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IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.

FXYD domain-containing ion transport regulator 5 (FXYD5) is a cancer-associated cell membrane glycoprotein which is a part of the FXYD family. FXYD5 is engaged in down-regulation of E-cadherin, which takes part in tumor development and metastasis and results in reduced cell adhesion.FXYD is found in spleen, lung, skeletal muscle, and testis tissue, and maps to human chromosome 19q13.2.

BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.

TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is situated on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in TNNT2 gene are related with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy. TNNT2 mutation takes part in hypertrophic cardiomyopathy.

GPN-loop GTPase 1 (GPN1) is a member of the GPN-loop GTPase family. GPN1 is a guanosine triphosphatase enzyme which has a role in DNA repair and may function in activation of transcription. Small GTPases, which share a biochemical mechanism, act as binary molecular switches and function in the cell is nucleocytoplasmic transport of both proteins and RNA. In addition, GPN1 establishs an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, proposing that it is essential to connect RNA polymerase II to regulators of protein complex formation. GPN1 may also be involved in nuclear localization of XPA.

BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

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.

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.

HMGB2 belongs to the non-histone chromosomal high-mobility group protein family which are chromatin-associated and highly spread in the nucleus of higher eukaryotic cells. HMGB2 can successfully bend DNA and form DNA circles which indicates that HMGB2 facilitates cooperative interactions between cis-acting proteins by promoting DNA flexibility. Additionally, HMGB2 takes part in the final ligation step in DNA end-joining processes of DNA double-strand breaks repair and V(D)J recombination.

Sjogren syndrome/scleroderma autoantigen 1, SSSCA1 is involved in mitosis. SSSCA1 is a centromere-associated protein which can induce anti-centromere antibodies. In addition SSSCA1 is recognized by a subset of anti-centromere antibodies from patients with sclerodermaand Sjogren's syndrome.

High mobility group protein HMG-I/HMG-Y (HMGA1) belongs to the non-histone chromosomal high mobility group protein (HMG) family. HMGA1 is composed of a highly conserved AT-hook DNA-binding domain which mediates binding to AT-rich sequences in the minor groove of chromosomal DNA. HMGA1 functions as an architectural chromatin-binding transcription factor modifying the conformation of DNA by modulating nuclear protein-DNA complexes. Furthermore, HMGA1 is involved in numerous cellular processes including growth regulation, viral induction of beta-IFN gene and regulation of inducible gene transcription.

RGS2 belongs to the RGS family which are regulatory molecules that act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. RGS2 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits and as a result driving them into their inactive GDP-bound form.

RDBP is a putative RNA binding protein. RDBP protein is one of the five components of the multisubunit NELF complex which collaborates with DSIF to repress RNA polymerase II elongation. Control of transcription elongation needs a complex interaction between positive transcription elongation factor b and negative transcription elongation factors, DSIF and NELF. DSIF and NELF, act as negative transcription elongation factors by increasing the time the polymerase spends at pause sites. RDBP has a functional RNA-binding domain, whose mutations impair transcription repression without affecting known protein-protein interactions.

Purkinje cell protein 4-like protein 1 (PCP4L1) is a member of the PCP4 family and contains 1 IQ domain. PCP4L1 is a protein-coding gene.

TAR DNA Binding Protein (TARDBP) was initially recognized as a transcriptional repressor which binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, TARDBP has been detected in individuals diagnosed with chronic traumatic encephalopathy as well, which is a condition that often imitates ALS andhas been related with athletes who have experienced multiple concussions and other types of head injury.TARDBP has been shown to bind both DNA and RNA, it has multiple functions in transcriptional repression, pre-mRNAsplicing and translational regulation.

PAK4 is part of the group B family of p21-activated kinases (PAK). It's known as an effector protein for cell division cycle 42(Cdc42) and protein that plays an important role in regulating cytoskeletal organization and cell morphology. PAK4 expression is eminent in many cancer cell lines, and is involved in tumorigenesis. PAK proteins are significant effectors that associate Rho GTPases to cytoskeleton reorganization and nuclear signaling. PAK proteins are targets for the small GTP binding proteins Cdc42 and Rac and have been implicated in a wide range of biological activities. PAK4 cooperates specifically with the GTP-bound form of Cdc42Hs and weakly activates the JNK family of MAP kinases. PAK4 is a mediator of filopodia formation and is involved in the reorganization of the actin cytoskeleton. PAK4 activates the JNK pathway. PAK4 phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments.

Tyrosine-protein kinase Lyn (LYN) belongs to the src family of non-receptor protein tyrosine kinases, which is primarily expressed in haematopoietic tissues. LYN protein is involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. LYN protein stimulates SAPK by a MKK7- and MEKK1-dependent mechanism. The LYN - MEKK1 - MKK7 - SAPK pathway is efficient in the induction of apoptosis by genotoxic agents.

S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.

GTF2B is one of the ubiquitous factors needed for transcription initiation by RNA polymerase II preinitiation factor. GTF2B localizes to the nucleus where it forms a complex (the DAB complex) with transcription factors IID and IIA. GTF2 plays a role as a bridge between IID, which initially recognizes the promoter sequence, and RNA polymerase II. GTF2B is involved in the selection of the transcription start site.

TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

SMAD2 is part of the SMAD family of proteins that mediate signal transduction by the TGF-beta/BMP-2/4 cytokine superfamily from receptor Ser/Thr protein kinases at the cell surface to the nucleus. Phosphorylated SMAD2 is then able to form a complex with SMAD4 or SARA. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression. SMAD2 mediates the signal of the TGF-beta, and therefore regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. SMAD2 is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein.
TGF-beta 1 acts on adjacent stromal cells to turn on SMAD2 signalling that could lead to stromal decidualization. SMAD2 is the downstream signal transducers of TGF-beta-1 in human dental pulp cells.

RANGRF is a protein which acts as a guanine nucleotide release factor in mouse and regulates the expression and function of the Nav1.5 cardiac sodium channel in human. RANGRF also controls the intracellular trafficking of RAN. In cardiac cells, the RANGRF appears to regulate the cell surface localization of SCN5A.

LIN7B (VELI2), is a member of the Velis family. Velis family contains minor synaptic proteins which interact with other proteins at the post-synaptic density (PSD) of neuronal synapses. Velis which contain the PDZ motif, participate in recruiting cell adhesion molecules, receptors, and channels. Lin7B protein is ubiquitously expressed with a high expression in the brain, liver, and testis. Lin7B localizes at the synaptic junctions in neurons, bind to CASK, which is a neurexin-binding protein highly concentrated in synapses, and Mint1, a binding partner with a vesicle trafficking protein.