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FXYD domain-containing ion transport regulator 5 (FXYD5) is a cancer-associated cell membrane glycoprotein which is a part of the FXYD family. FXYD5 is engaged in down-regulation of E-cadherin, which takes part in tumor development and metastasis and results in reduced cell adhesion.FXYD is found in spleen, lung, skeletal muscle, and testis tissue, and maps to human chromosome 19q13.2.

PDCD1 is a cell surface membrane protein of the immunoglobulin superfamily. PDCD1 is expressed in pro-B-cells and is thought to have a role in their differentiation. In mice, expression of PDCD1 gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for the PDCD1 gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that the PDCD1 gene product may also be important in T cell function and contribute to the prevention of autoimmune diseases.

The proteasome is a multicatalytic proteinase complex with a highly assembled ring-shaped 20S core structure which is composed of 4 rings of 28 non-identical subunits, 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are found throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. PSMA7 is part of the peptidase T1A family, that is a 20S core alpha subunit. PSMA7 interacts particularly with the hepatitis B virus X protein, a protein critical to viral replication. PSMA7 is involved in regulating hepatitis virus C internal ribosome entry site activity that is crucial for viral replication. PSMA7 is in charge for regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. PSMA7 is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. PSMA7 interacts specifically with two subdomains of HIF-1alpha and inhibited the transactivation function of HIF-1alpha under both normoxic and hypoxia-mimicking conditions.

SPG21 binds to the hydrophobic C-terminal amino acids of CD4 which take part in suppression of CD-4 dependant T cell activation. The interaction with CD4 is mediated by the noncatalytic alpha/beta hydrolase fold domain. SPG21 adapts the stimulatory activity of CD4. SPG21 is broadly expressed in diverse tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Mutations in SPG21 cause Mast syndrome, an autosomal-recessive complicated form of hereditary spastic paraplegia characterized by dementia, thin corpus callosum and white matter abnormalities.

SNRPF is a member of the snRNP Sm proteins family. There are at least seven isoforms, E, F, G, D1, D2, D3 and B/B. This type of common proteins have a crucial part in the biogenesis of the snRNPs. Moreover, they represent the major targets for the so-called anti-Sm auto-antibodies that are diagnostic for systemic lupus erythematosus (SLE). SNRPF assist in the cytoplasmic construction of the UsnRNPs by binding to aconserved Sm site on UsnRNA and forming a stable snRNP core complex.

Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes

Pirin (PIR) which belongs to the cupin superfamily, is an Fe(II)-containing nuclear protein expressed in all tissues of the body and concentrated within dot-like subnuclear structures. Pirin may function as a transcriptional cofactor and is involved in the regulation of DNA transcription and replication, as a result of interactions with nuclear factor I/CCAAT box transcription factor as well as B cell lymphoma 3-encoded oncoprotein.

Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.

S100A2 belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A2 may function as a modulator against excess calcium accumulation in normal human mammary epithelial cells and also have a role in suppressing tumor cell growth. S100A2 may have a tumor suppressor function. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. Chromosomal rearrangements and altered expression of the S100A2 gene are implicated in breast cancer.

SERPINB2 is an inhibitory serpin produced primarily in keratinocytes, stimulated monocytes, and placental trophoblasts. SERPINB2 is found primarily as a 47 kDa non-glycosylated intracellular protein that is induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated SERPINB2 are similarly effective as inhibitors of urokinase-type plasminogen activator (uPA), the only proven physiological target of SERPINB2.

XIAP Associated Factor 1 (XAF1) is a protein which binds to and counteracts the inhibitory effect of a member of the IAP (inhibitor of apoptosis) protein family. IAP proteins bind to and inhibit caspases which are activated in the course of apoptosis. The ratio of IAPs and proteins which interfere with their activity, such as the XAF1 protein, influence the progress of the apoptosis signaling pathway. Additionally, XAF1 inhibits anti-caspase activity of BIRC4. XAF1 induces cleavage and inactivation of BIRC4 independent of caspase activation. Furthermore, XAF1 mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells.

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

E3 ubiquitin ligase RNF4 (RNF4) contains a RING finger motif and functions as a transcription regulator. RNF4 interacts with, and inhibits the activity of, TRPS1, a transcription suppressor of GATA-mediated transcription. Transcription repressor ZNF278/PATZ also interacts with the RNF4 protein thus reducing the enhancement of androgen receptor-dependent transcription mediated by RNF4. RNF4 is broadly expressed at low levels in many tissues and highly expressed in the testis.

