ID GCR_MOUSE Reviewed; 792 AA. AC P06537; E0ZPU5; E9PUR6; E9PYV1; Q06VW2; Q3U126; Q3U2M7; Q61628; Q61629; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 29-SEP-2021, sequence version 2. DT 27-MAR-2024, entry version 235. DE RecName: Full=Glucocorticoid receptor; DE Short=GR; DE AltName: Full=Nuclear receptor subfamily 3 group C member 1; GN Name=Nr3c1; Synonyms=Grl, Grl1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 78-GLN--GLN-86 DEL. RX PubMed=3780669; DOI=10.1002/j.1460-2075.1986.tb04529.x; RA Danielsen M., Northrop J.P., Ringold G.M.; RT "The mouse glucocorticoid receptor: mapping of functional domains by RT cloning, sequencing and expression of wild-type and mutant receptor RT proteins."; RL EMBO J. 5:2513-2522(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-91 DEL, AND RP POLYMORPHISM. RX PubMed=17012242; DOI=10.1096/fj.06-5926fje; RA Xu D., Buehner A., Xu J., Lambert T., Nekl C., Nielsen M.K., Zhou Y.; RT "A polymorphic glucocorticoid receptor in a mouse population may explain RT inherited altered stress response and increased anxiety-type behaviors."; RL FASEB J. 20:2414-2416(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, INDUCTION, AND VARIANT 78-GLN--GLN-86 DEL. RX PubMed=20660300; DOI=10.1210/me.2009-0411; RA Hinds T.D. Jr., Ramakrishnan S., Cash H.A., Stechschulte L.A., Heinrich G., RA Najjar S.M., Sanchez E.R.; RT "Discovery of glucocorticoid receptor-beta in mice with a role in RT metabolism."; RL Mol. Endocrinol. 24:1715-1727(2010). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP 78-GLN--GLN-86 DEL. RC STRAIN=NOD; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP 78-GLN--GLN-86 DEL. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-764 (ISOFORMS 1 AND 2). RX PubMed=2911477; DOI=10.1093/nar/17.1.445; RA Nohno T., Kasai Y., Saito T.; RT "Novel cDNA sequence possibly generated by alternative splicing of a mouse RT glucocorticoid receptor gene transcript from Shionogi carcinoma 115."; RL Nucleic Acids Res. 17:445-445(1989). RN [8] RP GLUCOCORTICOID-MEDIATED DOWN-REGULATION. RX PubMed=2702670; RA Vedeckis W.V., Ali M., Allen H.R.; RT "Regulation of glucocorticoid receptor protein and mRNA levels."; RL Cancer Res. 49:2295-2302(1989). RN [9] RP PHOSPHORYLATION AT SER-131; SER-159; THR-168; SER-221; SER-229; SER-243 AND RP SER-324. RX PubMed=2019585; DOI=10.1016/s0021-9258(20)89482-4; RA Bodwell J.E., Orti E., Coull J.M., Pappin D.J.C., Smith L.I., Swift F.; RT "Identification of phosphorylated sites in the mouse glucocorticoid RT receptor."; RL J. Biol. Chem. 266:7549-7555(1991). RN [10] RP IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1. RX PubMed=9195923; DOI=10.1074/jbc.272.26.16224; RA Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., RA Chinkers M., Pratt W.B.; RT "Protein phosphatase 5 is a major component of glucocorticoid RT receptor.hsp90 complexes with properties of an FK506-binding RT immunophilin."; RL J. Biol. Chem. 272:16224-16230(1997). RN [11] RP INTERACTION WITH STAT5A AND STAT5B. RX PubMed=9528750; DOI=10.1128/mcb.18.4.1783; RA Cella N., Groner B., Hynes N.E.; RT "Characterization of Stat5a and Stat5b homodimers and heterodimers and RT their association with the glucocortiocoid receptor in mammary cells."; RL Mol. Cell. Biol. 18:1783-1792(1998). RN [12] RP INTERACTION WITH TRIM28. RX PubMed=9742105; DOI=10.1128/mcb.18.10.5880; RA Chang C.J., Chen Y.L., Lee S.C.; RT "Coactivator TIF1beta interacts with transcription factor C/EBPbeta and RT glucocorticoid receptor to induce alpha1-acid glycoprotein gene RT expression."; RL Mol. Cell. Biol. 18:5880-5887(1998). RN [13] RP INTERACTION WITH TGFB1I1. RX PubMed=10848625; DOI=10.1091/mbc.11.6.2007; RA Yang L., Guerrero J., Hong H., DeFranco D.B., Stallcup M.R.; RT "Interaction of the tau2 transcriptional activation domain of RT glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, RT which localizes to both focal adhesions and the nuclear matrix."; RL Mol. Biol. Cell 11:2007-2018(2000). