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CCR6 belongs to the beta chemokine receptor family, which is predicted to be a 7 transmembrane protein similar to G protein-coupled receptors. CCR6 is preferentially expressed by immature dendritic cells and memory T cells. The ligand of CCR6 receptor is macrophage inflammatory protein 3 alpha (MIP-3 alpha). CCR6 receptor has been shown to be vital for B-lineage maturation and antigen-driven B-cell differentiation, and it may regulate the migration and recruitment of dentritic and T cells during inflammatory and immunological responses.

The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.

CD33 is putative adhesion molecule of myelomonocytic-derived cells which mediates sialic-acid dependent binding to cells. CD33 prefers to bind to alpha-2,6-linked sialic acid. The sialic acid recognition site is masked by cis interactions with sialic acids on the same cell surface. In the immune response, CD33 perform as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatases through their SH2 domains which block signal transduction through dephosphorylation of signaling molecules. In addition, CD33 induces apoptosis in acute myeloid leukemia.

CD207 (C-type lectin domain family 4 member K) is expressed in Langerhans cells which are immature dendritic cells of the epidermis and mucosa. Moreover, CD207 is expressed in several other dendritic cell types including dermal CD103+ DCs and splenic CD8+ DCs. Langerin is localized in the Birbeck granules, the organelles present in the cytoplasm of Langerhans cells and comprised of superimposed and zippered membranes. CD207 is a C-type lectin with mannose binding specificity, and it has been suggested that mannose binding by the CD207 protein leads to internalization of antigen into Birbeck granules thus providing access to a nonclassical antigen-processing pathway.

Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.

Smac/Diablo is a proapoptotic protein that increases caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway by its binding to the inhibitor of apoptosis proteins (IAPs) and removing their inhibitory activity. Smac/Diablo is a mitochondrial protein which enters the cytosol when cells go through apoptosis, and it moderates the caspase inhibition of IAPs.Smac/DIABLO expression is associated with the result of renal cell carcinoma.Dimeric form of Smac/DIABLO implies that once expressed in the cell the protein has a little probability of dissociation and, thus, loss of function. Survivin, Smac/DIABLO, & PKC-? play an important part in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells. Mitochondrial survivin associates with Smac/DIABLO, delaying its release. Decreased expression of Smac protein takes part in ovarian carcinogenesis and chemotherapeutic resistance. Smac/DIABLO plays a role in tumor cells during the pathway of apoptosis induction. SMAC protein is regulated by XIAP and degraded by proteasome. SMAC protein takes part inleukemic cell apoptosis. Smac is released during stress-induced apoptosis in multiple myeloma cells.

AXIN1 is a cytoplasmic protein, which contains a regulation of G-protein signaling (RGS) domain and a dishevelled and axin (DIX) domain. Axin1 is has been characterized as a tumor suppressor. In addition, Axin1 has an essential role in the formation of the embryonic neural axis. It has also been reported that Axin is found in mitotic spindles and centrosomes. AXIN1 interacts with adenomatosis polyposis coli, catenin beta-1, glycogen synthase kinase 3 beta, protein phosphate 2, and itself. AXIN1 functions as a negative regulator of the WNT1 signaling pathway and is able to induce apoptosis. Axin can be identified in a mouse mutant strain, created by random integration of a transgene. Mutations in the AXIN1 gene are linked to hepatocellular carcinoma, hepatoblastomas, ovarian endometriod adenocarcinomas, and medullablastomas.

NTAL participates in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. NTAL takes part in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.

CD40 belongs to the TNF-receptor super family. CD40 has been found to be vital in mediating a wide range of immune and inflammatory responses including T cell-dependent immunoglobulin classswitching, memory B cell development, and germinal center formation. AT-hook transcription factor AKNA isaccounted to coordinately regulate the expression of CD40 and its ligand, which is significant forhomotypic cell interactions. Adaptor protein TNFR2 interacts with CD40 and functions as a mediator of thesignal transduction. The interaction of CD40 and its ligand is found to be essential for amyloid-beta-inducedmicroglial activation, and therefore is considered to be an early event in Alzheimer disease pathogenesis.

Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

Hepatitis A Virus Cellular Receptor 2 (HAVCR2) is a member of the immunoglobulin superfamily. HACVR2 controls macrophage activation. HACVR2 inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and stimulates immunological tolerance.

CD52 is a small GPI (glycosylphosphatidylinositol) anchored glycoprotein which is tied to the cell surface with a GPI linkage. CD52 induces immune suppression by complement-meditated cell lysis. Moreover, CD52 is expressed on lymphocytes, eosinophils, monocytes-derived dendritic cells, monocytes, as well as neutrophils, however not on the stem cells from which these lymphocytes were derived. Furthermore, CD52 is a significant goal for therapeutic interventions intended for leukocyte depletion in post-transplant immunosuppression & hematological malignancies.

LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.

Synovial Sarcoma, X Breakpoint 2 (SSX2) is a part of the family of highly homologous synovial sarcoma X breakpoint proteins which play a role as transcriptional repressors. Homologous synovial sarcoma X breakpoint proteins are also able to bring out spontaneous humoral and cellular immune responses in cancer patients, and are effective targets in cancer vaccine-based immunotherapy.

Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.

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.

CD80 which is a member of cell surface immunoglobulin superfamily takes part in the costimulatory signal essential for T-lymphocyte activation. CD80 binds to either human or mouse CD28 and CTLA-4 – binding to CD28 induces T-cell proliferation and cytokine production while binding to CTLA-4 inhibits T-cell activation. CD80 is expressed on activated B cells, activated T cells, and macrophages.

CD8B encodes the CD8 beta chain isoforms of the CD8 antigen. CD8 is a cell surface glycoprotein which facilitates efficient cell-cell interactions within the immune system and is located on most cytotoxic T lymphocytes. The T-cell receptor on the T lymphocyte and the co-receptor CD8 antigen identify antigens exposed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional co-receptor is either a heterodimer composed of one alpha and one beta chain or a homodimer composed of two alpha chains. Both alpha and beta chains share substantial homology to immunoglobulin variable light chains.

CD3D, also known as Delta Polypeptide (TiT3 Complex), is a single-pass type 1 membrane protein. CD3D jointly with CD3-zeta, CD3-gamma, CD3-epsilon and the T-cell receptor alpha/beta and gamma/delta heterodimers, creates the T-cell receptor-CD3 complex. Once antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transferred through the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. Likewise, CD3D takes an important part in adaptive immune response and participates in thymocyte differentiation.

PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.

B2M is a part of the MHC class I family that participates in the presentation of peptide antigens to the immune system. B2M is localized on the surface of numerous cells and abundant on the surface of white blood cells. High production or destruction of these cells causes B2M levels in the blood to raise. This increase is observed in people with cancers involving white blood cells, but it is mainly significant in people newly diagnosed with multiple myeloma. B2M Testing is done primarily when evaluating a person for certain kinds of cancer affecting white blood cells including chronic lymphocytic leukemia, non-Hodgkin''s lymphoma, and multiple myeloma or kidney disease.

SLAMF7 belongs to the CS2 family of cell surface receptors. SLAMF7 is a single-pass type 1 membrane protein, SLAMF7 Isoform 1 mediates NK cell activation via aSH2D1A-independent extracellular signal-regulated ERK-mediated pathway. SLAMF7 functions in lymphocyteadhesion. Furthermore, SLAMF7 can exert activating of inhibitory influences on cells of the immune system depending on cellular context as well as the availability of effector proteins.

ABI gene family member 3 (ABI3) is a member of the ABI family. Members of the ABI family encode proteins which contain a homeobox homology domain, proline rich region and Src-homology 3 (SH3) domain. Abi family members are assumed to negatively regulate cell growth and transformation, including cellular transformation through v-Abl as well controlling as mediate cell motility by regulating actin polymerization in lamellipodia and filopodia. ABI3 impedes ectopic metastasis of tumor cells as well as cell migration, which is accomplished through interaction with p21-activated kinase.