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IL-12 is a heterodimeric cytokine that stimulates the production of IFN gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

TGFBR2 is part of the Ser/Thr protein kinase family and the TGFB receptor subfamily. TGFBR2 is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 expression is increased in oral squamous cell carcinoma cells. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity of tamoxifen metabolites in breast cancer.

TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

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.

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.

Nuclear receptor binding factor 2 (NRBF2) which works as transcriptional activator, modulates transcriptional activation by target nuclear receptors.

CD93, is a receptor or else an element of a larger receptor complex for C1q, MBL2-mannose-binding lectin and SPA-pulmonary surfactant protein A. CD93 mediates the enhancement of phagocytosis in monocytes as well as macrophages upon interaction with soluble defense collagens. CD93 takes part in the intercellular adhesion. Furthermore, CD93 was expressed on (pre) plasmablasts/plasma cells, including long-lived plasma cells which demonstrated decreased cell cycle activity, high levels of isotype-switched Ig secretion, as well as modification of the transcriptional network. CD93 is vital for the maintenance of plasma cells in bone marrow niches.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DL1 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, p58.1, cl-42, NKAT1, or KIR-K6), which recognizes class I MHC molecules (HLA-Cw2, -Cw4, -Cw5, and Cw6). The extracellular domain of KIR2DL1 was over expressed as insoluble protein aggregates (inclusion bodies).

GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DS4 is an activating Killer Cell Ig-like Receptor (KIR, previously called p50 KIR, p50.3, cl39, or KAR-K1), which may recognize class I MHC molecules. KIR2DS4 does not inhibit the activity of NK cells.

Epidermal Growth Factor­like Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake.

Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Zinc Finger HIT-Type Containing 3 (ZNHIT3) which contains one HIT-type zinc finger, requires the presence of thyroid hormone for its interaction. Thyroid receptor interacting proteins particularly interact with the ligand binding domain of the thyroid receptor (TR).

RAMP belongs to the type I transmembrane family of proteins called RAMP (receptor/calcitonin activity modifying proteins) which include an extracellular N terminus and a cytoplasmic C terminus. RAMPs are essential for CRLR transport to the plasma membrane. CRLR (calcitonin-receptor-like receptor) has seven transmembrane domains. Depending on which members of the RAMP family are expressed CRLR receptor functions as either an adrenomedullin receptor or a calcitonin-gene-related peptide (CGRP) receptor. In the presence of RAMP1, CRLR functions as a CGRP receptor. The RAMP1 protein takes part in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.

Receptor-associated Protein (aka RAP) averts the GCM-mediated enhancement of axon growth- ApoE-containing lipoproteins which are known to bind to receptors of the LDLr superfamily. In the presence of RAP, GCM doesn’t increase the axon extension rate in relation to base medium. Furthermore, the addition of RAP to the base medium doesn’t change the rate of axon extension. This implies that the growth stimulatory effect of apoE-containing lipoproteins secreted by glial cells is mediated by the LDLr family receptors. RAP annuls the growth stimulatory effect of GCM.

FGFR1 oncogene partner (FGFR1OP) is a member of the FGFR1OP family. The FGFR1OP protein is an essentially hydrophilic protein proposed to be a leucine-rich protein family member. A t(6;8)(q27;p11) chromosomal translocation, fusing the FGFR1OP gene and the FGFR1 gene, is seen in cases of myeloproliferative disorder. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP gene is believed to play a significant role in normal proliferation and differentiation of the erythroid lineage.

Cluster of Differentiation 244 (CD244/Natural Killer Cell Receptor 2B4) contains 2 Ig-like (immunoglobulin-like) domains. CD244 is a cell surface receptor expressed on natural killer (NK) cells (and some T cells) which mediate non-major histocompatibility complex (MHC) restricted killing. NK-cell and target cells interaction via the CD244 receptor is believed to modulate NK-cell cytolytic activity. CD244 molecules function in eosinophil adhesion and chemotaxis, and have a role in the pathophysiology of allergic rhinitis (AR).

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Milk fat globule-EGF factor 8 protein (Mfge8) is pleiotropic secreted glycoprotein which promotes mammary gland morphogenesis, angiogenesis, and tumor progression. Mfge8 has also an imperative role in tissue homeostasis and the prevention of inflammation. Mfge8 functions as a bridge between phosphatidylserine on apoptotic cells and Integrin alpha V beta 3 on phagocytes, leading to the clearance of apoptotic debris.

Osteoclast-associated immunoglobulin-like receptor isoform 6 or OSCAR, is a receptor for surfactant protein D that can be found on human myeloid cells. OSCAR is part of the TNF-α release from human CCR2+ inflammatory monocytes process. The protein is involved in antigen presentation and activation of dendritic cells. Preosteoclasts or mature osteoclasts express the OSCAR protein. Patients that suffer from RA (rheumatoid arthritis) has upregulations on monocytes which present increased proosteoclastogenic potential.

Tumor necrosis factor receptor superfamily member 21 or TNFRSF21, is a protein that located in the cell membrane from the TNF receptor superfamily. By activating the NF-kappaB pathway, TNFRSF21 promotes cell apoptosis. The degeneration of cells caused by activating caspase 3 and caspase 6, the TNFRSF21 binds to the N-terminal APP in neuronal cell bodies and axons which leads to apoptosis. TNFRSF21 takes part in signaling cascades activated by stimulation of T-cell receptor.