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10678832; DOI=10.1126/science.287.5456.1262; RA McNally J.G., Mueller W.G., Walker D., Wolford R., Hager G.L.; RT "The glucocorticoid receptor: rapid exchange with regulatory sites in RT living cells."; RL Science 287:1262-1265(2000). RN [15] RP SUBCELLULAR LOCATION, HETEROMULTIMERIC COMPLEX FORMATION, INTERACTION WITH RP FKBP4, AND MECHANISM OF TRANSLOCATION TO THE NUCLEUS. RX PubMed=11278753; DOI=10.1074/jbc.m010809200; RA Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.; RT "Evidence that the peptidylprolyl isomerase domain of the hsp90-binding RT immunophilin FKBP52 is involved in both dynein interaction and RT glucocorticoid receptor movement to the nucleus."; RL J. Biol. Chem. 276:14884-14889(2001). RN [16] RP UBIQUITINATION AT LYS-435, MUTAGENESIS OF LYS-435, AND RP GLUCOCORTICOID-MEDIATED DOWN-REGULATION. RX PubMed=11555652; DOI=10.1074/jbc.m106033200; RA Wallace A.D., Cidlowski J.A.; RT "Proteasome-mediated glucocorticoid receptor degradation restricts RT transcriptional signaling by glucocorticoids."; RL J. Biol. Chem. 276:42714-42721(2001). RN [17] RP ALTERNATIVE INITIATION, AND MUTAGENESIS OF MET-1 AND MET-28. RX PubMed=11435610; DOI=10.1210/mend.15.7.0667; RA Yudt M.R., Cidlowski J.A.; RT "Molecular identification and characterization of A and B forms of the RT glucocorticoid receptor."; RL Mol. Endocrinol. 15:1093-1103(2001). RN [18] RP HETEROMULTIMERIC COMPLEX FORMATION, AND MECHANISM OF TRANSLOCATION TO THE RP NUCLEUS. RX PubMed=11751894; DOI=10.1074/jbc.c100531200; RA Davies T.H., Ning Y.M., Sanchez E.R.; RT "A new first step in activation of steroid receptors: hormone-induced RT switching of FKBP51 and FKBP52 immunophilins."; RL J. Biol. Chem. 277:4597-4600(2002). RN [19] RP INVOLVEMENT IN IMMUNE SYSTEM DEVELOPMENT. RX PubMed=12949501; DOI=10.1038/nm895; RA Brewer J.A., Khor B., Vogt S.K., Muglia L.M., Fujiwara H., Haegele K.E., RA Sleckman B.P., Muglia L.J.; RT "T-cell glucocorticoid receptor is required to suppress COX-2-mediated RT lethal immune activation."; RL Nat. Med. 9:1318-1322(2003). RN [20] RP POSSIBLE FUNCTION IN THE CONTROL OF BODY GROWTH. RX PubMed=15037546; DOI=10.1101/gad.284704; RA Tronche F., Opherk C., Moriggl R., Kellendonk C., Reimann A., Schwake L., RA Reichardt H.M., Stangl K., Gau D., Hoeflich A., Beug H., Schmid W., RA Schuetz G.; RT "Glucocorticoid receptor function in hepatocytes is essential to promote RT postnatal body growth."; RL Genes Dev. 18:492-497(2004). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [22] RP FUNCTION IN ADIPOGENESIS, INTERACTION WITH FKBP5 AND PPP5C, PHOSPHORYLATION RP AT SER-221; SER-229 AND SER-243, AND DEPHOSPHORYLATION AT SER-221 AND RP SER-243 BY PPP5C. RX PubMed=21994940; DOI=10.1074/jbc.m111.311662; RA Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A., RA Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.; RT "Protein phosphatase 5 mediates lipid metabolism through reciprocal control RT of glucocorticoid receptor and peroxisome proliferator-activated receptor-? RT (PPAR?)."; RL J. Biol. Chem. 286:42911-42922(2011). RN [23] RP INTERACTION WITH CRY1 AND CRY2. RX PubMed=22170608; DOI=10.1038/nature10700; RA Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., RA Downes M., Evans R.M.; RT "Cryptochromes mediate rhythmic repression of the glucocorticoid RT receptor."; RL Nature 480:552-556(2011). RN [24] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-24, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [25] RP INTERACTION WITH CIART. RX PubMed=24736997; DOI=10.1371/journal.pbio.1001839; RA Goriki A., Hatanaka F., Myung J., Kim J.K., Yoritaka T., Tanoue S., Abe T., RA Kiyonari H., Fujimoto K., Kato Y., Todo T., Matsubara A., Forger D., RA Takumi T.; RT "A novel protein, CHRONO, functions as a core component of the mammalian RT circadian clock."; RL PLoS Biol. 12:E1001839-E1001839(2014). RN [26] RP FUNCTION. RX PubMed=25847991; DOI=10.1073/pnas.1411356112; RA Matthews L.C., Berry A.A., Morgan D.J., Poolman T.M., Bauer K., Kramer F., RA Spiller D.G., Richardson R.V., Chapman K.E., Farrow S.N., Norman M.R., RA Williamson