STING has several transmembrane domains, and is expressed in a variety of endothelial cells, epithelial cells and hematopoietic liver cells. STING participates in the DNA-mediated innate immune response. Non-CpG double-stranded DNA from viruses or bacteria binds to cGAS protein and is catalyzed to the second messenger cGAMP; then the dimerized STING binds to cGAMP and undergoes conformational changes. Through the autophagsome and the endoplasmic reticulum and the Golgi apparatus, it further enters the cytoplasm. During the period, it is ubiquitinated and recruited TBK1 protein, then phosphorylated, and then combined with IRF3; then IRF3 is phosphorylated and enters the nucleus to induce the expression of IFNs, etc. In conclusion, it can enhance the body's immune ability and kill bacteria, viruses and other pathogens to a greater extent.
Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90.
STK3(serine/threonine kinase 3) Homo sapiens This gene encodes a serine/threonine protein kinase activated by proapoptotic molecules indicating the encoded protein functions as a growth suppressor. Cleavage of the protein product by caspase removes the inhibitory C-terminal portion. The N-terminal portion is transported to the nucleus where it homodimerizes to form the active kinase which promotes the condensation of chromatin during apoptosis. Multiple transcript variants encoding different isoforms have been found for this gene.
The protein encoded by this gene is a cytoplasmic kinase that is structurally similar to the yeast Ste20p kinase, which acts upstream of the stress-induced mitogen-activated protein kinase cascade. The encoded protein can phosphorylate myelin basic protein and undergoes autophosphorylation. A caspase-cleaved fragment of the encoded protein has been shown to be capable of phosphorylating histone H2B. The particular phosphorylation catalyzed by this protein has been correlated with apoptosis, and it's possible that this protein induces the chromatin condensation observed in this process.
Enables GTPase binding activity; T cell receptor binding activity; and cardiolipin binding activity. Involved in intracellular calcium ion homeostasis; mitochondrion organization; and protein complex oligomerization. Acts upstream of or within T cell receptor signaling pathway. Located in several cellular components, including immunological synapse; membrane raft; and mitochondrial envelope.
Phosphinothricin N-acetyltransferase (PAT) is an enzyme that acetylates the free NH2 group of L-phosphinothricin (L-PPT) in the presence of acetyl-CoA as a co-substrate. It is highly specific for L-PPT and does not acetylate other L-amino acids or structurally similar molecules. L-PPT is a glutamate analog that can inhibit glutamine synthetase activity in plants, resulting in the accumulation of ammonia to toxic levels and impairment of photosynthesis. The introduction of a PAT gene into a plant genome can confer resistance to glufosinate herbicide during post-emergent applications.
This gene encodes a type 1 transmembrane protein that mediates Ca2+ influx after depletion of intracellular Ca2+ stores by gating of store-operated Ca2+ influx channels (SOCs). It is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. This gene may play a role in malignancies and disease that involve this region, as well as early hematopoiesis, by mediating attachment to stromal cells. Mutations in this gene are associated with fatal classic Kaposi sarcoma, immunodeficiency due to defects in store-operated calcium entry (SOCE) in fibroblasts, ectodermal dysplasia and tubular aggregate myopathy. This gene is oriented in a head-to-tail configuration with the ribonucleotide reductase 1 gene (RRM1), with the 3' end of this gene situated 1.6 kb from the 5' end of the RRM1 gene. Alternative splicing of this gene results in multiple transcript variants.
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