Receptor for glucocorticoids (GC) (PubMed:7649084, PubMed:8766708). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (By similarity). Affects inflammatory responses, cellular proliferation and differentiation in target tissues (By similarity). Involved in chromatin remodeling (By similarity). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). Mediates glucocorticoid-induced apoptosis (By similarity). Promotes accurate chromosome segregation during mitosis (By similarity). May act as a tumor suppressor (By similarity). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity). Heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C. Upon ligand binding FKBP5 dissociates from the complex and FKBP4 takes its place, thereby linking the complex to dynein and mediating transport to the nucleus, where the complex dissociates. Directly interacts with UNC45A. Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers. Interacts with NRIP1, POU2F1, POU2F2 and TRIM28. Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6. Interaction with BAG1 inhibits transactivation. Interacts with HEXIM1, PELP1 and TGFB1I1. Interacts with NCOA1, NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (By similarity). After ligand activation, translocates from the cytoplasm to the nucleus. Isoform 1 is expressed in all tissues tested including liver, gills, intestine, skeletal muscle, kidney, heart, spleen, stomach, brain, pituitary, ovary, testis, skin and bladder. Isoform 2 is found only in testis. Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The ligand-binding domain is required for correct chromosome segregation during mitosis although ligand binding is not required. Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. May be dephosphorylated by PPP5C, attenuates NR3C1 action (By similarity). Belongs to the nuclear hormone receptor family. NR3 subfamily.