Receptor for glucocorticoids (GC) (PubMed:8018720). 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 HSP90. Upon ligand binding the complex undergoes a conformation change and moves to the nucleus, where it dissociates. Binds to DNA as a homodimer, and as heterodimer with NR3C2. Interaction with numerous other transcription factors modulates transcription activation (By similarity). After ligand activation, translocates from the cytoplasm to the nucleus. Expressed in liver with relative abundance. Rareley expressed between embryonic stages 17 and 24. Expression starts from stage 32. 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. Belongs to the nuclear hormone receptor family. NR3 subfamily.