##gff-version 3 P04150 UniProtKB Chain 1 777 . . . ID=PRO_0000019937;Note=Glucocorticoid receptor P04150 UniProtKB Domain 524 758 . . . Note=NR LBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01189 P04150 UniProtKB DNA binding 418 493 . . . Note=Nuclear receptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P04150 UniProtKB Zinc finger 421 441 . . . Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P04150 UniProtKB Zinc finger 457 476 . . . Note=NR C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00407 P04150 UniProtKB Region 1 420 . . . Note=Modulating P04150 UniProtKB Region 1 23 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04150 UniProtKB Region 98 115 . . . Note=Required for high transcriptional activity of isoform Alpha-C3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23820903;Dbxref=PMID:23820903 P04150 UniProtKB Region 130 183 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04150 UniProtKB Region 394 415 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04150 UniProtKB Region 485 777 . . . Note=Interaction with CLOCK P04150 UniProtKB Region 487 523 . . . Note=Hinge P04150 UniProtKB Region 532 697 . . . Note=Interaction with CRY1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22170608;Dbxref=PMID:22170608 P04150 UniProtKB Compositional bias 130 149 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04150 UniProtKB Compositional bias 166 183 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04150 UniProtKB Modified residue 8 8 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P04150 UniProtKB Modified residue 23 23 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06537 P04150 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P04150 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06537 P04150 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 P04150 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06537 P04150 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:12000743,ECO:0000269|PubMed:18483179,ECO:0000269|PubMed:25847991,ECO:0007744|PubMed:24275569;Dbxref=PMID:12000743,PMID:18483179,PMID:24275569,PMID:25847991 P04150 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12000743,ECO:0000269|PubMed:18483179,ECO:0000269|PubMed:25847991;Dbxref=PMID:12000743,PMID:18483179,PMID:25847991 P04150 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18483179,ECO:0007744|PubMed:18669648;Dbxref=PMID:18483179,PMID:18669648 P04150 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 P04150 UniProtKB Modified residue 404 404 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18838540;Dbxref=PMID:18838540 P04150 UniProtKB Modified residue 480 480 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Modified residue 492 492 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Modified residue 494 494 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Modified residue 495 495 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Cross-link 258 258 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P04150 UniProtKB Cross-link 277 277 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144530;Dbxref=PMID:12144530 P04150 UniProtKB Cross-link 277 277 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P04150 UniProtKB Cross-link 293 293 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144530;Dbxref=PMID:12144530 P04150 UniProtKB Cross-link 293 293 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211 P04150 UniProtKB Cross-link 419 419 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06537 P04150 UniProtKB Cross-link 703 703 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144530;Dbxref=PMID:12144530 P04150 UniProtKB Alternative sequence 1 335 . . . ID=VSP_058312;Note=In isoform Alpha-D3. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Alternative sequence 1 330 . . . ID=VSP_058313;Note=In isoform Alpha-D2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Alternative sequence 1 315 . . . ID=VSP_058314;Note=In isoform Alpha-D1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Alternative sequence 1 97 . . . ID=VSP_058315;Note=In isoform Alpha-C3. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Alternative sequence 1 89 . . . ID=VSP_058316;Note=In isoform Alpha-C2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Alternative sequence 1 85 . . . ID=VSP_058317;Note=In isoform Alpha-C1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Alternative sequence 1 26 . . . ID=VSP_018773;Note=In isoform Alpha-B and isoform Beta-B. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04150 UniProtKB Alternative sequence 313 338 . . . ID=VSP_043908;Note=In isoform 10. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17404046;Dbxref=PMID:17404046 P04150 UniProtKB Alternative sequence 451 451 . . . ID=VSP_007363;Note=In isoform Alpha-2 and isoform Beta-2. G->GR;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.6 P04150 UniProtKB Alternative sequence 491 674 . . . ID=VSP_013340;Note=In isoform GR-A alpha and isoform GR-A beta. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04150 UniProtKB Alternative sequence 728 777 . . . ID=VSP_003703;Note=In isoform Beta%2C isoform Beta-B%2C isoform Beta-2 and isoform GR-A beta. VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK->NVMWLKPESTSHTLI;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2867473;Dbxref=PMID:2867473 P04150 UniProtKB Natural variant 23 23 . . . ID=VAR_014140;Note=Reduces transactivation activity%3B does not affect transrepression activity. R->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391209,ECO:0000269|PubMed:10898924,ECO:0000269|PubMed:12351458,ECO:0000269|PubMed:15276593,ECO:0000269|PubMed:15292341,ECO:0000269|PubMed:16030164,ECO:0000269|PubMed:9150737,ECO:0000269|Ref.9;Dbxref=dbSNP:rs6190,PMID:10391209,PMID:10898924,PMID:12351458,PMID:15276593,PMID:15292341,PMID:16030164,PMID:9150737 P04150 UniProtKB Natural variant 29 29 . . . ID=VAR_015628;Note=F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898924;Dbxref=dbSNP:rs148102613,PMID:10898924 P04150 UniProtKB Natural variant 65 65 . . . ID=VAR_014622;Note=F->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391209,ECO:0000269|Ref.9;Dbxref=dbSNP:rs6192,PMID:10391209 P04150 UniProtKB Natural variant 72 72 . . . ID=VAR_075797;Note=Associated in cis with A-321 and S-766 in one individual%3B doubles transactivation potential. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21701417;Dbxref=PMID:21701417 P04150 UniProtKB Natural variant 112 112 . . . ID=VAR_015629;Note=L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898924;Dbxref=dbSNP:rs542110718,PMID:10898924 P04150 UniProtKB Natural variant 233 233 . . . ID=VAR_015630;Note=D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898924;Dbxref=dbSNP:rs1241576112,PMID:10898924 P04150 UniProtKB Natural variant 321 321 . . . ID=VAR_075798;Note=Associated in cis with D-72 and S-766 in one individual%3B doubles transactivation potential. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21701417;Dbxref=PMID:21701417 P04150 UniProtKB Natural variant 363 363 . . . ID=VAR_004675;Note=Enhances transactivation activity%3B does not affect transrepression activity%3B may increase sensitivity to exogenously administered glucocorticoids%3B may contribute to central obesity in men and show lack of association with other risk factors for coronary heart disease and diabetes mellitus. N->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391209,ECO:0000269|PubMed:10898924,ECO:0000269|PubMed:11344238,ECO:0000269|PubMed:16030164,ECO:0000269|PubMed:8445027,ECO:0000269|PubMed:9150737;Dbxref=dbSNP:rs56149945,PMID:10391209,PMID:10898924,PMID:11344238,PMID:16030164,PMID:8445027,PMID:9150737 P04150 UniProtKB Natural variant 421 421 . . . ID=VAR_015631;Note=C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8358735;Dbxref=PMID:8358735 P04150 UniProtKB Natural variant 423 423 . . . ID=VAR_075799;Note=In GCCR%3B uncertain significance%3B reduces transactivation activity%3B delays nuclear translocation%3B does not exert a dominant negative effect%3B impairs DNA binding. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23426617;Dbxref=PMID:23426617 P04150 UniProtKB Natural variant 477 477 . . . ID=VAR_013472;Note=In GCCR. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11589680;Dbxref=dbSNP:rs104893913,PMID:11589680 P04150 UniProtKB Natural variant 477 477 . . . ID=VAR_077143;Note=In GCCR%3B loss of DNA-binding and of transactivation activity%3B incomplete dexamethasone-induced translocation to the nucleus%3B no effect on dexamethasone-binding affinity compared with wild-type. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27120390;Dbxref=PMID:27120390 P04150 UniProtKB Natural variant 478 478 . . . ID=VAR_077144;Note=In GCCR%3B decreased DNA-binding and transactivation activity%3B incomplete dexamethasone-induced translocation to the nucleus%3B no effect on dexamethasone-binding affinity compared with wild-type. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27120390;Dbxref=PMID:27120390 P04150 UniProtKB Natural variant 556 556 . . . ID=VAR_075800;Note=In GCCR%3B reduces transactivation activity%3B enhances transrepression activity%3B reduces affinity for ligand%3B delays nuclear translocation%3B does not exert a dominant negative effect%3B does not impair DNA binding. T->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21362280,ECO:0000269|PubMed:26541474;Dbxref=PMID:21362280,PMID:26541474 P04150 UniProtKB Natural variant 559 559 . . . ID=VAR_015632;Note=In GCCR%3B interferes with translocation to the nucleus and thereby strongly reduces transcription activation%3B is equally impaired in nuclear export%3B acts as dominant negative mutant. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11701741;Dbxref=dbSNP:rs104893909,PMID:11701741 P04150 UniProtKB Natural variant 571 571 . . . ID=VAR_025014;Note=In pseudohermaphroditism%3B female with hypokalemia due to glucocorticoid resistance%3B 6-fold reduction in binding affinity compared with the wild-type receptor. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11932321;Dbxref=dbSNP:rs104893911,PMID:11932321 P04150 UniProtKB Natural variant 575 575 . . . ID=VAR_075801;Note=In GCCR%3B uncertain significance%3B reduces transactivation activity%3B enhances transrepression activity%3B reduces affinity for ligand%3B delays nuclear translocation%3B does not exert a dominant negative effect%3B does not impair DNA binding. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24483153;Dbxref=PMID:24483153 P04150 UniProtKB Natural variant 641 641 . . . ID=VAR_004676;Note=In GCCR. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1704018;Dbxref=dbSNP:rs104893908,PMID:1704018 P04150 UniProtKB Natural variant 672 672 . . . ID=VAR_077145;Note=In GCCR%3B loss of dexamethasone-binding%2C dexamethasone-induced translocation to the nucleus and of transactivation activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27120390;Dbxref=PMID:27120390 P04150 UniProtKB Natural variant 679 679 . . . ID=VAR_013473;Note=In GCCR%3B has 50%25 binding affinity. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11589680;Dbxref=dbSNP:rs104893914,PMID:11589680 P04150 UniProtKB Natural variant 714 714 . . . ID=VAR_075802;Note=In GCCR%3B uncertain significance%3B reduces transactivation%3B reduces affinity for ligand%3B exerts a dominant negative effect%3B does not impair DNA binding. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20335448;Dbxref=PMID:20335448 P04150 UniProtKB Natural variant 726 726 . . . ID=VAR_075803;Note=In GCCR%3B uncertain significance%3B reduces transactivation and transrepression activity%3B reduces affinity for ligand%3B delays nuclear translocation%3B does not impair DNA binding. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26031419;Dbxref=PMID:26031419 P04150 UniProtKB Natural variant 729 729 . . . ID=VAR_004677;Note=In GCCR. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7683692;Dbxref=dbSNP:rs1027058734,PMID:7683692 P04150 UniProtKB Natural variant 737 737 . . . ID=VAR_071935;Note=In GCCR%3B reduces transactivation of the glucocorticoid-inducible tumor virus promoter%3B reduces affinity for ligand%3B delays its nuclear translocation%3B acts as dominant negative mutant. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635946;Dbxref=dbSNP:rs121909727,PMID:17635946 P04150 UniProtKB Natural variant 747 747 . . . ID=VAR_015633;Note=In GCCR%3B alters interaction with NCOA2 and strongly reduces transcription activation%3B acts as a dominant negative mutant. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050230;Dbxref=dbSNP:rs104893910,PMID:12050230 P04150 UniProtKB Natural variant 753 753 . . . ID=VAR_004678;Note=L->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8316249,ECO:0000269|PubMed:8358735;Dbxref=dbSNP:rs121909726,PMID:8316249,PMID:8358735 P04150 UniProtKB Natural variant 766 766 . . . ID=VAR_075804;Note=Associated in cis with D-72 and A-321 in one individual%3B doubles transactivation potential. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21701417;Dbxref=PMID:21701417 P04150 UniProtKB Natural variant 773 773 . . . ID=VAR_071936;Note=In GCCR%3B reduces transactivation of the glucocorticoid-inducible tumor virus promoter%3B reduces affinity for ligand%3B delays its nuclear translocation%3B acts as dominant negative mutant. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15769988;Dbxref=dbSNP:rs104893912,PMID:15769988 P04150 UniProtKB Mutagenesis 1 1 . . . Note=Abolishes expression of A-type isoforms. M->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11435610,ECO:0000269|PubMed:15866175;Dbxref=PMID:11435610,PMID:15866175 P04150 UniProtKB Mutagenesis 27 27 . . . Note=Abolishes expression of B-type isoforms. M->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11435610,ECO:0000269|PubMed:15866175;Dbxref=PMID:11435610,PMID:15866175 P04150 UniProtKB Mutagenesis 86 86 . . . Note=Abolishes expression of C-type isoforms%3B when associated with I-90 and I-98. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Mutagenesis 90 90 . . . Note=Abolishes expression of C-type isoforms%3B when associated with I-86 and I-98. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Mutagenesis 98 98 . . . Note=Abolishes expression of C-type isoforms%3B when associated with I-86 and I-90. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Mutagenesis 101 101 . . . Note=Reduces transcription activation activity of isoform Alpha-C3 by half. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23820903;Dbxref=PMID:23820903 P04150 UniProtKB Mutagenesis 101 101 . . . Note=Reduces transcription activation activity of isoform Alpha-C3 by half. Suppresses apoptosis-inducing activity of isoform Alpha-C3. Impairs recruitment of selected coregulators onto DNA binding sites. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23820903;Dbxref=PMID:23820903 P04150 UniProtKB Mutagenesis 106 107 . . . Note=Reduces activity of isoform Alpha-C3 by half. QQ->LL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23820903;Dbxref=PMID:23820903 P04150 UniProtKB Mutagenesis 113 114 . . . Note=Does not affect the activity of isoform Alpha-C3. SS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23820903;Dbxref=PMID:23820903 P04150 UniProtKB Mutagenesis 191 191 . . . Note=Reduces transactivation by the ADA complex. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 193 193 . . . Note=Reduces transactivation by the ADA complex. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 194 194 . . . Note=Strongly reduces transactivation by the ADA complex%3B when associated with V-224 and F-225. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 197 197 . . . Note=Reduces transactivation by the ADA complex. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 211 211 . . . Note=Reduces expression of target genes IGFBP1 and IRF8. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18483179;Dbxref=PMID:18483179 P04150 UniProtKB Mutagenesis 213 213 . . . Note=Strongly reduces transactivation by the ADA complex. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 224 224 . . . Note=Strongly reduces transactivation by the ADA complex%3B when associated with A-194 and F-225. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 225 225 . . . Note=Strongly reduces transactivation by the ADA complex%3B when associated with A-194 and V-224. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 226 226 . . . Note=Abolishes phosphorylation and enhances transcriptional activation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18483179;Dbxref=PMID:18483179 P04150 UniProtKB Mutagenesis 235 235 . . . Note=Strongly reduces transactivation by the ADA complex%3B when associated with V-236. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 236 236 . . . Note=Strongly reduces transactivation by the ADA complex%3B when associated with L-235. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154805;Dbxref=PMID:9154805 P04150 UniProtKB Mutagenesis 277 277 . . . Note=Strongly reduces sumoylation. Almost complete loss of sumoylation%3B when associated with R-293. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144530;Dbxref=PMID:12144530 P04150 UniProtKB Mutagenesis 293 293 . . . Note=Strongly reduces sumoylation. Almost complete loss of sumoylation%3B when associated with R-277. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144530;Dbxref=PMID:12144530 P04150 UniProtKB Mutagenesis 316 316 . . . Note=Abolishes expression of D-type isoforms%3B when associated with I-331 and I-336. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Mutagenesis 331 331 . . . Note=Abolishes expression of D-type isoforms%3B when associated with I-316 and I-336. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Mutagenesis 336 336 . . . Note=Abolishes expression of D-type isoforms%3B when associated with I-316 and I-331. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15866175;Dbxref=PMID:15866175 P04150 UniProtKB Mutagenesis 404 404 . . . Note=Abolishes phosphorylation. Does not affect translocation to the nucleus following ligand stimulation. Increases protein half-life and transcriptional repressor activity. Alters repertoire of regulated genes. Increases cell death. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18838540;Dbxref=PMID:18838540 P04150 UniProtKB Mutagenesis 404 404 . . . Note=Does not affect translocation to the nucleus following ligand stimulation. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18838540;Dbxref=PMID:18838540 P04150 UniProtKB Mutagenesis 480 480 . . . Note=Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer%3B when associated with A-492%3B A-494 and A-495. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Mutagenesis 492 492 . . . Note=Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer%3B when associated with A-480%3B A-494 and A-495. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Mutagenesis 494 494 . . . Note=Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer%3B when associated with A-495. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer%3B when associated with A-480%3B A-492 and A-495. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Mutagenesis 495 495 . . . Note=Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer%3B when associated with A-494. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer%3B when associated with A-480%3B A-492 and A-494. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19141540;Dbxref=PMID:19141540 P04150 UniProtKB Mutagenesis 585 585 . . . Note=Reduces activation mediated by ligand binding domain%3B when associated with A-590. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12151000;Dbxref=PMID:12151000 P04150 UniProtKB Mutagenesis 590 590 . . . Note=Reduces activation mediated by ligand binding domain%3B when associated with A-585. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12151000;Dbxref=PMID:12151000 P04150 UniProtKB Mutagenesis 602 602 . . . Note=Increases solubility. No effect on transactivation by dexamethasone. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12151000;Dbxref=PMID:12151000 P04150 UniProtKB Mutagenesis 625 625 . . . Note=Decreases transactivation by dexamethasone by 95%25. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12151000;Dbxref=PMID:12151000 P04150 UniProtKB Mutagenesis 628 628 . . . Note=Decreases dimerization and transactivation by dexamethasone%3B when associated with S-602. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12151000;Dbxref=PMID:12151000 P04150 UniProtKB Mutagenesis 703 703 . . . Note=Slightly reduces sumoylation. Inhibits the stimulatory effect of RWDD3 on its transcriptional activity. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12144530,ECO:0000269|PubMed:23508108;Dbxref=PMID:12144530,PMID:23508108 P04150 UniProtKB Sequence conflict 399 399 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04150 UniProtKB Sequence conflict 754 754 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04150 UniProtKB Turn 422 424 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Beta strand 430 432 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Beta strand 435 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Helix 439 450 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Beta strand 458 461 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Turn 467 472 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Helix 474 484 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E69 P04150 UniProtKB Helix 488 497 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6CFN P04150 UniProtKB Turn 525 527 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1M2Z P04150 UniProtKB Helix 532 538 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Beta strand 550 552 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3K22 P04150 UniProtKB Helix 556 579 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 584 586 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 589 615 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Beta strand 617 619 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4P6W P04150 UniProtKB Beta strand 621 624 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Beta strand 627 629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 631 634 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 639 655 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 660 671 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Beta strand 673 675 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 683 702 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Beta strand 704 706 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4P6W P04150 UniProtKB Helix 708 741 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 743 745 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 751 765 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4UDD P04150 UniProtKB Helix 766 768 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6DXK P04150 UniProtKB Beta strand 769 771 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UC3 P04150 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P04150 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378