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rRNA-processing protein UTP23 homolog (UTP23) is a small subunit (SSU) processome component. The SSU processome is a complex involved in ribosome biogenesis and essential for pre-18S rRNA maturation. UTP23 is vital for the first 3 cleavage steps in 18S rRNA maturation. Furthermore, single-point mutations in the conserved putative active site of Utp24 but not Utp23 annul its function in ribosome biogenesis.

YY1 Transcription Factor, also known as YY1, is a part of the GLI-Kruppel class of zinc finger proteins. YY1 has a positive and negative effect on a various cellular and viral genes by binding to sites overlapping the transcription start site. YY1 leads histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter.

STAM Binding Protein (STAMBP) is a zinc metalloprotease which specifically cleaves Lys-63-linked polyubiquitin chains, however it doesn’t cleave Lys-48-linked polyubiquitin chains. STAMBP has a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. In addition, STAMBP potentiates BMP signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. STAMBP also has a major role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is essential for efficient EGFR degradation but not for its internalization. STAMBP is also involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.

Plasminogen Activator Inhibitor-2 (Serpine2) which inhibits thrombin, plasmin and plasminogen activators is a part of the Serpin superfamily of the serine protease inhibitors. Serpine2 is able to transform human embryonic kidney cells into neuron-like cells. Furthermore, Serpine2's over expression in mice leads to progressive neuronal and motor dysfunction.

Killer cell immunoglobulin-like receptor 2DL4, also known as KIR2DL4 is part of the killer cell Ig-like receptor (KIR) family. KIR proteins with the long cytoplasmic domain transduce inhibitory signals through an immune tyrosine-based inhibitory motif (ITIM), whereas KIR proteins which contain the short cytoplasmic domain, lack the ITIM motif and as a substitute associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. KIR2DL4 stimulates NK cells to produce IFN-gamma and stimulation with IL-2 upregulates cell surface expression on CD56dimcells and leads to the inhibition of the cytolytic NK cell function.

Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Protein-c Receptor (PROCR) is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The PROCR protein is an N-glycosylated type I membrane protein which enhances the activation of protein C. PROCR gene mutations are linked with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. In addition, PROCR may have a role in malarial infection and has been linked with cancer.

Canopy FGF Signaling Regulator 4 (CNPY4) is a part of the canopy family which owns one saposin B-type domain. CNPY4 takes part in the regulation process of the cell surface expression of TLR4.

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.

Cytokeratin 8 belongs to the type B (basic) subfamily of high molecular weight keratins and exists in combination with keratin 18. Cytokeratin 8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin polypeptides 8 and 18.

SSR4 is a member of the TRAP-delta family. SSR4 is the delta subunit of the translocon-associated protein complex that participates in translocating proteins through the endoplasmic reticulum membrane. SSR4 positioned in the Xq28 region and organized in a compact head-to-head manner with the isocitrate dehydrogenase 3 (NAD+) gamma gene. Both genes are motivated by a CpG-embedded bidirectional promoter.

The proteasome is a multicatalytic proteinase complex which holds an extremely organized 20S core structure shaped like a ring. The central structure is assembled from 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. There is a high concentration of proteasomes all over the eukaryotic cells and their job is to cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. PSMA3 encodes several of the peptidase T1A family which is a 20S core alpha subunit. Two alternative transcripts encoding diverse isoforms were recognized.

Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.

Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMFstimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation.

PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.

RALY belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) gene family. RALY takes part in pre-mRNA splicing and also in embryonic development. Moreover, alternate splicing results in multiple transcript variants have been found for RALY.

Cell Adhesion Molecule 1, also known as CADM1 belongs to the nectin family. CADM1 mediates homophilic cell-cell adhesion in a Ca2+-independent manner as well as mediating heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Furthermore, CADM1 perform as a tumor suppressor in non-small-cell lung cancer, NSCLC, cells. The interaction with CRTAM promotes natural killer (NK) cell cytotoxicity & IFN-gamma secretion by CD8+ cells in vitro over and above NK cell-mediated rejection of tumors expressing CADM3 in vivo.

