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EED is a part of the Polycomb-group family whose members form multimeric protein complexe that are involved in preserving the transcriptional repressive state of genes over successive cell generations. EED mediates repression of gene activity through histone deacetylation, and acts as a specific regulator of integrin function. EED protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin ?7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins.

Family with Sequence Similarity 107, Member B (FAM107B) which is a part of the FAM107 family, is expressed in most tissues in the human body. FAM107B exists in all stages of human development.

DNA Cytosine-5--Methyltransferase 3-Like (DNMT3L) is a nuclear protein with similarity to DNA methyltransferases, but is not believed to act as a DNA methyltransferase since it doesn’t contain the amino acid residues needed for methyltransferase activity. Nevertheless, DNMT3L stimulates de novo methylation by DNA cytosine methyltransferase 3 alpha and is assumed to be required for the formation of maternal genomic imprints. DNMT3L also mediates transcriptional repression as a result of interaction with histone deacetylase 1. DNMT3L is a catalytically inactive regulatory factor of DNA methyltransferases, which is vital for the function of DNMT3A and DNMT3B. DNMT3L activates DNMT3A and DNMT3B by binding to their catalytic domain. Furthermore, DNMT3L accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases.

Serum-and glucocorticoid-regulated kinase (SGK1) is a serine/threonine protein kinase and a member of the “AGC” subfamily, which includes protein kinases A, G, and C. The SGK1 protein has an imperative role in activating specific potassium, sodium and chloride channels, suggesting a participation in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK1 is activated in vitro by PDK-1 (3-phosphoinositide-dependent protein kinase-1) and in vivo in reaction to signals which activate phosphatidylinositol (PI) 3-kinase.

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.

AN1-type zinc finger protein 1 isoform a (ZFAND1) is a member of the Zinc-finger proteins. Proteins from this family contain DNA-binding domains and have an extensive variety of functions, most of which encompass some form of transcriptional activation or repression. ZFAND1 is a 268 amino acid protein, which contains two AN1-type zinc fingers that are repeatedly found in proteins which contain an ubiquitin-like domain and for that reason have a role in the ubiquitination pathway ZFAND1 is comprised of 6 conserved cysteines and 2 histidines and have a dimetal (zinc)-bound alpha/beta fold. As a result of alternative splicing events two isoforms of ZFAND1 are produced.

YWHAZ accession number NP_ 663723 belongs to the 14-3-3 family of proteins which are in charge for checkpoint control, apoptotic & nutrient sensing pathways as well as signal transduction by binding to phosphoserine-containing proteins. The 14-3-3 protein family is found in both plants and mammals, and KCIP-1 protein is 99% identical to the mouse, rat and sheep orthologs. KCIP-1 interacts with IRS1 protein, signifying a role in regulating insulin. 14-3-3 proteins are highly conserved and ubiquitously expressed. YWHAZ function as an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAZ binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

RAB27B is a member of the RAB family and is an important regulator of vesicular transport. RAB27B is expressed in pituitary tissue, but is more extensively expressed in brain and spleen. RAB27B may be functionally redundant to Rab27a, as it can salvage Rab27a mutants.

Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

SIRT5 belongs to the Sirtuin family of proteins, homologs to the yeast Sir2 protein. Sirtuin family members hold a sirtuin core domain and grouped into four classes. The protein encoded by this gene is included in class III of the sirtuin family. Human sirtuins functions were not yet determined; still, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies propose that human sirtuin could operate as intracellular regulatory protein with mono-ADP-ribosyltransferase activity.

ARL4D is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). ARL4D takes part in membrane-associated intracellular trafficking. Mutations in this gene is linked to Bardet-Biedl syndrome (BBS).

Protein phosphatase 1 regulatory subunit 11 (PPP1R11) is located within the major histocompatibility complex class I region on chromosome 6 and is expressed in a variety of both adult and embryonic tissues. PPP1R11 acts as an inhibitor of PP1 (protein phosphatase 1), particularly showing a sensitivity toward the metal-independent and metal-dependent forms of PP1. Deletion of a portion of the q arm of chromosome 6 is related with early onset intestinal cancer, proposing the presence of a cancer vulnerability locus.

Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.

Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.

CUTA is the 179 amino acid mammalian homolog of the cutA E. coli protein and is ubiquitously expressed, particularly in brain tissue. CUTA participates in cellular tolerance to a broad range of divalent cations other than copper. The CUTA protein is a cytoplasmic protein, encoded by the single-gene operon and has been related to divalent cation tolerance.

CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.

CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.

Escherichia coli Hsp31 (HchA) is a homodimeric member of the ThiI/DJ-1/PfpI superfamily which combines molecular chaperone and aminopeptidase activities. HchA uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress.

DLX3 belongs to the Distal-less (Dlx) family of genes which includes at least 6 different members. DLX3 plays a regulatory role in the development of the ventral forebrain and also in craniofacial patterning and morphogenesis. Mutation in DLX3 is correlated with Trichodentoosseous syndrome which is an autosomal dominant condition. DLX3 is located in a tail-to-tail configuration with another member of the gene family on the long arm of chromosome 17.

HNRNPC is a member of the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs) which are related to pre mRNAs in the nucleus and effect pre mRNA processing and other aspects of mRNA metabolism and transport. Although all of the hnRNPs are present in the nucleus, several hnRNPs travel between the nucleus and the cytoplasm. The hnRNP proteins have specific nucleic acid binding properties.

RAP2A belongs to the RAS oncogene family and a Ras-like small G protein. The RAP2A protein shares 60% identity with Rap1A and exhibits a carboxy-terminal CAAX motif and 2 upstream cysteines similar to those of the H-Ras, K-Ras and N-Ras proteins. In contrast with Rap1A and Rap1B, overexpression of RAP2A doesn’t obstruct the Ras signaling pathway.

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.

UBL3 - a member of the ubiquitin-like family is found in the membrane. UBL3 holds two N-glycosylation sites, a C-terminal prenylation site and a protein kinase C phosphorylation site. Even though Ubiquitin-like proteins are not directly involved in protein degradation, it seems they have several mechanistic similarities to the ubiquitin pathway.