A.J., Whetton A.D., Taylor S.S., Tuckermann J.P., White M.R., RA Ray D.W.; RT "Glucocorticoid receptor regulates accurate chromosome segregation and is RT associated with malignancy."; RL Proc. Natl. Acad. Sci. U.S.A. 112:5479-5484(2015). RN [27] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-493. RX PubMed=25676786; DOI=10.1016/j.steroids.2015.01.022; RA Banuelos J., Shin S.C., Lu N.Z.; RT "A hotspot in the glucocorticoid receptor DNA-binding domain susceptible to RT loss of function mutation."; RL Steroids 96:115-120(2015). RN [28] RP INTERACTION WITH CRY1 AND CRY2. RX PubMed=28751364; DOI=10.1073/pnas.1704955114; RA Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E., RA Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T., RA Zhao X., Downes M., Evans R.M., Lamia K.A.; RT "Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors RT and modulate transcriptional activity."; RL Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017). RN [29] RP INTERACTION WITH HSP90AA1 AND HSP90AB1, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=27686098; DOI=10.1242/jcs.190959; RA Okabe T., Chavan R., Fonseca Costa S.S., Brenna A., Ripperger J.A., RA Albrecht U.; RT "REV-ERBalpha influences the stability and nuclear localization of the RT glucocorticoid receptor."; RL J. Cell Sci. 129:4143-4154(2016). CC -!- FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: CC as a transcription factor that binds to glucocorticoid response CC elements (GRE), both for nuclear and mitochondrial DNA, and as a CC modulator of other transcription factors. Affects inflammatory CC responses, cellular proliferation and differentiation in target CC tissues. Involved in chromatin remodeling (PubMed:10678832). Plays a CC role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs CC and interacting with PNRC2 in a ligand-dependent manner which recruits CC the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to CC RNA decay (By similarity). Could act as a coactivator for STAT5- CC dependent transcription upon growth hormone (GH) stimulation and could CC reveal an essential role of hepatic GR in the control of body growth CC (PubMed:15037546). {ECO:0000250|UniProtKB:P04150, CC ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:15037546}. CC -!- FUNCTION: [Isoform 1]: Has transcriptional activation and repression CC activity (By similarity). Mediates glucocorticoid-induced apoptosis (By CC similarity). Promotes accurate chromosome segregation during mitosis CC (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May CC play a negative role in adipogenesis through the regulation of CC lipolytic and antilipogenic gene expression (PubMed:21994940). CC {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:21994940, CC ECO:0000269|PubMed:25847991}. CC -!- FUNCTION: [Isoform 3]: Acts as a dominant negative inhibitor of isoform CC 1 (PubMed:20660300). Has intrinsic transcriptional activity independent CC of isoform Alpha when both isoforms are coexpressed (By similarity). CC Loses this transcription modulator function on its own (By similarity). CC Has no hormone-binding activity (PubMed:20660300). May play a role in CC controlling glucose metabolism by maintaining insulin sensitivity CC (PubMed:20660300). Reduces hepatic gluconeogenesis through down- CC regulation of PEPCK in an isoform Alpha-dependent manner (By CC similarity). Directly regulates STAT1 expression in isoform Alpha- CC independent manner (By similarity). {ECO:0000250|UniProtKB:P04150, CC ECO:0000269|PubMed:20660300}. CC -!