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.

WAP four-disulfide core domain protein 2 (WFDC2) is a protease inhibitor, which belongs to the WFDC domain family. WFDC2 is effective with a broad range of proteases, e.g. aspartic, serine or thiol proteases. WFDC2 is expressed in several normal tissues, including the male reproductive system, regions of the respiratory tract and nasopharynx. WFDC2 may be involved in sperm maturation. WFDC2 is also highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines.

Protein Kinase CAMP-Dependent Catalytic Beta (PRKACB) belongs to the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule imperative for various cellular functions. cAMP activates the cAMP-dependent protein kinase, which transduces the signal by way of phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of 2 regulatory and 2 catalytic subunits. cAMP triggers the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to 4 cAMP and 2 free monomeric catalytic subunits. PRKACB mediates cAMP-dependent signaling initiated by receptor binding to GPCRs. PKA activation regulates various cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, in addition to regulation of intracellular transport mechanisms and ion flux. PRKACB regulates the abundance of compartmentalized pools of its regulatory subunits via phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their consequent proteolysis.

TP53I3 participates in the generation of reactive oxygen species (ROS). TP53I3 has low NADPH-dependent naphtoquinone reductase activity, with a preference for 1,2-naphtoquinone over 1,4-naphtoquinone. TP53I3 has low NADPH-dependent diamine reductase activity (in vitro). TP53I3 is localized to the cytoplasm and induced in primary, non-transformed and transformed cell cultures after exposure to genotoxic agents. TP53I3 microsatellite polymorphism is associated with differential susceptibility to cancer.

FHIT is a member of the histidine triad gene family. FHIT gene encodes a diadenosine 5',5'''-P1,P3-triphosphate hydrolase involved in purine metabolism. FHIT gene includes the common fragile site FRA3B on chromosome 3, where carcinogen-induced damage can lead to translocations and abnormal transcripts of this gene. The FHIT protein is a tumor suppressor with reduced or no expression in numerous types of cancer. FHIT may also act as a tumor suppressor in normal cells. Alterations and deletions of the FHIT (Fragile Histidine Triad) gene are strongly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach, and pancreas. The expression of FHIT is more often lost in cancers of individuals with familial mutations causing deficiency in DNA repair genes such as BRCA1, BRCA2 and MSH2. In vitro FHIT functions as a hydrolase that cleaves diadenosine triphosphate (Ap3A) to ADP and AMP. The FHIT -Ap3A enzyme-substrate complex seems to be the tumor suppressor signal. The restoration of FHIT expression in FHIT -deficient cancer cells leads to apoptosis, involving the intrinsic caspase pathway, in cancer-derived cells and in tumor xenografts.

The mammaglobin gene was first identified using a differential screening approach directed at the isolation of novel, human breast cancer-associated genes. Mammaglobin encodes a 10 kDa glycoprotein and is distantly relaetd to a family of epithelial secretory proteins that includes rat estramustine-binding protein/prostatein and human Clara cell 10 kDa protein (CC10)/uteroglobin. Mammaglobin, a mammary-specific member of the uterglobin family, is known to be overexpressed in human breast cancer. Studies suggest that mammaglobin is one of the first relatively mammary-specific and mammary-sensitive markers (85%). Mammaglobin may be valuable used in a panel with BRST-2 (GCDFP-15) and ER in evaluating tumors of unknown primary sites.
SCGB2A2 (the mammaglobin gene) is located on chromosome 11, at locus 11q13. SCGB2A2 is member of the secretoglobin superfamily of which is a group of small dimeric secreted and sometimes glycosylated proteins. Expressed mainly in mucosa, secretoglobins appear to be involved in cell signalling, immune response, chemotaxis, and might also serve as transporters for steroid hormones in humans.