HMGA1 a chromatin-associated protein involved in the regulation of gene transcription, integration of retroviruses into chromosomes, and the metastatic progression of cancer cells. HMGA1 preferentially binds to the minor groove of AT-rich regions in double-stranded DNA.
HMGB1(high mobility group box 1) Homo sapiens. This gene encodes a protein that belongs to the High Mobility Group-box superfamily. The encoded non-histone, nuclear DNA-binding protein regulates transcription, and is involved in organization of DNA. This protein plays a role in several cellular processes, including inflammation, cell differentiation and tumor cell migration. Multiple pseudogenes of this gene have been identified. Alternative splicing results in multiple transcript variants that encode the same protein.
High mobility group (HMG) proteins 1 and 2 are ubiquitous non-histone components of chromatin. Evidence suggests that the binding of HMG proteins to DNA induces alterations in the DNA architecture including DNA bending and unwinding of the helix. HMG proteins synergize with Oct-2, members of the NFB family, ATF-2 and c-Jun to activate transcription. Other studies indicate that phosphorylation of HMG protein is required to stimulate the transcriptional activity of the protein. Human HMG-1 and HMG-2 both contain two DNA-binding domains, termed HMG boxes. HMG proteins bind single-stranded DNA but induce conformational changes in double-stranded DNA alone.
Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury.
HMGB2 belongs to a family of highly conserved proteins that contain HMG box domains. HMGB2 is widely expressed during embryonic development, but it is restricted to lymphoid organs and testis in adult animals. HMGB2 facilitate the binding of Hox proteins, Oct proteins, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters. Furthermore, HMGB2 interacts with RAG1 to facilitate RAG complex binding to the recombinant signal sequence (RSS) and stimulate DNA-bending and subsequent VDJ cleavage at antigen receptor genes. In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation. HMGB2 is secreted by myeloid cells and promotes proliferation and migration of endothelial cells by binding to the receptor for advanced glycation end products (RAGE).
3-Hydroxy-3-methylglutaryl-CoA reductase (HMGCR) is a transmembrane glycoprotein of the endoplasmic reticulum. It is the rate-limiting enzyme for cholesterol biosynthesis and non-sterol isoprenoid biosynthesis. Play a key role in cellular cholesterol homeostasis. The activity of HMGCR is regulated by negative feedback, in which cholesterol and other end products of the metabolic pathway inhibit the activity of HMGCR in a multivalent manner. Cholesterol inhibits reductase activity mainly by inhibiting the transcription rate of HMGCR gene. HMGCR is the main target of statins, which are a class of cholesterol-lowering drugs.
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