V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.

Opticin also known as OPTC is a member of the class III of the small leucine-rich repeat protein (SLRP) family. Members of this family are usually linked with the extracellular matrix. OPTC is attended in significant quantities in the vitreous of the eye and also localizes to the cornea, iris, ciliary body, optic nerve, choroid, retina, and fetal liver. OPTC might noncovalently bind collagen fibrils and regulate fibril morphology, spacing and organization. OPTC is mapped to a an area of chromosome 1 which is linked with the inherited eye diseases age-related macular degeneration (AMD) and posterior column ataxia with retinosa pigmentosa (AXPC1).

Pancreatitis-associated protein (PAP) is a secretory protein not normally expressed in healthy pancreas but highly induced during acute pancreatitis. While PAP has been shown to be anti-bacterial and antiapoptotic in vitro, its definitive biological function in vivo is not clear. Using antisepse oligonucleotides, inhibition of PAP expression significantly worsened pancreatitis in a rat model. During pancreatitis, PAP released by the pancreas could mediate lung inflammation through induction of hepatic TNF- alpha expression and subsequent increase in circulating TNF-alpha.
PAP is activated in primary liver cancers. In normal liver, the protein is undetectable in normal mature hepatocytes and found only in some ductular cells, representing potential hepatic progenitor cells. PAP can be considered hepatic cytokine that combines mitogenic and anti-apoptotic functions regarding hepatocytes, and consequently acts as a growth factor in vivo to enhance liver regeneration. In pancreatic cancor, PAP was overexpressed in 79% (30 of 38) of pancreatic ductal adenocarcinoma, 19% (7 of 36) of chronic pancreatitis, and 29% (2 of 7) of mucinous cystadenoma. PAP was found in malignant ductular structures in pancreatic carcinomas as well as in benign proliferating ductules and acinar cells in chronic pancreatitis. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells and is also correlated to tumour load as expressed by the UICC stages.
Epithelial expression of PAP was induced under intestinal mucosal inflammation initiated by exposure to commensal bacteria or DSS as well as inflamed IBD colon. Increased serum level of PAP diagnosed ileal location in active Crohn disease with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%. Elevated serum PAP (> 50 ng/mL) is significantly associated with disease activity and ileal location of Crohn disease.

SNRPD2 is a member of the small nuclear ribonucleoprotein core protein family. SNRPD2 is a small nuclear ribonucleoprotein (snRNPs) which comprises the spliceosome in eukaryotes. SNRPD2 is required for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis.

TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.

DBI, also known as Acyl-CoA-binding protein isoform 2, is a binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.

Ribosomal Protein L26 (RPL26) is a ribosomal protein which is a component of the 60S subunit (the large subunit of the ribosome). RPL26 is a part of the L24P family of ribosomal proteins which is located in the cytoplasm. There are numerous processed pseudogenes of RPL26 dispersed through the genome as usual for genes encoding ribosomal proteins.

Diphthamide biosynthesis protein 2 (DPH2) is a homodimer and each of its monomers can bind a [4Fe-4S] cluster. DPH2 is the target of ADP ribosylating diphtheria toxin (DT) and Pseudomonas exotoxin A (PE). DPH2 was identified by its ability to complement a diphthamide mutant strain, and thus serves in diphthamide biosynthesis. The loss of DPH2 pre-activates NF-kB and death receptor pathways and renders MCF7 cells hypersensitive to tumor necrosis factor.

CARD18 belongs to the death-domain-fold superfamily which is induced by proinflammatory stimuli. CARD18 contains basically only a Caspase recruitment domain, inhibits generation of IL-1b by cooperating with caspase-1 and inhibiting connotation with RIP 2. The connotation of CARD18 to caspase-1 is enabled by the charge-charge interactions between the prodomain of caspase-1 and the surface charge of CARD18.

In the absence of additional proteins - the general transcription factors (GTFs) RNA polymerases are unable to initiate RNA synthesis. GTFs accumulate in a complex on the DNA promoter and recruit the RNA polymerase. GTF3C family proteins are vital for RNA polymerase III to produce several small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin.