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Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

UBL5 is believed to be a reversible modulator of protein function unlike ubiquitin which is a protein degrader. UBL5 influences a nuclear phase obligatory for increasing a reaction against the risk of mitochondrial protein misfolding.

TPM4 is a member of the tropomyosin family. Tropomyosins exist in practically all eukaryotic cells (both muscle and nonmuscle), where they bind actin filaments and function to modulate actin-myosin interaction and stabilize actin filament structure. TPM4 binds to actin filaments in muscle and nonmuscle cells and plays a central role, in connection with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction.

TSR2 is part of the TSR2 family. TSR2 is involved in 20S pre-rRNA processing. Among the diseases which are associated with TSR2 are blepharospasm and diamond-blackfan anemia.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

CAB39 protein and STE20-related adaptor-alpha pseudo kinase, form a regulatory complex that is able of stimulating the activity of the LKB1 tumor suppressor protein kinase. CAB39 takes part as a scaffolding component of the STK11/STRAD complex and regulates STK11 activity and cellular localization.

TatD DNase Domain Containing 1, also known as TATDN1, is a protein coding gene which is a part of the TatD DNase family. TATDN1 which is a deoxyribonuclease binds two divalent metal cations per subunit.

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.

CRABP1 is a member of special carrier proteins for members of the vitamin A family. It is believed that CRABP1 has an essential role in retinoic acid-mediated differentiation and proliferation processes. Though, CRABP1 is structurally similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. CRABP1 is constitutively expressed and is thought to have different functions in the cell than the related CRABP2. CRABP1 forms a beta-barrel structure which accommodates hydrophobic ligands in its interior.
Loss of CRABP1 function as a result of hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma. Furthermore, frequent methylation-associated silencing of CRABP1 is linked to esophageal squamous-cell carcinoma.

sRAGE is a member of the immunoglobulin superfamily of cell surface molecules. sRAGE is a receptor for various molecules, including the amyloidogenic form of serum amyloid A, amyloid-beta protein, members of the S100/calgranulin superfamily and advanced glycation end products. sRAGE lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Alternative splicing results in two transcript variants encoding different isoforms. sRAGE mediates interactions of nonenzymatic glycosylated proteins which accumulate in vascular tissue during aging & at an increasing rate in diabetes. sRAGE is a receptor for amyloid beta peptide.

The MutS DNA Mismatch Protein Identifies heteroduplex DNAs comprising mis-paired or unpaired bases. The MutS DNA Mismatch Protein binds in vitro to heteroduplex DNAs comprising mis-paired or unpaired bases over a varied temperature range from 4-70 °C and obtains a thermostable ATPase activity. The MutS DNA Mismatch Protein is active at temperature between 0 to 75°C. Since The MutS DNA Mismatch Protein competently binds to 1-4 bases deletion (or insertion) and mismatch base pairs of GT, CT and AG, it is suitable for sensing these mutations. Mutations can be distinguished in polyacrylamide gels or on a solid phase such as Ni agarose or beads or magnetic Ni-NTA particles.

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.

Cytochrome c oxidase assembly factor 4 (COA4) is the last enzyme of the mitochondrial respiratory chain which needs a great number of accessory factors. COA4 is vital for oxidative phosphorylation and comprises multiple complexes including cytochrome c oxidase, assembled in macromolecular supercomplexes. COX4 is a protein-coding gene which defect in it causes an acute human encephalomyopathies.

Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

V-Ets Avian Erythroblastosis Virus E26 Oncogene 2 (ETS2) is a transcription factor that regulates genes involved in development and apoptosis. ETS2 is also a protooncogene which takes part in regulation of telomerase. ETS2 protein’s pseudogene is located on the X chromosome.

Ganglioside GM2 activator (GM2A) is a small glycolipid transport protein which functions as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. GM2A participates in lipid metabolism. GM2A protein is localized in lysosomes. The GM2A protein forms a large binding pocket for a number of single chain phospholipids and fatty acids. GM2A demonstrates calcium-independent phospholipase activity. GM2A stimulates ganglioside GM2 degradation by presenting GM2 to beta-hexosaminidase A. The Beta-hexosaminidase A, along with GM2A, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. GM2A gene mutations result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease.

Myeloid differentiation primary response gene 88 (MYD88) is a cytosolic adapter protein, which has a central role in the innate and adaptive immune response. MYD88 functions as a vital signal transducer in the interleukin-1 and Toll-like receptor signaling pathways. MYD88 acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. The MYD88 protein increases IL-8 transcription. MYD88 is involved in IL-18-mediated signaling pathway. MYD88 activates IRF1, resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MYD88 is comprised of an N-terminal death domain and a C-terminal Toll-interleukin1 receptor domain. Patients with defects in the MYD88 gene have an increased susceptibility to pyogenic bacterial infections.

KPNA2 belongs to the karyopherin alpha family. KPNA2 has a vital part in the nuclear import of proteins with a conventional nuclear localization signal (NLS).
In vitro, KPNA2 bound specifically and directly to substrates having a simple or bipartite NLS motif. KPNA2 stimulated docking of import substrates to the nuclear envelope and together with Ran reconstituted complete nuclear protein import.

The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.

Neural Cell Adhesion Molecule 1 (NCAM1) is apart of the immunoglobulin superfamily. NCAM1 bindsspecifically to neurite fasciculation, neuronneuron adhesion, outgrowth of neurites, and more. The polysialyation of NCAM1 reduces its adhesive property and increases its neurite outgrowth promoting features.NCAM1is mainly expressed in NK cells and a subset of T lymphocytes that mediate MHC-unrestricted cellmediated cytotoxicity. High expression of NCAM-1 differentiates NK cells as having an activated phenotype. During hematopoiesis, NCAM1plays a role as the prototypic marker of NK cells and also present on subset of CD4+, CD8+ and T cells. In cell adhesion, NCAM1 contributes to cell-cell adhesion during embryonic development.

b-synuclein (amino acids 1-134), an acidic neuronal protein of 134 amino acids, is extremely heat-resistant. b-synucelin also has a chaperone-like activity. Recently, b-synuclein has been suggested to inhibit a-synuclein aggregation. b and a-synuclein are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer disease.

TBC1D1 belongs to a family of proteins sharing a 180-200 a.a TBC domain having a role in regulating cell growth and differentiation of various tissues. These proteins share significant homology with TRE2, yeast Bub2, and CDC16. TBC1D1 function as a GTPase-activating protein for Rab family proteins. TBC1D1 is involved in the trafficking and translocation of GLUT4-containing vesicles. Among the diseases associated with TBC1D1 are tuberculous meningitis, and meningitis.