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90AA1, CC HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, CC or the immunophilin homolog PPP5C (PubMed:9195923, PubMed:21994940). CC Upon ligand binding FKBP5 dissociates from the complex and FKBP4 takes CC its place, thereby linking the complex to dynein and mediating CC transport to the nucleus, where the complex dissociates CC (PubMed:9195923, PubMed:11278753). Probably forms a complex composed of CC chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client CC protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain CC co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Directly CC interacts with UNC45A (By similarity). Binds to DNA as a homodimer, and CC as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and CC STAT5B homodimers and heterodimers (PubMed:9528750). Interacts with CC NRIP1, POU2F1, POU2F2 and TRIM28 (PubMed:9742105). Interacts with CC several coactivator complexes, including the SMARCA4 complex, CC CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 CC and NCOA6 (By similarity). Interaction with BAG1 inhibits CC transactivation (By similarity). Interacts with HEXIM1 and TGFB1I1 CC (PubMed:10848625). Interacts with NCOA1 (By similarity). Interacts with CC NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (By similarity). CC Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion CC (PubMed:22170608, PubMed:28751364). Interacts with CIART CC (PubMed:24736997). Interacts with RWDD3 (By similarity). Interacts with CC UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 CC (By similarity). Interacts with GRIP1 (By similarity). Interacts with CC NR4A3 (via nuclear receptor DNA-binding domain), represses CC transcription activity of NR4A3 on the POMC promoter Nur response CC element (NurRE) (By similarity). Directly interacts with PNRC2 to CC attract and form a complex with UPF1 and DCP1A; the interaction leads CC to rapid mRNA degradation (By similarity). Interacts with GSK3B (By CC similarity). Interacts with FNIP1 and FNIP2 (By similarity). Interacts CC (via C-terminus) with HNRNPU (via C-terminus) (By similarity). CC Interacts with MCM3AP (By similarity). Interacts (via domain NR LBD) CC with HSP90AA1 and HSP90AB1 (PubMed:27686098). In the absence of CC hormonal ligand, interacts with TACC1 (By similarity). Interacts (via CC NR LBD domain) with ZNF764 (via KRAB domain); the interaction regulates CC transcription factor activity of NR3C1 by directing its actions toward CC certain biologic pathways (By similarity). CC {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06536, CC ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:10848625, CC ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:21994940, CC ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:24736997, CC ECO:0000269|PubMed:27686098, ECO:0000269|PubMed:28751364, CC ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9528750, CC ECO:0000269|PubMed:9742105}. CC -!- INTERACTION: CC P06537; O88485: Dync1i1; NbExp=2; IntAct=EBI-492753, EBI-492834; CC P06537; P30416: Fkbp4; NbExp=3; IntAct=EBI-492753, EBI-492746; CC P06537; Q64378: Fkbp5; NbExp=2; IntAct=EBI-492753, EBI-492796; CC P06537; P11499: Hsp90ab1; NbExp=2; IntAct=EBI-492753, EBI-492813; CC P06537-1; P97784: Cry1; NbExp=3; IntAct=EBI-15959147, EBI-1266607; CC P06537-1; Q9R194: Cry2; NbExp=3; IntAct=EBI-15959147, EBI-1266619; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278753, CC ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. Nucleus CC {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753, CC ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. CC Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding CC (PubMed:11278753). The hormone-occupied receptor undergoes rapid CC exchange between chromatin and the nucleoplasmic compartment CC (PubMed:10678832). In the presence of NR1D1 shows a time-dependent CC subcellular localization, localizing to the cytoplasm at ZT8 and to the CC nucleus at ZT20 (PubMed:27686098). Lacks this diurnal pattern of CC localization in the absence of NR1D1, localizing to both nucleus and CC the cytoplasm at ZT8 and ZT20 (PubMed:27686098). CC {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753, CC ECO:0000269|PubMed:27686098}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. CC Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, CC spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, CC translocates from the cytoplasm to the nucleus. CC {ECO:0000250|UniProtKB:P04150}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus CC {ECO:0000269|PubMed:20660300}. Cytoplasm {ECO:0000269|PubMed:20660300}. CC Note=Expressed predominantly in the nucleus with some expression also CC detected in the cytoplasm. {ECO:0000269|PubMed:20660300}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=1; Synonyms=1-A, GR form A, Alpha; CC IsoId=P06537-1; Sequence=Displayed; CC Name=2; Synonyms=2-A, GR form B, Gamma; CC IsoId=P06537-2; Sequence=VSP_003704; CC Name=1-B; CC IsoId=P06537-3; Sequence=VSP_018774; CC Name=2-B; CC IsoId=P06537-4; Sequence=VSP_018774, VSP_003704; CC Name=3; Synonyms=Beta; CC IsoId=P06537-5; Sequence=VSP_058320, VSP_058321; CC -!- TISSUE SPECIFICITY: Expressed in spleen, kidney and liver CC (PubMed:20660300). Expressed in a circadian manner in the liver CC (PubMed:27686098). {ECO:0000269|PubMed:20660300, CC ECO:0000269|PubMed:27686098}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed at highest level in spleen CC with lesser amounts in kidney and liver. {ECO:0000269|PubMed:20660300}. CC -!- INDUCTION: [Isoform 1]: Down-regulated by glucocorticoids. CC {ECO:0000269|PubMed:20660300}. CC -!- INDUCTION: [Isoform 3]: Up-regulated by glucocorticoids and insulin. CC {ECO:0000269|PubMed:20660300}. CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a CC DNA-binding domain and a C-terminal ligand-binding domain. The ligand- CC binding domain is required for correct chromosome segregation during CC mitosis although ligand binding is not required. CC {ECO:0000250|UniProtKB:P04150}. CC -!- PTM: Acetylation by CLOCK reduces its binding to glucocorticoid CC response elements and its transcriptional activity. CC {ECO:0000250|UniProtKB:P04150}. CC -!- PTM: Increased proteasome-mediated degradation in response to CC glucocorticoids. {ECO:0000269|PubMed:11555652}. CC -!- PTM: Phosphorylated in the absence of hormone; becomes CC hyperphosphorylated in the presence of glucocorticoids. Phosphorylated CC in the absence of hormone; becomes hyperphosphorylated in the presence CC of glucocorticoid. The Ser-221, Ser-243 and Ser-421-phosphorylated CC forms are mainly cytoplasmic, and the Ser-229-phosphorylated form is CC nuclear (By similarity). Phosphorylation at Ser-229 increases CC transcriptional activity (By similarity). Phosphorylation at Ser-221, CC Ser-243 and Ser-421 decreases signaling capacity (By similarity). CC Phosphorylation at Ser-421 may protect from glucocorticoid-induced CC apoptosis (By similarity). Phosphorylation at Ser-221 and Ser-229 is CC not required in regulation of chromosome segregation (By similarity). CC May be dephosphorylated by PPP5C, attenuates NR3C1 action CC (PubMed:21994940). {ECO:0000250|UniProtKB:P04150, CC ECO:0000269|PubMed:2019585, ECO:0000269|PubMed:21994940}. CC -!- PTM: Sumoylation at Lys-294 and Lys-310 negatively regulates its CC transcriptional activity. Sumoylation at Lys-718 positively regulates CC its transcriptional activity in the presence of RWDD3. Sumoylation at CC Lys-294 and Lys-310 is dispensable whereas sumoylation at Lys-718 is CC critical for the stimulatory effect of RWDD3 on its transcriptional CC activity. Heat shock increases sumoylation in a RWDD3-dependent manner. CC {ECO:0000250|UniProtKB:P06536}. CC -!- PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional CC signaling. {ECO:0000269|PubMed:11555652}. CC -!- POLYMORPHISM: The poly-Gln region in 78-91 is polymorphic CC (PubMed:3780669, PubMed:17012242, PubMed:20660300, PubMed:16141072, CC PubMed:15489334). Polymorphism plays a role in complex mechanisms CC leading to lower corticosterone response to stress, and may also be CC associated with decreased locomotive and increased anxiety-type CC behaviors (PubMed:17012242). {ECO:0000269|PubMed:15489334, CC ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:17012242, CC ECO:0000269|PubMed:20660300, ECO:0000269|PubMed:3780669}. CC -!- MISCELLANEOUS: T-cell is a critical cellular target of GR, as immune CC activation in mice lacking GR resulted in significant mortality. This CC lethal activation is rescued by PTGS2 inhibition but not steroid CC administration or cytokine neutralization. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 1-B]: Produced by alternative initiation at CC Met-28 of isoform 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 2-B]: Produced by alternative initiation at CC Met-28 of isoform 2. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04435; CAA28031.1; -; mRNA. DR EMBL; DQ504162; ABF57998.1; -; mRNA. DR EMBL; HM236293; ADM18962.1; -; mRNA. DR EMBL; AK155200; BAE33113.1; -; mRNA. DR EMBL; AK156323; BAE33674.1; -; mRNA. DR EMBL; GL456180; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC129912; AAI29913.1; -; mRNA. DR EMBL; BC129913; AAI29914.1; -; mRNA. DR EMBL; X13358; CAA31738.1; -; mRNA. DR EMBL; X13359; CAA31739.1; -; mRNA. DR CCDS; CCDS37791.1; -. [P06537-1] DR PIR; A25691; A25691. DR RefSeq; NP_032199.3; NM_008173.3. [P06537-1] DR RefSeq; XP_006525721.1; XM_006525658.1. [P06537-2] DR RefSeq; XP_006525722.1; XM_006525659.3. [P06537-2] DR RefSeq; XP_006525723.1; XM_006525660.2. [P06537-2] DR RefSeq; XP_006525724.1; XM_006525661.2. [P06537-2] DR RefSeq; XP_006525725.1; XM_006525662.1. [P06537-2] DR RefSeq; XP_006525726.1; XM_006525663.3. [P06537-2] DR RefSeq; XP_006525727.1; XM_006525664.1. [P06537-2] DR RefSeq; XP_006525728.1; XM_006525665.3. [P06537-2] DR RefSeq; XP_006525729.1; XM_006525666.3. DR RefSeq; XP_017173324.1; XM_017317835.1. DR RefSeq; XP_017173325.1; XM_017317836.1. DR RefSeq; XP_017173326.1; XM_017317837.1. DR RefSeq; XP_017173327.1; XM_017317838.1. DR PDB; 3MNE; X-ray; 1.96 A; A=536-792. DR PDB; 3MNO; X-ray; 1.55 A; A=536-792. DR PDB; 3MNP; X-ray; 1.50 A; A=536-792. DR PDBsum; 3MNE; -. DR PDBsum; 3MNO; -. DR PDBsum; 3MNP; -. DR AlphaFoldDB; P06537; -. DR SMR; P06537; -. DR CORUM; P06537; -. DR DIP; DIP-11N; -. DR IntAct; P06537; 13. DR MINT; P06537; -. DR STRING; 10090.ENSMUSP00000111229; -. DR BindingDB; P06537; -. DR ChEMBL; CHEMBL3144; -. DR DrugCentral; P06537; -. DR GuidetoPHARMACOLOGY; 625; -. DR GlyGen; P06537; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P06537; -. DR PhosphoSitePlus; P06537; -. DR SwissPalm; P06537; -. DR EPD; P06537; -. DR jPOST; P06537; -. DR MaxQB; P06537; -. DR PaxDb; 10090-ENSMUSP00000095199; -. DR PeptideAtlas; P06537; -. DR ProteomicsDB; 271197; -. [P06537-1] DR ProteomicsDB; 271198; -. [P06537-2] DR ProteomicsDB; 271199; -. [P06537-3] DR ProteomicsDB; 271200; -. [P06537-4] DR ProteomicsDB; 271201; -. [P06537-5] DR ProteomicsDB; 333325; -. DR ProteomicsDB; 355014; -. DR Pumba; P06537; -. DR Antibodypedia; 1329; 1586 antibodies from 44 providers. DR DNASU; 14815; -. DR Ensembl; ENSMUST00000025300.13; ENSMUSP00000025300.7; ENSMUSG00000024431.16. [P06537-1] DR Ensembl; ENSMUST00000097592.9; ENSMUSP00000095199.3; ENSMUSG00000024431.16. [P06537-2] DR Ensembl; ENSMUST00000115567.8; ENSMUSP00000111229.2; ENSMUSG00000024431.16. [P06537-1] DR Ensembl; ENSMUST00000115571.8; ENSMUSP00000111233.2; ENSMUSG00000024431.16. [P06537-1] DR GeneID; 14815; -. DR KEGG; mmu:14815; -. DR UCSC; uc008esx.1; mouse. DR AGR; MGI:95824; -. DR CTD; 2908; -. DR MGI; MGI:95824; Nr3c1. DR VEuPathDB; HostDB:ENSMUSG00000024431; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000156385; -. DR HOGENOM; CLU_020317_0_0_1; -. DR InParanoid; P06537; -. DR OMA; GLYMGDT; -. DR OrthoDB; 5305911at2759; -. DR TreeFam; TF106510; -. DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway. DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors. DR BioGRID-ORCS; 14815; 1 hit in 83 CRISPR screens. DR ChiTaRS; Nr3c1; mouse. DR EvolutionaryTrace; P06537; -. DR PRO; PR:P06537; -. DR Proteomes; UP000000589; Chromosome 18. DR RNAct; P06537; Protein. DR Bgee; ENSMUSG00000024431; Expressed in median eminence of neurohypophysis and 273 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0034056; F:estrogen response element binding; IBA:GO_Central. DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI. DR GO; GO:0042562; F:hormone binding; ISO:MGI. DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI. DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0004883; F:nuclear glucocorticoid