Stromal interaction molecule 1, also known as STIM1 and GOK, is a cell membrane, a single-pass type I membrane protein and a endoplasmic reticulum membrane protein. STIM1 / GOK is ubiquitously expressed in various human primary cells and tumor cell lines. It contains oneEF-hand domain and oneSAM (sterile alpha motif) domain. STIM1 / GOK plays a role in mediating Ca2+influx following depletion of intracellular Ca2+stores. It acts as Ca2+sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca2+depletion, STIM1 / GOK translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca2+release-activated Ca2+(CRAC) channel subunit, TMEM142A / ORAI1. Transfection of STIM1 / GOK into cells derived from a rhabdoid tumor and from a rhabdomyosarcoma that do not express detectable levels of STIM1 can induce cell death, suggesting a possible role in the control of rhabdomyosarcomas and rhabdoid tumors. Defects in STIM1 are the cause of immune dysfunction with T-cell inactivation due to calcium entry defect type 2 (IDTICED2) which is an immune disorder characterized by recurrent infections, impaired T-cell activation and proliferative response, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels.
Stimulator of Interferon Gene(Sting,TMEM173) belongs to the TMEM173 family. STING is 379 amino acids (aa) in length. It contains an N-terminal cytoplasmic region (aa 1-20), four transmembrane segments (aa 21-173), and a C-terminal cytoplasmic domain (aa 174-379). It ubiquitously expressed in skin endothelial cells, alveolar type 2 pneumocytes, bronchial epithelium and alveolar macrophagesand. Its subunit structure associated with the MHC-II complex and Interacts with DDX58/RIG-I, MAVS and SSR2, RNF5 and TRIM56 along with TBK1. This type of protein often uses as facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon.
Serine / threonine-protein kinase 10, also known as Lymphocyte-oriented kinase, STK10 and LOK, which belongs to theprotein kinase superfamily, STE Ser / Thr protein kinase family and STE20 subfamily. Protein kinases constitute a large superfamily of enzymes with key regulatory functions in nearly all signal transmission processes of eukaryotic cells. The Ste20 family of serine/threonine kinases plays an important role in numerous cellular functions such as growth, apoptosis, and morphogenesis. STK10 is similar to several known polo-like kinase kinases. It can associate with and phosphorylate polo-like kinase 1, and overexpression of a kinase-dead version of the protein interferes with normal cell cycle progression. STK10 can also negatively regulate interleukin 2 expression in T-cells via the mitogen activated protein kinase kinase 1 pathway. Stk10 can associate with Plk1 in cells and furthermore can phosphorylate Plk1. It can also act on substrates such as myelin basic protein and histone 2A on serine and threonine residues.
Serine/threonine-protein kinase 16, also known as myristoylated and palmitoylated serine/threonine-protein kinase, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, MPSK1 and STK16, is a membrane protein which is ubiquitously expressed at very low levels. STK16 / MPSK1 belongs to theprotein kinase superfamily and Ser/Thr protein kinase family. It contains oneprotein kinase domain. Transforming growth factor-beta (TGF-beta) shows a variety of biological activities in various organs or cells. Some factors such as Smads and TGF-beta activating kinase 1 have been characterized as signalling molecules downstream of TGF-beta. Several TGF-beta response elements have been identified such as cAMP response element, Smad binding element, and recognition sites for activating protein-1 and stimulating protein-1 in various gene promoters. STK16 / MPSK1 is an unique factor with two biological functions, transcriptional regulation and protein phosphorylation, that may be involved in TGF-beta signals. STK16 / MPSK1 is a protein kinase that act on both serine and threonine residues. STK16 / MPSK1 possessed DNA-binding ability and activated the TGF-beta responsive CNP promoter or vascular endothelial growth factor gene promoter which possesses a sequence element analogous to the TGF-beta responsive GC-rich element of the CNP promoter. STK16 / MPSK1 did not directly activate a Smads-dependent promoter from plasminogen activator inhibitor 1 gene, but it showed enhancement in co-operation with Smad3 and Smad4. STK16 / MPSK1 mRNA as well as its protein level were stimulated by TGF-beta treatment.
Serine / threonine-protein kinase SRPK3, also known as Muscle-specific serine kinase 1, Serine/arginine-rich protein-specific kinase 3, SR-protein-specific kinase 3, Serine / threonine-protein kinase 23, MSSK-1, SRPK3 and MSSK1, is a member of the protein kinase superfamily and CMGC Ser / Thr protein kinase family. SRPK3 is a protein kinase belonging to serine/arginine protein kinases (SRPK) family, which phosphorylates serine / arginine repeat-containing proteins, and is controlled by a muscle-specific enhancer directly regulated by MEF2. SRPK3 / MSSK1 contains oneprotein kinase domain. SRPK3 / MSSK1 is exclusively expressed in skeletal and heart muscle. It is required for normal muscle development. Myocyte enhancer factor 2 (MEF2) plays essential roles in transcriptional control of muscle development. Normal muscle growth and homeostasis require MEF2-dependent signaling by SRPK3.
MST3 encodes a serine/threonine protein kinase that functions upstream of mitogen-activated protein kinase (MAPK) signaling. The encoded protein is cleaved into two chains by caspases; the N-terminal fragment (MST3/N) translocates to the nucleus and promotes programmed cells death. There is a pseudogene for this gene on chromosome X. Alternative splicing results in multiple transcript variants.
STK40 localized to both the cytoplasm and the nucleus. It is ubiquitously expressed. Mechanistically, Stk40 interacts with Rcn2, which also activates Erk1/2 to induce ExEn specification in mouse ESCs. Stk40 is able to activate the Erk/MAPK pathway and induce extraembryonic-endoderm (ExEn) differentiation in mouse ESCs. Interestingly, cells overexpressing Stk40 exclusively contribute to the ExEn layer of chimeric embryos when injected into host blastocysts. In contrast, deletion of Stk40 in ESCs markedly reduces ExEn differentiation in vitro. STK40 has a central serine/threonine protein kinase domain and is homologous to TRB-3, a protein that regulates activation of MAP kinases and inhibits NFκB-mediated gene transcription. Similarly, overexpression of STK40 inhibits NFκB activation triggered by TNF and also inhibits p53-mediated transcription. There are four named isoforms of STK40 that are produced as a result of alternative splicing.
MST1 protein encoded by this gene contains four kringle domains and a serine protease domain, similar to that found in hepatic growth factor. Despite the presence of the serine protease domain, the encoded protein may not have any proteolytic activity. The receptor for this protein is RON tyrosine kinase, which upon activation stimulates ciliary motility of ciliated epithelial lung cells. This protein is secreted and cleaved to form an alpha chain and a beta chain bridged by disulfide bonds.
Stathmin (STMN1) is a ubiquitous cytosolic phosphoprotein which belongs to the Stathmin family. STMN1 is expressed in many tissues, with the highest expression in the brain, spinal cord, and cerebellum. It can also be expressed in the colon, ovary, placenta, uterus, and trachea. STMN1 participates in the regulation of the microtubule filament structure by destabilizing microtubules. STMN1 promotes the disassembly of microtubules and prevents assembly. STMN1 is involved in the control of the learned and innate fear. STMN1 is an intracellular relay integrating regulatory signals of the cellular environment and as an Oncoprotein in regulation of the cell cycle. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Mutation in STMN1 effects cell homeostasis that may lead to tumorigenicity.
E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.
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