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NUDT16 is nuclear nucleoside diphosphatase proteins restricted in foci in the nucleolus and nucleoplasm. NUDT16 is a RNA-decapping enzyme. It binds specifically to U8 snoRNA and can remove m7G and m227G caps from RNAs, rendering them substrates for 5’-3’ exonucleases for degradation in vivo.

Survivin is part of the of the inhibitor of apoptosis (IAP) family, which encodes negative regulatory proteins that prevent apoptotic cell death. Members of the IAP family include multiple baculovirus IAP repeat (BIR) domains, but Survivin has only a single BIR domain.
Survivin is an inhibitor of caspase activation therefore leading to negative regulation of apoptosis. BIRC5 is expressed in Merkel cell carcinoma.
BIRC5 polymorphism causes survivin expression, thus contributing to the genetic susceptibility to lung cancer. BIRC5 expression in large cell lung cancer is substantially higher than in normal tissue cells. Survivin mRNA is up-regulated in tumors. Apoptotic response of infected intestinal epithelial cells is suppressed by C. parvum via upregulation of BIRC5, favoring parasite infection. Up-regulation of of Survivin is associated with breast carcinomas.
BIRC5 increases the activity of an oncolytic adenovirus in the presence of low-dose radiotherapy. ER- breast cancer cells become dependent on Notch-survivin signaling for their maintenance, in vivo. Survivin mRNA positive cases are related with bladder tumour recurrence elevated expression of survivin might play an important role of development in nasal polyps.

Syntaxin 3 (STX3) is a member of the syntaxin family. The syntaxin family members are cellular receptors for transport vesicles which participate in exocytosis in neutrophils. STX3 has a significant role in the growth of neurites and functions as a direct target for omega-6 arachidonic acid. STX3 is steered to the apical membrane of epithelial cells where it forms clusters and is vital in establishing and maintaining polarity required for protein trafficking involving vesicle fusion and exocytosis.

Platelet-activating Factor Acetylhydrolase 1b Catalytic Subunit 3 (PAFAH1B3) is a member of the 'GDSL' lipolytic enzyme family. Acetylhydrolase catalyzes the elimination of an acetyl group from the glycerol backbone of platelet-activating factor. PAFAH1B3, which is a subunit of the platelet-activating factor cetylhydrolase isoform 1B complex, is comprised of the catalytic beta and gamma subunits and the regulatory alpha subunit. The PAFAH1B3 complex has an imperative role during the development of brain.

Bromodomain Containing 3 (BRD3) was classified based on its homology to the gene encoding the RING3 protein, which is a serine/threonine kinase. The BRD3 protein localizes to 9q34, a region which contains a number of major histocompatibility complex (MHC) genes. The function of the BRD3 protein is unknown.

Lymphokine-activated killer T-cell-originated protein kinase (PBK) is a serine/threonine kinase related to the dual specific mitogen-activated protein kinase (MAPKK) family. PBK is abundant in placenta (is also found in the testis’ outer cell layer of seminiferous tubules) and absent from adult brain tissue. PBK is involved in the activation of lymphoid cells and supports testicular functions, with a possible role in the process of spermatogenesis. Mitotic phosphorylation is required for PBK’s catalytic activity. Once phosphorylated,PBK forms a complex with TP53, leading to TP53 destabilization and weakening of G2/M checkpoint during some kind of DNA damage. PBK is active only during mitosis. In addition, a PDZ domain in the tumor suppressor protein Dlg can coordinate with the T/SXV motif of PBK. PBK also phosphorylates MAP kinase p38, and may have a role in the activation of lymphoid cells.

FARSB, also known as Phenylalanyl-TRNA Synthetase Beta is a member of the phenylalanyl-tRNA synthetase beta subunit family. FARSB is composed tetramer of two alpha and two beta subunits. In the presence of ATP, this tetramer is accountable for attaching L-phenylalanine to the terminal adenosine of the appropriate tRNA.

