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Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belongs to the CC chemokine family which is also known as monocyte chemotactic protein-1 (MCP-1). MCP 1 is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts. CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. MCP 1is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

PNP is a member of the PNP/MTAP phosphorylase family of proteins. PNP catalyzes the reversible phosphorolysis of ribonucleosides and 2’-deoxyribonucleosides with specificity for guanine, hypoxanthine and their analogs. PNP deficiency is a rare autosomal recessive genetic disease linked to a severe defect in T-lymphocyte function and neurologic disorder in children, comprising four percent of combined immunodeficiency cases.

Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species. A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore. Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin. Alpha-1-microglobulin was first discovered in pathological human urine. It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include: inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.
Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

Heterogeneous Nuclear Ribonucleoprotein K, also known as HNRNPK, is a part of the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPK takes part in p53/TP53 reaction to DNA damage, acting at the level of both transcription activation and repression. HNRNPK is located in the nucleoplasm and has 3 repeats of KH domains which bind to RNAs.

The granulocytic anaplasmosis disease is initiated by the Gram-negative bacterium Anaplasma phagocytophilum. Anaplasma Msp5 is preserved among the Anaplasma classes and expressed in the salivary glands of infected ticks.

Mycoplasma pneumonia is part of the atypical pneumonia subtype which is caused by the bacteria M. pneumoniae. Mycoplasma pneumonia affects individuals younger than 40. It makes up 15 - 50% of all pneumonia cases in adults and especially in school-aged children. People at great risk for mycoplasma pneumonia comprise of those living or working in busy areas such as schools and homeless shelters, although many people who contract mycoplasma pneumonia have no identifiable risk factor. P1, P30, and P116 of mycoplasma pneumonia membrane proteins have been recognized as adhensive factors, P1 is considered as a main adhension protein of the organism colonization.

BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.

Chemokine (C-C motif) ligand 8 (CCL8) is a small cytokine belonging to the CC chemokine family that was once called monocyte chemotactic protein-2 (MCP-2). The CCL8 protein is produced as a precursor containing 109 amino acids, which is cleaved to produce mature CCL8 containing 75 amino acids. The gene for CCL8 is encoded by 3 exons and is located within a large cluster of CC chemokines on chromosome 17q11.2 in humans. MCP-2 is chemotactic for and activates a many different immune cells, including mast cells, eosinophils and basophils, (that are implicated in allergic responses), and monocytes, T cells, and NK cells that are involved in the inflammatory response. CCL8 elicits its effects by binding to several different cell surface receptors called chemokine receptors. These receptors include CCR1, CCR2B and CCR5.

PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.

MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.

Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction. Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

MVK is a member of the GHMP kinase family. Mevalonate is a vital mediator, and MVK an important early enzyme, in isoprenoid and sterol synthesis. MVK deficiency can result in gene mutation associated with Mevalonic aciduria, an illness which causes psychomotor retardation, failure to thrive hepatosplenomegaly, anemia and frequent febrile crises. Mutations in this gene also cause hyperimmunoglobulinaemia D and sporadic fever syndrome, in which the person suffers from recurrent episodes of fever related with lymphadenopathy, skin rash, gastrointestinal dismay and arthralgia.

PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

Charged multivesicular body protein 6 (CHMP6) is a member of the SNF7 family. The CHMP6 protein is a core component of the endosomal sorting necessary for transport complex III (ESCRT-III) that is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) which are produced by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes facilitating degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.

MAPK3 is a part of the MAP kinase family which is recognized as extracellular signal-regulated kinases (ERKs), that function in a signaling cascade that controls various cellular procedures such as proliferation, differentiation, and cell cycle progression in reaction to a variety of extracellular signals. MAPK3 is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets.

MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.

MOB3B is similar to yeast Mob1 protein which binds Mps1p, a protein kinase vital for spindle pole body duplication and mitotic checkpoint regulation. MOB3B is situated on the opposite strand as the INF kappa precursor (IFNK) gene.

MYL9 is one of the numerous regulatory myosin light chains. Myosin which is a structural component of the muscle consists of 2 heavy chains and 4 light chains. MYL9 is a myosin light chain regulates muscle contraction by modulating the ATPase activity of myosin heads. MYL9 binds calcium and is activated by myosin light chain kinase. Regulatory myosin light chains regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of regulatory myosin light chains is catalyzed by MLCK in the presence of calcium and calmodulin and it increases the actin-activated myosin ATPase activity, thus regulates the contractile activity.

Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

MORF4L2 belongs to the mortality factor (MORF) family of transcriptional regulator which is involved in cell growth, regulation and senescence. MORF4L2 localizes to the nucleus, and it has a protein kinase C phosphorylation site as well as a tyrosine phosphorylation site. MORF4L2 interacts with the Rb tumor suppressor through its helix-loop-helix and leucine zipper regions. Furthermore, MORF4L2 has histone deacetylase activity and can either repress or promote the activity of the B-Myb promoter depending on the tissue.

MAPK12 is a member of the MAP kinase family. MAPK12 acts as a signal transducer during differentiation of myoblasts to myotubes. p38 proteins utilizes magnesium as a cofactor to catalyze the ATP-dependent phosphorylation of target proteins and is produced in several regions all over the body with common expression patterns in heart.

Macrophage Inflammatory Proteins 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 also named CCL3 and CCL4. Both factors are produced by macrophages after they are stimulated with bacterial endotoxins. MIP-1a and MIP-1b activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. MIP-1a and MIP-1b induce synthesis and release of other pro-inflammatory cytokines such as interleukin-1 (IL-1), IL-6 and TNF-alpha from fibroblasts and macrophages. CCL3 and CCL4 genes are both located on human chromosome 17.

Acid phosphatase, prostate (ACPP) is a non-specific tyrosine phosphatase, which dephosphorylates a varied number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.