin-mediated protein degradation. No change in sumoylation%3B when associated with A-344 and A-345. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10655479,ECO:0000269|PubMed:17173941,ECO:0000269|PubMed:17717077;Dbxref=PMID:10655479,PMID:17173941,PMID:17717077 P06401 UniProtKB Mutagenesis 294 294 . . . Note=Decreases protein stability and increases progesterone-induced transcriptional activity. S->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10655479,ECO:0000269|PubMed:17173941,ECO:0000269|PubMed:17717077;Dbxref=PMID:10655479,PMID:17173941,PMID:17717077 P06401 UniProtKB Mutagenesis 344 344 . . . Note=No interaction with SP1. No change in progestin-induced protein degradation%3B when associated with A-345. No change in sumoylation%3B when associated with A-294 and A-345. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10655479,ECO:0000269|PubMed:18202149;Dbxref=PMID:10655479,PMID:18202149 P06401 UniProtKB Mutagenesis 345 345 . . . Note=No change in progestin-induced protein degradation%3B when associated with A-344. No change in sumoylation%3B when associated with A-294 and A-344. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10655479,ECO:0000269|PubMed:18202149;Dbxref=PMID:10655479,PMID:18202149 P06401 UniProtKB Mutagenesis 388 388 . . . Note=Great loss of sumoylation%3B when associated with R-7. Completely abolishes sumoylation%3B when associated with R-7 and R-531. Loss of CUEDC2-mediated protein degradation. Increased ligand-dependent transcriptional activity. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17020914,ECO:0000269|PubMed:17347654,ECO:0000269|PubMed:17717077;Dbxref=PMID:17020914,PMID:17347654,PMID:17717077 P06401 UniProtKB Mutagenesis 400 400 . . . Note=Abolishes CDK2-induced activity in the absence%2C but not in the presence%2C of progestin. Delayed nuclear translocation in presence of progestin. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15572662,ECO:0000269|PubMed:18202149;Dbxref=PMID:15572662,PMID:18202149 P06401 UniProtKB Mutagenesis 531 531 . . . Note=Some loss of sumoylation%3B when associated with R-7. Completely abolishes sumoylation%3B when associated with R-7 and R-388. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17020914;Dbxref=PMID:17020914 P06401 UniProtKB Sequence conflict 226 226 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P06401 UniProtKB Sequence conflict 256 256 . . . Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P06401 UniProtKB Turn 568 570 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Beta strand 576 578 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Beta strand 581 583 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Helix 585 596 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Beta strand 604 607 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Turn 613 618 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Helix 620 629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CC0 P06401 UniProtKB Helix 686 694 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 711 735 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 739 741 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 744 771 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Beta strand 774 779 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Beta strand 782 784 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 786 788 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 792 811 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 815 826 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Beta strand 828 830 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 838 857 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 863 896 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 898 901 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Helix 907 921 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN P06401 UniProtKB Beta strand 925 927 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1SQN