receptor activity; IDA:MGI. DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB. DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI. DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030325; P:adrenal gland development; IMP:MGI. DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI. DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISO:MGI. DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI. DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI. DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central. DR GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:MGI. DR GO; GO:0042711; P:maternal behavior; IGI:MGI. DR GO; GO:0014004; P:microglia differentiation; IMP:MGI. DR GO; GO:0061744; P:motor behavior; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0031914; P:negative regulation of synaptic plasticity; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI. DR GO; GO:0150076; P:neuroinflammatory response; IMP:MGI. DR GO; GO:0051647; P:nucleus localization; ISO:MGI. DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI. DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI. DR GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; ISO:MGI. DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IGI:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:CAFA. DR GO; GO:0031946; P:regulation of glucocorticoid biosynthetic process; IMP:MGI. DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:MGI. DR GO; GO:0010906; P:regulation of glucose metabolic process; ISO:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0046685; P:response to arsenic-containing substance; ISO:MGI. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISO:MGI. DR CDD; cd07172; NR_DBD_GR_PR; 1. DR CDD; cd07076; NR_LBD_GR; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR InterPro; IPR001409; Glcrtcd_rcpt. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR48092:SF5; GLUCOCORTICOID RECEPTOR; 1. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. DR Pfam; PF02155; GCR; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00528; GLCORTICOIDR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing; KW Chromatin regulator; Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond; KW Lipid-binding; Metal-binding; Methylation; Mitochondrion; Nucleus; KW Phosphoprotein; Receptor; Reference proteome; Steroid-binding; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..792 FT /note="Glucocorticoid receptor" FT /id="PRO_0000019939" FT DOMAIN 539..773 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 434..509 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 437..457 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 473..497 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..436 FT /note="Modulating" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 67..98 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 148..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..792 FT /note="Interaction with CLOCK" FT /evidence="ECO:0000250" FT REGION 503..538 FT /note="Hinge" FT REGION 547..712 FT /note="Interaction with CRY1" FT /evidence="ECO:0000250" FT MOD_RES 24 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:2019585" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:2019585" FT MOD_RES 168 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:2019585" FT MOD_RES 221 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:2019585, FT ECO:0000269|PubMed:21994940" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:2019585, FT ECO:0000269|PubMed:21994940" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:2019585, FT ECO:0000269|PubMed:21994940" FT MOD_RES 284 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT MOD_RES 324 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:2019585" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 496 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT MOD_RES 508 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT MOD_RES 510 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT MOD_RES 511 