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Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.

Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

Protein tyrosine phosphatase type IVA 1 (PTP4A1) is a cell signaling molecule that has regulatory roles in a variety of cellular processes. PTP4A1 is a unique nuclear PTP which is induced in regenerating liver and mitogen stimulated cells. PTP4A1 is primarily expressed in the spleen, bone marrow, thymus, lymph nodes, T lymphocytes and tonsil and is overexpressed in tumor cell lines.

LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

Human immunodeficiency virus (HIV) is a retrovirusthat can lead to a condition in which the immune systembegins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the humanimmune systemsuch as helper T cells(specifically CD4+ T cells), macrophagesand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosisin infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytesthat recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunityis lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genomeis converted to double-stranded DNAby a virally encoded reverse transcriptasethat is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integraseso that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latentand the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.

Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

FGF-1 Intracellular-Binding Protein (FIBP) which is a member of Fibroblast growth factors (FGFs) binds to internalized FGF-1 and is thought to be involved in mitogenic function of FGF-1. FGF activity effects development, adult tissue homeostasis, angiogenesis and cancer progression. FIBP localizes to the nucleus and is greatly expressed in heart, skeletal muscle and pancreas and at lower levels in brain, placenta, liver and kidney.

Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

Cysteine-rich PDZ-binding protein, also known as CRIPT, takes part in the cytoskeletal anchoring of DLG4 in excitatory synapses.

Cysteine-Rich Secretory Protein 2 (CRISP2) regulates some ion channels activity and thereby regulates calcium fluxes during sperm capacitation. Amongst its related pathways are p53 signaling. Diseases related with CRISP2 include epididymitis and orchitis.

The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

Serpin Peptidase Inhibitor, Clade A Member 9, also known as serpin A9, belongs to the Serpin superfamily of serine protease inhibitors. Serpins are the most extensively distributed superfamily of protease inhibitors which use a conformational modification to inhibit target enzymes. Serpins are known to inhibit serine proteases as well as inhibiting caspases in addition to papain-like cysteine proteases. Serpins are conformational labile and numerous of the disease-linked mutations of serpins outcome in misfolding or in pathogenic, inactive polymers. serpin A9 demonstrates inhibition towards trypsin, thrombin, as well as plasmin and binds DNA and heparin.

Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

LASP1 has a vital part in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation can additionally assist in regulation of actin-associated ion transport activities in the parietal cell and in several other F-actin-rich secretory epithelial cell types.

RTN4IP1 is a unique mitochondrial protein that interacts with reticulon 4, which is an effective inhibitor of regeneration ensuing spinal cord injury. The reticulon 4 interaction with mitochondrial proteins may offer insight into the mechanisms for reticulon-induced inhibition of neurite growth.

Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.

Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.

PABPN1 is an highly expressed nuclear protein which has high affinity to nascent poly(A) tails. PABPN1 is essential for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and regulates the length of the poly(A) tail to about 250 nt. In its steady-state, PABPN1 is restricted to the nucleus however there are different poly(A) binding proteins which can be found in the cytoplasm. PABPN1 has a GCG trinucleotide repeat at the 5' end of the coding region. Expansion of this repeat from the normal 6 copies to 8-13 copies results in autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Associated pseudogenes were located on chromosomes 19 and X. Additionally, there is a read-through transcription between PABPN1 gene and the adjacent upstream BCL2L2 (BCL2-like 2) gene.

PAIP2 has a role as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. PAIP2 inhibitory activity on translation is mediated through its action on PABPC1. PAIP2 displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. PAIP2 association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.

Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

The 23kDa two-domain periplasmic chaperone FIMC from E.coli is vital for the assembly of type-1 pili, which are filamentous, very oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces and persist in macrophages.

GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.