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FGFR1, also called fibroblast growth factor receptor 1 protein is encoded by the FGFR1 Gene. There are 4 types of related proteins (fibroblast growth factor receptors), one of them is the FGFR1 protein. The fibroblast growth factor receptors are responsible for many key cell pathways and processes, cell growth regulations, maturation processes, cell division, embryonic development, blood vessels formations etc.

Mesenchymal epithelial transition factor (c-MET) is a proto-oncogenic receptor tyrosine kinase. The endogenous ligand for c-MET is HGF (hepatocyte growth factor), which is a disulfide-linked heterodimeric molecule produced predominantly by mesenchymal cells. In the adult, c-MET protein expression is limited to stem and progenitor cells and is required for wound healing and hepatocyte regeneration. In the embryo, c-MET receptors are expressed on cells of epithelial origin, which are vital for invasive growth and mediate epithelial-mesenchymal transition (EMT). Abnormal activation of the HGF/MET pathway leads to a variety of cancers. c-MET mutation is linked with a poor prognosis since it can trigger tumor growth, angiogenesis and metastasis.

The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, HBEGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide (FCER1A) binds to the Fc region of immunoglobulins epsilon. FCER1A is a high affinity receptor. In addition FCER1A is responsible for starting the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators such as histamine which is responsible for the manifestations of allergy. This receptor is contains of an alpha subunit, a beta subunit, and two gamma subunits. FCER1A stands for the alpha subunit. Among the diseases associated with FCER1A are mast-cell leukemia, and allergic asthma.

The B7 proteins are crucial in the regulation of the adaptive immune system. Among them is NCR3LG1. NCR3LG1 is part of the B7 family and is expressed on tumor cells. NCR3LG1 Interaction with NKp30 protein results in cytotoxicity and natural killer cell activation.Humans and rats have a single NCR3LG1 gene; though, numerous B7H6 genes were detected in a single large cluster in the Xenopus genome. NCR3LG1, a ligand for the NK cell activating receptor NKp30, targest to produce CAR that targets multiple tumor types. NCR3LG1 is expressed on many primary human tumors, including leukemia, lymphoma and gastrointestinal stromal tumors, though it is not constitutively expressed on normal tissues.

Protein Tyrosine Phosphatase Receptor Type C, also known as PTPRC, which is a vital regulator of T- and B-cell antigen receptor signaling, is also a part of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules which regulate a variety of cellular processes including differentiation, cell growth, mitosis, and oncogenic transformation. PTPRC contains an extracellular domain, a single transmembrane segment and 2 tandem intracytoplasmic catalytic domains, and therefore is classified as a receptor type PTP.

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).

GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

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.

The retinoid X receptor (RXR) is a pleiotropic nuclear receptor transcription factor that interacts with a variety of nuclear receptor dimeric partner. RXR binds cognate response elements as a homodimer in the presence of its ligand, 9-cis retinoic acid, or as a heterodimer with other members of the nuclear hormone receptor superfamily including retinoic acid receptors (RAR), thyroid hormone receptors (TR), vitamin D receptors and peroxisome proliferators-activated receptors (PPAR). The RXR family includes three different isoforms; RXR a, b, g . Human RXR a gene is localized on 9q34.9 and encodes two major isoforms (RXR a1, RXR a2). The DNA binding domain of RXR (111-228aa) was purified by using conventional column chromatography techniques.

Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.

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.

Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

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.

Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

LAIR1 is a glycoprotein expressed on the surface of the majority of human peripheral blood mononuclear leukocytes including T cells, B cells, NK cells, macrophages and dendritic cells. LAIR-1 functions as an inhibitory receptor in NK cells, T cells and B cells. Inhibitory receptors control the immune response to prevent lysis of cells recognized as self. Lair1 consists of a leader sequence, extracellular domain, transmembrane domain, cytoplasmic region.LAIR1 is a member of both the immunoglobulin superfamily and the leukocyte-associated inhibitory receptor family. LAIR1 maps to a region of 19q13.4 labeled the leukocyte receptor cluster, which contains at least 29 genes encoding leukocyte-expressed receptors of the immunoglobulin superfamily.

GABARAP is a ligand-gated chloride channel that mediates inhibitory neurotransmission. GABARAP is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. GABARAP clusters neurotransmitter receptors by mediating interaction with the cytoskeleton.

The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.