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Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

DNAJB11 is a member of the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJB11 serves as a co-chaperone for HSPA5 and binds directly to both unfolded proteins which are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed.

VSNL1 is a member of the visinin/recoverin subfamily of neuronal calcium sensor proteins. VILIP1 is strongly expressed in granule cells of the cerebellum where it associates with membranes in a calcium-dependent manner and modulates intracellular signaling pathways of the central nervous system by directly or indirectly regulating the activity of adenylyl cyclase. Changes in cellular expression of VSNL1 were found in hipppocampi of schizophrenics, since more interneurons showed immunoreactivity.
VILIP1 is expressed in pancreatic beta-cells. VILIP1 elevation enhances insulin secretion in cAMP-associated manner. Down-regulation of VILIP-1 decreased cAMP accumulation but increased insulin gene transcription. VILIP-1 interacts with cell membrane and actin-based cytoskeleton. VSNL1 modulates cAMP-accumulation in C6 glioma cells. HLP3 modulates cGMP-accumulation in transfected neural cells and cerebellar granule neurons.

Nephroblastoma Overexpressed (NOV) is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein is comprised of 4 structural domains, which present distinct, and sometimes opposing, biological activities. An elevated expression of NOV is linked with certain tumors, including Wilm’s tumor and most nephroblastomas. On the other hand, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is associated with decreased NOV expression.

The homeobox protein family of transcription factors has many members that take part in developmental processes such as HHEX. HHEX is known to interact with Promyelocytic leukemia protein and expression in specific hematopoietic lines indicates that this protein is involved in hematopoietic differentiation.

NANOGP8 belongs to the homeobox family of DNA binding transcription factors which is known to conserve pluripotency of embryonic stem cells. One change only separate NANOGP8 from NANOG – instead of 'Gln-253' in the inferred amino acid sequence in NANOG there is a ‘His-253’ in NANOGP8.

RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

RNA Guanylyltransferase And 5'-Phosphatase also known as RNGTT is a bifunctional mRNA-capping enzyme which exhibits RNA 5'-triphosphatase activity in the N-terminal section and mRNA guanylyltransferase activity in the C-terminal section. In addition, RNGTT catalyzes the first two steps of cap formation, through removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and also by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.

Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.

Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

HMGB3 is a member of the high mobility group (HMG) protein superfamily. HMGB3 holds DNA-binding HMG box domains, as do HMG1 and HMG2, and like the rest of the HMG protein superfamily members has a vital part in DNA replication, transcription and nucleosome assembly.

CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

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.

TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.

Vanin 1 (VNN1) belongs to the vanin family of proteins, which share extensive sequence similarity with each other, and also with biotinidase. This family includes secreted and membrane-associated proteins, a few of which have been described to participate in hematopoietic cell trafficking. No biotinidase activity has been established for any of the vanin proteins; nevertheless, they possess pantetheinase activity, which may have a role in oxidative-stress response. VNN1 protein, like its mouse homolog, is probably a GPI-anchored cell surface molecule. The mouse VNN1 protein is expressed by the perivascular thymic stromal cells and regulates migration of T-cell progenitors to the thymus. VNN1 is an amidohydrolase which hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5).

Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.

NMRAL1 is a redox sensor protein which goes through reformation and subcellular rearrangement in reaction to alterations in intracellular NADPH/NADP+ levels. When the NADPH concentration is low the protein is found mostly as a monomer, and binds argininosuccinate synthase (ASS1), which takes part in nitric oxide synthesis. Association with ASS1 defects NMRAL1 activity and diminishes the production of nitric oxide, which then inhibits apoptosis. When the NADPH concentration is normal , the protein is found as a dimer and hides the binding site for ASS1.

Translin is a DNA and RNA binding protein that identifies specifically preserved target sequences at the breakpoint junction of chromosomal translocations. TSN forms a ring-shaped configuration, that is in charge of DNA binding, and in addition has a leucine zipper motif, which is believed to assist TSN to form dimers. TSN exports specific mRNAs out of the nucleus, reinforced by its localization in both the nuclei and cytoplasm of neurons, and regulates their translation.

Guanine Nucleotide Binding Protein Gamma 11 (GNG11) which belongs to the guanine nucleotide-binding protein (G protein) gamma family encodes a lipid-anchored, cell membrane protein. G proteins act as a modulator or transducer in various transmembrane signaling systems. GNG11 is also subject to carboxyl-terminal processing.

GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.

Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.