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GNAQ, also known as Guanine nucleotide-binding protein belong to the G-alpha family. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in a variety of transmembrane signaling systems. GNAQ regulates B-cell selection and survival and is essential in order to prevent B-cell-dependent autoimmunity. GNAQ also regulates chemotaxis of BM-derived neutrophils and dendritic cells, in vitro. GNAQ is an alpha subunit in the Gq class, couples aseven-transmembrane domain receptor to activation of phospolipase C-beta. Mutations at this locus have beenconnected with problems in platelet activation and aggregation. A related pseudogene to GNAQ exists on chromosome 2.

Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-b1 is comprised of an Ig domain and an EGF-like domain which is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. Even though HRG1-b1 biological effects are still unclear, it has been discovered to advance motility and invasiveness of breast cancer cells which in addition might entail up-regulation of expression and function of the autocrine motility-promoting factor (AMF).

Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). There are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.

Agrin or AGRN is a large protein (proteoglycan) that has a crucial part in the development of neuromuscular junction amid embryogenesis. The protein has an involvement in the collection and aggregation of acetylcholine receptors through synaptogenesis. The agrin gene can be found and expressed in rat embryonic nervous system andmuscle tissue. This Agrin protein is aggregated in the synapses, there it can take part in regeneration & development. The protein binds to receptors on the surface of skeletal muscle.

Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

NANOG is a multidomain homeobox transcription factor which functions to maintain the undifferentiated state of pluripotent stem cells. NANOG expression counteracts the differentiation-promoting signals induced by the extrinsic factors LIF, Stat3 and BMP. Once NANOG expression is downregulated, cell differentiation can proceed. Proteins which regulate NANOG expression include transcription factors Oct4, SOX2, FoxD3, and Tcf3 and tumor suppressor p53.

Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.

Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.

ERGIC And Golgi 3, also known as ERGIC3 is a member of the ERGIC family and interacts with ERGIC1/ERGIC32. ERGIC3 takes part in the transport between endoplasmic reticulum and Golgi. One of the diseases which is associated with ERGIC3 is Breast Cancer.

RHOG belongs to the Rac subfamily of the Rho family of small G proteins. RHOG is a small monomeric GTP-binding protein (G protein), and is a key element of several intracellular signalling pathways. RHOG is needed for the formation of membrane ruffles during macropinocytosis. RHOG takes part in cell migration and is essential for the formation of cup-like structures during trans-endothelial migration of leukocytes. Similar to various small G proteins RHOG has a role in several cellular signalling mechanisms such as cell motility, gene transcription, endocytosis, neurite outgrowth, protection from anoikis and regulation of the neutrophil NADPH oxidase.

Nob1 takes part in pre-rRNA processing and cleaves in a late cytoplasmic processing step a 20S rRNA intermediate at cleavage site D to create the mature 18S rRNA. In yeast, more than 200 protein and RNA cofactors are essential for ribosome assembly, and these are mostly conserved in eukaryotes. These factors oversee alteration and cleavage of the initial 35S precursor rRNA transcript into the mature 18S, 5.8S, and 25S rRNAs, folding of the rRNA, and binding of ribosomal proteins and 5S RNA.

Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

Neuroglobin, 151 amino acid residue protein, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O (2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. Moreover, neuroglobin may be a novel oxidative stress-responsive sensor for signal transduction in the brain. Neuroglobin expression is increased by neuronal hypoxia in vitro and focal cerebral ischemia in vivo, and neuronal survival after hypoxia is reduced by inhibiting neuroglobin expression with an antisense oligodeoxynucleotide and enhanced by neuroglobin overexpression.

Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

NAGK is a member of the eukaryotic-type N-acetylglucosamine kinase family. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a key component of complex carbohydrates, from lysosomal degradation or alimentary sources into GlcNAc 6-phosphate. NAGK is a prominent salvage enzyme of amino sugar metabolism in mammals. NAGK cooperates with STK16 and LNX1 and has ManNAc kinase activity.

NDRG2 belongs to the N-myc downregulated gene family that is a part of the alpha/beta hydrolase superfamily. NDRG2 takes part in dendritic and neuronal cell differentiation and outgrowth and is found in large quantities in heart, dendritic cells, brain, salivary gland and skeletal muscle and in small quantities in kidney and liver. In Alzheimer Disease (AD)-affected patients NDRG2 is found in brain lesions and is believed to be related to the progression of AD.

N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.

Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.