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NDRG1 is a cytoplasmic protein that is involved in stress responses, hormone responses, cell growth, and differentiation. NDRG1 is one of 4 members of the NDRG ?/?-hydrolase family. NDRG1 is classified in databases as a tumor suppressor and heavy metal-response protein. NDRG1’s functions include cell-cycle regulation, cellular differentiation, apoptosis, hypoxia response and metal-ion sensing. NDRG1 is also essential for p53-mediated caspase activation and apoptosis. The NDRG1 is a Rab4a effector that is involved in vesicular recycling of E-cadherin. NDRG1 is ubiquitous; it is expressed most notably in placental membranes and prostate, kidney, small intestine, and ovary tissues. NDRG1 has reduced expression in adenocarcinomas compared to normal tissues.
NDRG1 gene mutations are reported to be the cause for hereditary motor and sensory neuropathy-Lom (HMSNL), which is a severe autosomal recessive form of Charcot- Marie-Tooth (CMT) disease. In addition, decreased NDRG1 expression in glioma is linked to tumor progression. On the other hand, overexpression of NDRG1 is connected to malignant status of esophageal cancer. NDRG1 may also have a role in portal vein invasion and intrahepatic metastasis in human hepatocellular carcinoma.

Ferritin is a fairly large, iron-storage heteropolymeric protein composed of 2 subunit types, light Ferritin & heavy Ferritin polypeptides, which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin is composed of 24 self-assembled polypeptide subunits of the heavy and light ferritin chains and is characterized by the capacity to remove Fe from solution in the presence of oxygen.
Ferritin light polypeptide protein is the main intracellular iron storage protein in prokaryotes and eukaryotes. Variation in ferritin subunit composition influence the rates of iron uptake and release in various tissues. A key function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyper ferrit anemia-cataract syndrome.
Ferritin stores iron in a soluble, nontoxic, readily accessible form. Ferritin is needed for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after it has been oxidized.

Thyroid Hormone Receptor Interactor 10 (TRIP10) is a part of the F-BAR family of proteins which is expressed in a variety of tissues, including kidney, brain, liver, lung, heart and pancreas. The F-BAR family of proteins contains an N-terminal, alpha-helical, region which is hydrophobic and related to the Bin Amphiphysin Rvs (BAR) protein family. TRIP10 is vital for the coordination of membrane tubulation with Actin cytoskeletal reorganization during endocytosis.

Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

SNRPD3 is a small nuclear ribonucleoprotein (snRNPs) that contains the spliceosome in eukaryotes. SNRPD3 is essential for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis. Alternative splicing happens in this locus and two transcript variants encoding the same protein were branded.

Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.

Homeodomain-only protein (HOPX) functions via its interaction with SRF, thus modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. HOPX inhibits SRF-dependent transcription either by hindering SRF binding to DNA or by engaging histone deacetylase (HDAC) proteins which prevent transcription by SRF. HOPX is a homeodomain protein which lacks certain conserved residues required for DNA binding. HOPX overexpression causes cardiac hypertrophy.

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).

SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

MAGEA6 belongs to the MAGEA family, which directs the expression of tumor antigens which are seen on a human melanoma by autologous cytolytic T lymphocytes (CTL). Members of the MAGEA family encode proteins with 50 to 80% sequence identity to each other. The MAGE genes, which are clustered at chromosomal location Xq28, were originally isolated from separate kinds of tumors, and based on their practically exclusive tumor-specific expression in adult tissues; they are objects for cancer immunotherapy. MAGEA genes’ promoters and first exons exhibit substantial variability, implying that the existence of the MAGEA gene family enables the same function to be expressed under different transcriptional controls. MAGEA genes are implicated in several hereditary disorders, such as dyskeratosis congenita.

MAGE belongs to the MAGE gene family, that comprises 12 known genes, of which 6 are expressed in tumors. The Melanoma-associated antigen 3 genes were originally isolated from different kinds of tumors, and based on their virtually limited tumor-specific expression in adult tissues, they were used as targets for cancer immunotherapy. MAGEA3 is a tumor-specific antigen extensively expressed in solid and hematologic malignancies, but not in normal tissues, with the exclusion of testis and placenta. Consequently, MAGEA3 is an outstanding candidate tumor antigen.

Cytokeratin 5 (KRT5) belongs to the keratin gene family. The type II cytokeratins are comprised of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed throughout differentiation of simple and stratified epithelial tissues. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. The KRT5 type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes are linked with a complex of diseases termed epidermolysis bullosa simplex.

ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.

RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein.

Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.

Hematological and neurological expressed 1 protein (HN1) is a small protein which is extremely preserved among species. HN1 expression is upregulated in regenerating neural tissues, including the axotomized adult rodent facial motor nerve and dedifferentiating retinal pigment epithelial cells of the Japanese newt. HN1 is also expressed in several tissues during embryonic development as well as in regions of the adult brain which display high plasticity.

GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.

Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity, but not heparin.

Keratin 8 and 18 (K8/18) are the major components of intermediate filament (IF) proteins of simple or single-layered epithelia.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.