##gff-version 3 P03372 UniProtKB Chain 1 595 . . . ID=PRO_0000053618;Note=Estrogen receptor P03372 UniProtKB Domain 311 547 . . . Note=NR LBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01189 P03372 UniProtKB DNA binding 185 250 . . . Note=Nuclear receptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P03372 UniProtKB Zinc finger 185 205 . . . Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P03372 UniProtKB Zinc finger 221 245 . . . Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P03372 UniProtKB Region 1 184 . . . Note=Modulating (transactivation AF-1)%3B mediates interaction with MACROD1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914104;Dbxref=PMID:17914104 P03372 UniProtKB Region 35 174 . . . Note=Interaction with DDX5%3B self-association;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11682626;Dbxref=PMID:11682626 P03372 UniProtKB Region 35 47 . . . Note=Required for interaction with NCOA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11682626;Dbxref=PMID:11682626 P03372 UniProtKB Region 147 174 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P03372 UniProtKB Region 185 310 . . . Note=Mediates interaction with DNTTIP2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15047147;Dbxref=PMID:15047147 P03372 UniProtKB Region 251 310 . . . Note=Hinge P03372 UniProtKB Region 259 282 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P03372 UniProtKB Region 262 595 . . . Note=Interaction with AKAP13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9627117;Dbxref=PMID:9627117 P03372 UniProtKB Region 264 595 . . . Note=Self-association P03372 UniProtKB Region 311 595 . . . Note=Transactivation AF-2 P03372 UniProtKB Region 553 573 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P03372 UniProtKB Compositional bias 558 573 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P03372 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine%3B by CDK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10428798;Dbxref=PMID:10428798 P03372 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine%3B by CDK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10428798;Dbxref=PMID:10428798 P03372 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14764652;Dbxref=PMID:14764652 P03372 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7838153;Dbxref=PMID:7838153 P03372 UniProtKB Modified residue 260 260 . . . Note=Asymmetric dimethylarginine%3B by PRMT1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18657504,ECO:0000269|PubMed:24498420;Dbxref=PMID:18657504,PMID:24498420 P03372 UniProtKB Modified residue 537 537 . . . Note=Phosphotyrosine%3B by Tyr-kinases;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7539106;Dbxref=PMID:7539106 P03372 UniProtKB Lipidation 447 447 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03372 UniProtKB Glycosylation 10 10 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P03372 UniProtKB Alternative sequence 1 173 . . . ID=VSP_042460;Note=In isoform 3 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:16165085,ECO:0000303|PubMed:17974005;Dbxref=PMID:16165085,PMID:17974005 P03372 UniProtKB Alternative sequence 255 366 . . . ID=VSP_003680;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:3753802;Dbxref=PMID:3753802 P03372 UniProtKB Alternative sequence 458 595 . . . ID=VSP_042461;Note=In isoform 4. VYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV->ISHVEAKKRILNLHPKIFGNKWFPRV;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:16165085,ECO:0000303|PubMed:17974005;Dbxref=PMID:16165085,PMID:17974005 P03372 UniProtKB Natural variant 6 6 . . . ID=VAR_033028;Note=In a breast cancer sample%3B somatic mutation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17224074;Dbxref=dbSNP:rs139960913,PMID:17224074 P03372 UniProtKB Natural variant 77 77 . . . ID=VAR_018905;Note=G->S;Dbxref=dbSNP:rs9340773 P03372 UniProtKB Natural variant 160 160 . . . ID=VAR_004671;Note=G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9195227;Dbxref=dbSNP:rs149308960,PMID:9195227 P03372 UniProtKB Natural variant 264 264 . . . ID=VAR_033029;Note=In a breast cancer sample%3B somatic mutation. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17224074;Dbxref=PMID:17224074 P03372 UniProtKB Natural variant 375 375 . . . ID=VAR_070072;Note=In ESTRR%3B results in highly reduced activity. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23841731;Dbxref=dbSNP:rs397509428,PMID:23841731 P03372 UniProtKB Natural variant 394 394 . . . ID=VAR_078516;Note=In ESTRR%3B highly decreased estrogen receptor activity. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27754803;Dbxref=dbSNP:rs1131692059,PMID:27754803 P03372 UniProtKB Natural variant 400 400 . . . ID=VAR_004673;Note=Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius%2C but not at 4 degrees Celsius. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2792078,ECO:0000269|PubMed:3753802,ECO:0000269|PubMed:3754034;Dbxref=PMID:2792078,PMID:3753802,PMID:3754034 P03372 UniProtKB Natural variant 411 411 . . . ID=VAR_010143;Note=In a 80 kDa form found in a breast cancer line%3B contains an in-frame duplication of exons 6 and 7. D->RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHM P03372 UniProtKB Mutagenesis 39 39 . . . Note=Impairs AF-1 transactivation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11075817;Dbxref=PMID:11075817 P03372 UniProtKB Mutagenesis 43 43 . . . Note=Impairs AF-1 transactivation. Y->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11075817;Dbxref=PMID:11075817 P03372 UniProtKB Mutagenesis 104 104 . . . Note=Loss of cyclin A-dependent induction of transcriptional activation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10428798;Dbxref=PMID:10428798 P03372 UniProtKB Mutagenesis 106 106 . . . Note=Loss of cyclin A-dependent induction of transcriptional activation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10428798;Dbxref=PMID:10428798 P03372 UniProtKB Mutagenesis 118 118 . . . Note=Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409727,ECO:0000269|PubMed:14764652;Dbxref=PMID:10409727,PMID:14764652 P03372 UniProtKB Mutagenesis 118 118 . . . Note=Enhances transactivation activity. Insensitive to PPP5C inhibition of transactivation activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14764652;Dbxref=PMID:14764652 P03372 UniProtKB Mutagenesis 260 260 . . . Note=Loss of methylation. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657504;Dbxref=PMID:18657504 P03372 UniProtKB Mutagenesis 364 364 . . . Note=Has higher transcriptional activity in the absence of wild type ER. Inhibits transcriptional activity when coexpressed with the wild type receptor. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8961262;Dbxref=PMID:8961262 P03372 UniProtKB Mutagenesis 386 386 . . . Note=Loss of transmembrane localization%2C no effect on peripheral membrane localization. Impairs activation of estrogen-induced activation of NOS3 and production of nitric oxide. No effect on binding to ERES. I->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21937726;Dbxref=PMID:21937726 P03372 UniProtKB Mutagenesis 447 447 . . . Note=Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1577818;Dbxref=PMID:1577818 P03372 UniProtKB Mutagenesis 537 537 . . . Note=Reduces PELP1-mediated activation of transcriptional activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14963108;Dbxref=PMID:14963108 P03372 UniProtKB Mutagenesis 539 539 . . . Note=Abolishes interaction with NCOA1%2C NCOA2 and NCOA3. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12554772;Dbxref=PMID:12554772 P03372 UniProtKB Sequence conflict 452 452 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P03372 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCP P03372 UniProtKB Beta strand 194 196 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Beta strand 199 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Helix 203 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Beta strand 222 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Turn 231 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Helix 238 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1HCQ P03372 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LLO P03372 UniProtKB Helix 302 304 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3Q95 P03372 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 312 321 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RRX P03372 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QZO P03372 UniProtKB Helix 339 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 367 369 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 372 395 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Beta strand 396 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QE4 P03372 UniProtKB Beta strand 402 405 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Beta strand 408 410 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 412 415 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Beta strand 418 420 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5KCW P03372 UniProtKB Helix 421 438 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 442 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Turn 456 459 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UJO P03372 UniProtKB Helix 466 492 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 497 530 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 531 533 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RS0 P03372 UniProtKB Helix 538 545 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB P03372 UniProtKB Helix 547 549 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QVJ P03372 UniProtKB Helix 588 590 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5N10