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04150" FT CROSSLNK 294 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250|UniProtKB:P04150" FT CROSSLNK 294 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P04150" FT CROSSLNK 310 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250|UniProtKB:P04150" FT CROSSLNK 310 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P04150" FT CROSSLNK 435 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000305|PubMed:11555652" FT CROSSLNK 718 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:P04150" FT VAR_SEQ 1..27 FT /note="Missing (in isoform 1-B and isoform 2-B)" FT /evidence="ECO:0000305" FT /id="VSP_018774" FT VAR_SEQ 467 FT /note="G -> GR (in isoform 2 and isoform 2-B)" FT /evidence="ECO:0000303|PubMed:2911477" FT /id="VSP_003704" FT VAR_SEQ 744..757 FT /note="VENLLSYCFQTFLD -> STKHKSKTTAKKKK (in isoform 3)" FT /id="VSP_058320" FT VAR_SEQ 758..792 FT /note="Missing (in isoform 3)" FT /id="VSP_058321" FT VARIANT 78..86 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:20660300, FT ECO:0000269|PubMed:3780669" FT VARIANT 91 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:17012242" FT MUTAGEN 1 FT /note="M->T: Abolishes expression of A-type isoforms." FT /evidence="ECO:0000269|PubMed:11435610" FT MUTAGEN 28 FT /note="M->T: Abolishes expression of B-type isoforms. 1-B." FT /evidence="ECO:0000269|PubMed:11435610" FT MUTAGEN 435 FT /note="K->A: Abolishes glucocorticoid-mediated degradation FT and enhances transcription trans-activation." FT /evidence="ECO:0000269|PubMed:11555652" FT MUTAGEN 493 FT /note="R->A: Abolishes transactivation activity." FT /evidence="ECO:0000269|PubMed:25676786" FT MUTAGEN 493 FT /note="R->C: Abolishes transcriptional activity. Does not FT impair ligand binding." FT /evidence="ECO:0000269|PubMed:25676786" FT MUTAGEN 493 FT /note="R->K: Does not change transactivation activity." FT /evidence="ECO:0000269|PubMed:25676786" FT CONFLICT 432 FT /note="P -> L (in Ref. 4; BAE33674)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="G -> V (in Ref. 1; CAA28031)" FT /evidence="ECO:0000305" FT CONFLICT 792 FT /note="K -> E (in Ref. 4; BAE33674)" FT /evidence="ECO:0000305" FT HELIX 547..554 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 571..594 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 599..601 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 604..631 FT /evidence="ECO:0007829|PDB:3MNP" FT STRAND 634..639 FT /evidence="ECO:0007829|PDB:3MNP" FT STRAND 642..644 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 646..649 FT /evidence="ECO:0007829|PDB:3MNP" FT TURN 652..654 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 655..671 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 675..686 FT /evidence="ECO:0007829|PDB:3MNP" FT STRAND 688..691 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 698..717 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 723..756 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 758..760 FT /evidence="ECO:0007829|PDB:3MNP" FT HELIX 766..780 FT /evidence="ECO:0007829|PDB:3MNP" FT STRAND 784..786 FT /evidence="ECO:0007829|PDB:3MNP" SQ SEQUENCE 792 AA; 87164 MW; 528730BD2C517554 CRC64; MDSKESLAPP GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA AASQADSKQQ RILLDFSKGS ASNAQQQQQQ QQQQQQQQQQ QPQPDLSKAV SLSMGLYMGE TETKVMGNDL GYPQQGQLGL SSGETDFRLL EESIANLNRS TSRPENPKSS TPAAGCATPT EKEFPQTHSD PSSEQQNRKS QPGTNGGSVK LYTTDQSTFD ILQDLEFSAG SPGKETNESP WRSDLLIDEN LLSPLAGEDD PFLLEGDVNE DCKPLILPDT KPKIQDTGDT ILSSPSSVAL PQVKTEKDDF IELCTPGVIK QEKLGPVYCQ ASFSGTNIIG NKMSAISVHG VSTSGGQMYH YDMNTASLSQ QQDQKPVFNV IPPIPVGSEN WNRCQGSGED NLTSLGAMNF AGRSVFSNGY SSPGMRPDVS SPPSSSSTAT GPPPKLCLVC SDEASGCHYG VLTCGSCKVF FKRAVEGQHN YLCAGRNDCI IDKIRRKNCP ACRYRKCLQA GMNLEARKTK KKIKGIQQAT AGVSQDTSEN ANKTIVPAAL PQLTPTLVSL LEVIEPEVLY AGYDSSVPDS AWRIMTTLNM LGGRQVIAAV KWAKAIPGFR NLHLDDQMTL LQYSWMFLMA FALGWRSYRQ ASGNLLCFAP DLIINEQRMT LPCMYDQCKH MLFISTELQR LQVSYEEYLC MKTLLLLSSV PKEGLKSQEL FDEIRMTYIK ELGKAIVKRE GNSSQNWQRF YQLTKLLDSM HDVVENLLSY CFQTFLDKSM SIEFPEMLAE IITNQIPKYS NGNIKKLLFH QK //