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HSPB8 is part of the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. HSPB8 is induced by estrogen in estrogen receptor-positive breast cancer cells. HSPB8 protein functions as a chaperone in association with BAG3, a stimulator of macroautophagy. HSPB8 participates in the regulation of cell proliferation, apoptosis, and carcinogenesis. Mutations in HSPB8 gene have been related with different neuromuscular diseases, including Charcot-Marie-Tooth disease.

GF-like family receptor 1 (IGFLR1) is encoded by a gene mapping to human chromosome 19. IGFLR1 which is cell membrane receptor for the IGF-like family proteins binds IGFL1 and IGFL3 with a higher affinity and may as well bind IGFL2.

TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

Fibroblast Growth Factor-19 (FGF-19) is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.

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.

Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.

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.

TUBG1 belongs to the tubulin superfamily. TUBG1 localizes to the centrosome and binds to microtubules to create the gamma-tubulin ring complex. TUBG1 facilitates the microtubule nucleation and is essential for microtubule formation and progression of the cell cycle.

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. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. 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. This could be especially useful in

Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.

Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.

HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

60S ribosomal protein L8 (RPL8) is a member of the ribosomal protein L2P family. Ribosomes consist of a small 40S subunit and a large 60S subunit. RPL8 is found in the cytoplasm and exists as a component of the 60S subunit where it is assumed to have role in aminoacyl-tRNA binding, specifically at the ribosomal subunit interface. In rats, the RPL8 protein connects with the 5.8S rRNA, and possibly participates in the binding of aminoacyl-tRNA, and is a component of the elongation factor 2-binding site at the ribosomal subunit interface.

SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.

African swine fever virus (ASFV) causes African swine fever (ASF), a disease of swine characterized by high morbidity and mortality. ASFV is a large DNA virus which belongs to Asfarviridae family. ASFV’s multilayered virion consists from up to 54 polypeptides while p72 is the major capsid component. Middle part of p72 protein contains most epitopes tested by monoclonal antibodies, while C-terminal peptide of P72 isused for the genotyping of ASFV isolates.

RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

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.

E1 and E2 glycoproteins form a heterodimer which is involved in virus attachment to the host cell, virion internalization via clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, however this binding insufficient for infection, some additional liver specific cofactors may be required. The fusion function may perhaps be conducted by E1. E2 hinders human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively located on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses. These interactions allow seizure of circulating HCV particles by these cells and subsequent diffusion to permissive cells.

S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.

Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.

Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.

Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and assist in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit (MRPL13 is a 39S subunit protein) and have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. An additional difference between mammalian mitoribosomes and prokaryotic ribosomes is that the second contain a 5S rRNA. Among various species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology.

Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and aid in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) comprised of a small 28S subunit and a large 39S subunit. Among different species, the proteins comprising the mitoribosome vary greatly in sequence, and sometimes in biochemical properties, thus preventing simple recognition by sequence homology. Mitochondrial Ribosomal Protein L2 (MRPL2) is a 39S subunit protein which is a member of the EcoL2 ribosomal protein family.

E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.