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SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.

PTPN7 performs specifically on tyrosine-phosphorylated MAPK1. PTPN7 takes part in the regulation of signal transduction and T and B-lymphocyte development.

GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

Interleukin-27 protein is related to IL-12A & is one of the subunits of a heterodimeric cytokine complex. IL-27 interacts with EBV induced gene 3 also called EBI3, and forms a complex that drives rapid expansion of CD4 (+) T cells.
IL-27 complex is synergizes with IL-12 in order to trigger the cytokine production of IFN-Gamma of CD4 (+) T cells. The biological effect of IL-27 is mediated by class-I cytokine receptor (WSX1/TCRR).
The pro-inflammatory activity of IL-27 is mediated through the growing expression of key molecules involved in the MHC class-I & MHC class-II pathways. Both MHC class-I and MHC-class-II expression are increased in endothelial cells after Interleukin-27 stimulation which suggests that it may play an important role in conferring the immune function on vascular endothelium IL-27p28 subunit can be induced by IFN-beta and during LPS-induced maturation of dendritic cells in type-I IFN-dependent manner through IFN regulatory factor-1 activation. Interleukin-27 regulates Interleukin-12 responsiveness of CD4+ T cells through Stat1-dependent and -independent mechanisms. IL-17 & IL-23 play an important IL-17 role in inflammation. Interleukin-27 possesses potent anti-angiogenic activity that plays an important role in its antitumor and antimetastatic activities.
EBV induced gene 3 plays a role, independently from IL-27, in regulating anti-viral or anti-tumoral immune responses. Interleukin-27 is a potent inhibitor of HIV-1 replication in macrophages, CD4+ T cells, peripheral blood mononuclear cells.
Interleukin-27 triggers STAT activation and gene transcription.

IL-29 is distantly related to type I interferons and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires Interferon-Lambda 2 receptor tyrosine residues.

IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.

IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM-CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.

IL-28B is a cytokine remotely related to type I IFNs and the IL-10 family. Interleukin-28B, interleukin 28A (IL28A), and interleukin 29 (IL29) are 3 closely related cytokine genes which form a cytokine gene cluster on a chromosomal region mapped to 19q13. Expression of the cytokines encoded by these 3 genes can be induced by viral infection. All 3 cytokines interact with a heterodimeric class II cytokine receptor which consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha (IL28RA).

Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.

HER-2/neu (erbB-2) encodes an 185-kDa orphan receptor tyrosine kinase that is constitutively active as a dimer and displays potent oncogenic activity when overexpressed. Herstatin, as the product of alternative HER-2 transcript, retains intron 8. The herstatin mRNA is expressed in normal human fetal kidney and liver, but is at reduced levels relative to p185HER-2 mRNA in carcinoma cells that contain an amplified HER-2 gene. Herstatin appears to be an inhibitor of p185HER-2, because it disrupts dimers, reduces tyrosine phosphorylation of p185, and inhibits the anchorage-independent growth of transformed cells that overexpress HER-2.

The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

ANKRD1 takes part in endothelial cell activation and performs as a nuclear transcription factor which negatively controls the expression of cardiac genes.

Synaptotagmin-1(SYT1) is a member of the synaptotagmin family, which contains two C2 domains. The synaptotagmins are integral membrane proteins of synaptic vesicles assumed to function as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SYT1 is the principal regulator responsible for allowing the human brain to release neurotransmitters. SYT1 may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. SYT1 binds acidic phospholipids with a specificity which entails the presence of both an acidic head group and a diacyl backbone. SYT1 can also bind to at least 3 additional proteins in a Ca2+-independent manner; these being neurexins, syntaxin and AP2.

ZW10 Interacting Kinetochore Protein (ZWINT) is involved in kinetochore function. ZWINT is part of the MIS12 complex, which is essential for kinetochore formation and spindle checkpoint activity. ZWINT is localized to the cytoplasm during interphase and to kinetochores from late prophase to anaphase. ZWINT interacts with ZW10 (Zeste White 10) and regulates the association between ZW10 and kinetochores. ZWINT gene defects are linked with the pathogenesis of Roberts’s syndrome, an autosomal recessive disorder characterized by growth retardation due to premature chromosome separation.

The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function. Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine,

Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.

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.

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).