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Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

KRT20 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.

Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.

MICA (MHC class I chain-related gene A) is a transmembrane glycoprotein that functions as a ligand for human NKG2D. A closely related protein, MICB, shares 85% amino acid identity with MICA. These proteins are distantly related to the MHC class I proteins. They possess three extracellular Ig-like domains, but they have no capacity to bind peptide or interact with ?2-microglobulin. The genes encoding these proteins are found within the Major Histocompatibility Complex on human chromosome 6. The MICA locus is highly polymorphic with more than 50 recognized human alleles. MICA is absent from most cells but is frequently expressed in epithelial tumors and can be induced by bacterial and viral infections. MICA is a ligand for human NKG2D, an activating receptor expressed on NK cells, NKT cells,gammadelta T cells, and CD8+beta T cells. Recognition of MICA by NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. MICA recognition is involved in tumor surveillance, viral infections, and autoimmune diseases.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

Cystatin 5 (CST5) is a novel member of the cystatin superfamily, which encompasses proteins that contain multiple cystatin-like sequences. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions.

Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.

Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species.
A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.
Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin.
Alpha-1-microglobulin was first discovered in pathological human urine.
It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

Anthrax toxin receptor 2, also known as ANTXR2, takes part in the configuration of little blood vessels (capillaries). ANTXR2 helps the toxin that leads to anthrax to attach to cells and trigger illness. ANTXR2 is necessary for cellular interactions with laminin and the extracellular matrix.

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.

Amine Oxidase Copper Containing 1 or AOC1 is n enzyme, part of the copper-containing amine oxidase group of proteins. AOC1 is responsible for oxidation of many different biogenic amines, such as neurotransmitters, xenobiotic amines & histamine. Dietary histamine intolerance and histaminosis can be caused from AOC1 deficiencies. This enzyme can also cause Tumor Progression by AKT & EMT transduction promotion in stomach cancer.

DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.

Developmentally-regulated GTP-binding protein 1 (DRG1) is a member of the GTP1/OBG family. DRG1 has a role in cell proliferation and differentiation, as well as in apoptosis, proposing a role in tumor formation and metastasis. Expression of the DRG1 was considerably reduced in breast tumor cells, particularly in patients with lymph node or bone metastasis as compared to those with localized breast cancer. The DRG1 protein is expressed at high levels in the heart, kidney and skeletal muscle and at lower levels in the brain, liver, placenta, lung, colon and spleen.

ARL5A is a member of the ARF family of GTP-binding proteins. ARFs are vital in eukaryotic vesicular trafficking pathways and have a crucial part in the activation of phospholipase D. Different from ARF family members, ARL5 is believed to lack ADP-ribosylation enhancing activity. ARL5A is developmentally regulated and has a role in nuclear dynamics and signaling cascades during embryonic development.

ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

SMNDC1 is a vital splicing factor obligatory for spliceosome assembly which is a part of the SMN family. SMNDC1 has one Tudor domain with significant similarity to Survival Motor Neuron (SMN) and is expressed in heart, pancreas and skeletal muscle, localizing to Cajal bodies and nuclear speckles. Mutations in SMNDC1 are cause of autosomal recessive proximal spinal muscular atrophy.

ELL Associated Factor 1 (EAF1) is a part of the EAF family and is expressed mainly in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, prostate, testis, small intestine and colon. EAF1 plays a role as a transcriptional transactivator of ELL and ELL2 elongation activities.

EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.

EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

SOX2 is a transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. SOX4 is important for early embryogenesis and for embryonic stem cell pluripotency.

Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.