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Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.

Synaptotagmin V, (SYT5) is a member of synaptotagmin family, which is a family of type III membrane proteins characterized by cytoplasmic repeats related to protein kinase C regulatory (C2) domains that are considered to bind calcium. Synaptotagmins function as negative regulators of vesicle fusion, allowing fusion in the attendance of calcium, and as calcium receptors or sensor molecules. Among the diseases associated with SYT5 are labyrinthitis, and thyroiditis.

TGFBR1 is a single-pass type 1 membrane protein which is a part of the TGFB receptor subfamily and the protein kinase superfamily. TGFBR1 is a secreted protein that performs many cellular functions such as the control of cell growth, cell differentiation, cell proliferation and apoptosis. TGFBR1 also controls the immune system and shows different activities on various types of cell, or cells at different developmental stages.

L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

Glycophorin C, also known as GYPC, is an integral membrane glycoprotein. GYPC is a minor species which is carried by human erythrocytes, however plays an important role in regulating the mechanical stability of red cells. Numeral glycophorin C mutations have been described. The Gerbich and Yus phenotypes are due to deletion of exon 3 & 2, respectively. The Webb & Duch antigens, also identified as glycophorin D, result from single point mutations of the glycophorin C gene. The glycophorin C protein has very slight homology with glycophorins A & B.

Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.

The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

SLAM family member 6 (SLAMF6) is a member of the SLAM family of immune cell receptors. SLAMF6 is a unique receptor on T cells which, when triggered potentiates T cell expansion in a CD28-independent manner. SLAMF6 has a high expression on NK-, T-, and B cells. SLAMF6 exhibits homotypic interactions and can connect with adaptor molecules such as SAP to alter immune cell function.

Nuclear transport factor 2-like export factor 2 (NXT2) belongs to the NXT family proteins which are commonly involved in exporting nuclear RNA in eukaryotic cells. The NXT2 protein is a regulator of protein export for NES-containing proteins. In addition, NXT2 associates with NXF1, NXF2, NXF3 and NXF5 and has a role in mRNA nuclear export. NXT2 has a critical role in upholding morphogenetic integrity of embryonic heart in vertebrate species. The NXT2 protein contains a nuclear transport factor 2 (NTF2) domain, which has a vital role in the trafficking of macromolecules, ions, and small molecules between the cytoplasm and nucleus, it may also have a role in mRNA nuclear export.

BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.

Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.

Sulfotransferase 1A2 (SULT1A2) belongs to the sulfotransferase family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.

PDCD1 is a cell surface membrane protein of the immunoglobulin superfamily. PDCD1 is expressed in pro-B-cells and is thought to have a role in their differentiation. In mice, expression of PDCD1 gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for the PDCD1 gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that the PDCD1 gene product may also be important in T cell function and contribute to the prevention of autoimmune diseases.

TAF9 is a universal transcription factor which enables the preinitiation complex assembly by direct interactions with the TATA promoter element. TAF9 is a multisubunit complex consisting of a small TATA-binding polypeptide and other TBP-associated factors (TAFs) and performs as a channel for regulatory signals.

Ketosamine-3-kinase (FN3KRP) catalyzes the phosphorylation of psicosamines and ribulosamines compared to the adjacent gene which encodes a highly analogous enzyme, fructosamine-3-kinase that has different substrate specificity. The activity of both enzymes may cause deglycation of proteins to reinstate their function. A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). The proteins altered in this way, are less active or functional.

Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma.

Cofilin is a family of actin-binding proteins which disassembles actin filaments. It is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.

Glycoprotein-9 (GP9) is a small membrane glycoprotein found on the surface of human platelets. GP9 forms a one to one noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex which functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein and platelet glycoprotein V. GP9 gene defects cause the Bernard-Soulier syndrome, aka giant platelet disease whose patients have unusually large platelets and have a clinical bleeding tendency.

PSG5 belongs to the PSG family, which are a highly connected group of secreted glycoproteins, vastly expressed in fetal placental syncytiotrophoblast cells. PSGs are can be found in serum from the first 2-3 weeks of pregnancy and at higher levels as the pregnancy progresses, up to e point where they are the highest fetal protein found in maternal blood at term. PSG5’s role is inducing secretion of TH2-type cytokines from monocytes and modulating the maternal immune system throughout the pregnancy, thus defending the semi-allotypic fetus from rejection.

CIAO1 is a vital component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. CIAO1 protein is required for the maturation of extra mitochondrial Fe/S proteins and seems to specifically modulate the trans-activation activity of WT1. CIAO1 participates in chromosome segregation as a part of the mitotic spindle-associated MMXD complex.

HAND1 is a member of the basic helix-loop-helix family of transcription factors. HAND1 is one of two HAND proteins, two closely related family members that are irregularly expressed in the emerging ventricular chambers and have a key part in cardiac morphogenesis. Operating in a complementary manner, they work in the development of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. Furthermore, HAND1 is obligatory for early trophoblast differentiation.

Zinc Finger HIT-Type Containing 1 (ZNHIT1) is a member of the ZNHIT1 family and contains 1 HIT-type zinc finger. The ZNHIT1 protein is induced by DNA damage and appears to have a role in p53-mediated apoptosis induction. ZNHIT1 interacts with MAPK11 and MAPK14 and is a component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1. ZNHIT1 binds to NR1D2 and discharges it of its inhibitory effect on the transcription of APOC3 without affecting its DNA-binding activity.