TRAF2 protein is related with transduce signals from members of the TNFR superfamily. TRAF2 is located in the cytoplasm binds to TRAF1, TRAF2, or TRAF3, thus inhibiting TRAF function by sequestering the TRAFs in a suppressed state in the cytoplasm. Overexpression of TANK inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and inhibits LMP1-mediated NF-kappa-B activation by blocking the association of TRAF2 with LMP1. TRAF2 is necessary for the cellular response to TNF-alpha by connecting upstream signalling molecules to the IKKs and p65.

Ferredoxin-1 is a small iron-sulfur protein who transfers electrons from NADPH through ferredoxin reductase to a terminal cytochrome P450. This specific oxidation/reduction system is located in steroidogenic tissues, and is involved with the synthesis of bile acid and vitamin D. FDX1 takes part in the synthesis of thyroid hormones and transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450. FDX1 supports reactions catalyzed by human microsomal P450s- full length CYP17, truncated CYP17, and truncated CYP21. In addition to the FDX1 at the 11q22chromosomal locus, there are pseudogenes located on chromosomes 20 and 21.

C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.

Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.

Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.

Inositol-tetrakisphosphate 1-kinase (ITPK1) is a 414 amino acid monomer which is a member of the ITPK1 family and exists as 2 alternatively spliced isoforms. ITPK1 highest levels are found in the brain, followed by the heart, skeletal muscle, kidney, pancreas, liver, placenta and lung. ITPK1 is comprised of one ATP-grasp domain and has been shown to phosphorylate various inositol polyphosphates and modify TNFa induced apoptosis.

IYD is an enzyme that catalyzes the oxidative NADPH-dependent deiodination of both mono- and diiodotyrosine although acts more efficiently on monoiodotyrosine. The N-terminus of Iodotyrosine Deiodinase , also known as IYD, plays a role as a membrane anchor. IYD acts during the hydrolysis of thyroglobulin to liberate iodide, which then reenter the hormone-producing pathways.

Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

Group IB secretory phospholipase A2 (sPLA2-IB) mediates cell proliferation, cell migration, hormone release and eicosanoid production via its receptor in peripheral tissues. In the CNS, high-affinity binding sites of sPLA2-IB have been documented. sPLA2-IB induced neuronal cell death in a concentrationdependent manner depending on PGD2 metabolites, especially Delta12-PGJ2 that might mediate sPLA2-IB-induced apoptosis. The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

Ferritin is a fairly large, iron-storage heteropolymeric protein composed of 2 subunit types, light Ferritin & heavy Ferritin polypeptides, which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin is composed of 24 self-assembled polypeptide subunits of the heavy and light ferritin chains and is characterized by the capacity to remove Fe (II) from solution in the presence of oxygen.
Ferritin light polypeptide protein is the main intracellular iron storage protein in prokaryotes and eukaryotes. Variation in ferritin subunit composition influence the rates of iron uptake and release in various tissues. A key function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyper ferrit anemia-cataract syndrome.
Ferritin stores iron in a soluble, nontoxic, readily accessible form. Ferritin is needed for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after it has been oxidized.

Phosphomevalonate kinase (PMVK) is a cytosolic enzyme. PMVK is expressed highly in the heart, liver, skeletal muscle, kidney and pancreas and slightly lower in the brain, placenta, and lung. PMVK catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway. Induced by sterol, PMVK participates in isopentenyl diphosphate biosynthesis via the mevalonate pathway.

KLRC3 belongs to the NKG2 group that can be found mostly in natural killer (NK) cells and encodes a family of transmembrane proteins known for their C-type lectin domain and their type II membrane orientation (extracellular C terminus). The NKG2 gene family is situated inside the NK complex, a region which has quite a few C-type lectin genes mostly expressed on NK cells.

Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

Tripartite Motif Containing 28 (TRIM28) which is a member of the tripartite motif family includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM28 mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. TRIM28 is restricted to the nucleus and connected with particular chromatin regions.

Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.