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EBAG9 is a type III transmembrane protein that is primarily located in the Golgi. EBAG9 is a tumor-associated antigen that is expressed at high frequency in a variety of cancers, such as advanced breast and prostate cancers. while the EBAG9 acts to inhibit the growth of receptor-binding cells and induced apoptosis of immune cells, cancer cells may evade immune surveillance. Thus immunodetection of EBAG9 expression can be a negative prognostic indicator. EBAG9 promotes progression of bladder cancer. In rheumatoid arthritis, the deficiency of EBAG9 induces CTL infiltration through failure to evade immune attack, therefore leading to apoptosis of the synovial lining cells. EBAG9 is involved in controlling exocytosis processes. EBAG9 expression plays a role in the progression of oral squamous cell carcinoma. EBAG9 plays a specific role in premature stages of breast carcinogenesis.

EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

Cell surface glycoprotein MUC18 (MCAM), is an integral membrane glycoprotein which is part of the immunoglobulin superfamily. MCAM is related with a variety of carcinomas such as tumor progression, metastasis and is also implicated in embryonic neural development. In Addition, MCAM takes part in cell adhesion, as well as in cohesion of the endothelial monolayer at the intercellular junctions in vascular tissue.

Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.

ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

Vesicle-Associated Membrane Protein 7 (VAMP7) is a member of the synaptobrevin family. VAMP7 is a transmembrane protein, which is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family. VAMP7 is involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. VAMP7 localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. VAMP7 is essential for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. It is also necessary for calcium regulated lysosomal exocytosis. In addition, VAMP7 is involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Furthermore, VAMP7 is needed for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells.

VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

Calponin 2 also known as CNN2 protein is capable of binding actin, calmodulin, troponin C, and tropomyosin, and also function in the structural organization of actin filaments. Furthermore, the interaction of CNN2 with actin inhibits the actomyosin Mg-ATPase activity. CNN2 takes part in smooth muscle contraction and cell adhesion. Two transcript variants encoding different isoforms have been found for this gene.

Advanced Glycosylation End Product-Specific Receptor or RAGE is an immunoglobulin, part of the immunoglobulin transmembrane proteins family. RAGE moderates interactions between advanced glycosylation end products, also known as AGE. These signaling has a crucial part in the regulation of TNFalpha,oxidative stress, endothelial dysfunction in type 2 diabetesproduction and expression. RAGE helps the translocation of ABPP (amyloid-beta peptide) through the membrane of cells to the intracellular area in the cortical neurons.

Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.

RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.

Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

RAN Binding Protein 3, also known as RANBP3, is found in the nucleus and cytoplasm. RANBP3 which owns RanBD1 domain participates in nuclear export as part of a heteromeric complex. RANBP3 is also negatively regulates TGF-beta signaling by interacting with the R-SMAD proteins, SMAD2 and SMAD3.