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JAM3 belongs to the junctional adhesion molecule protein family and functions as a receptor for another member of this family. JAM3 plays a part in cell-cell adhesion. The soluble form of JAM3 is a mediator of angiogenesis. JAM3 is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). A mutation in an intron of the JAM3 gene is linked with hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts.

THAP3 is an element of a THAP1/THAP3-HCFC1-OGT complex which is essential for the regulation of the transcriptional activity of RRM1. THAP3 is vastly produced in placenta, skeletal muscle and heart.

APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport.

C-type Lectin Domain Family 4, Member M (CLEC4M) is a type II integral membrane proteinand A pathogen-recognition receptor which takes part in peripheral immune surveillance in liver. CLEC4M mediates the endocytosis of pathogens which than degraded in lysosomal compartments. CLEC4M is a receptor for ICAM3, binding to mannose-like carbohydrates and also recognizes various evolutionarily divergent pathogens with a large impact on public health, including tuberculosis mycobacteria, and viruses which among them are Ebola, hepatitis C,influenza A, HIV-1, West Nile virus and the SARS-CoV acute respiratory syndrome coronavirus.

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.

Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.

Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.

Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described. Protein phosphatase 2C(PP2Cα) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.

Killer Cell Lectin-Like Receptor Subfamily C, Member 1 (KLRC1) is a part of the killer cell lectin-like receptor family. KLRC1 functions as a receptor for the detection of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRC1 is also connects with CD94 and is expressed on NK cells and some activated T cell.

Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

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.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

DNAJC19 is part of a complex involved in the ATP-dependent transport of transit peptide-containing proteins from the inner cell membrane to the mitochondrial matrix. DNAJC19 is a single-pass membrane protein which contains a J domain and is localized to the inner membrane of the mitochondrion. Expressed ubiquitously, DNAJC19 acts as a component of the mitochondrial DNAJC19 complex that is responsible for the ATP-dependent translocation of select proteins from the inner mitochondrial membrane to the mitochondrial matrix. Defects in the DNAJC19 gene are the cause of 3-methylglutaconic aciduria type 5 (MGA5), otherwise known as dilated cardiomyopathy with ataxia (DCMA).

The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily.

The superfamily includes large families of growth and differentiation factors.

Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.

This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.

Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

Complement Component C5a (C5a) is involved in the complement system and it is encoded by the C5 gene in human. Complement C5 is cleaved into C5a and C5b. C5a has an imperative role in chemotaxis and C5b forms the 1st part of the complement membrane attack complex. Complement C5 is the 5th component of complement, which plays a central role in inflammatory and cell killing processes. C5a protein is composed of alpha and beta polypeptide chains, which are linked by a disulfide bridge. An activation peptide, C5a, which is an anaphylatoxin, which has potent spasmogenic and chemotactic activity, is derivative from the alpha polypeptide via cleavage with a convertase. The C5b macromolecular cleavage product forms a complex with the C6 complement component, and this complex is the basis for creation of the membrane attack complex, which includes supplementary complement components.

PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.

Mitochondrial Ribosomal Protein S23, also known as MRPS23 belongs to the mammalian mitochondrial ribosomal proteins which are encoded by nuclear genes and assist in proteinsynthesis inside the mitochondrion. Mitochondrial ribosomes consist of a small 28S subunit and a large 39S subunit. In addition, they have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio isreversed. An additional difference between mammalian mitoribosomes and prokaryotic ribosomes is that the lattercontain a 5S rRNA. Between different species, the proteins containing the mitoribosome differ very much in sequence, and occasionally in biochemical properties, which prevents easy recognition by sequence homology.

STE20-Related Kinase Adaptor Alpha (STRADA) is a part of the STE- 20 like kinase family which stimulates MAPK pathways by activating MAPKKK. STRADA is an upstream activator of LKB1 and also leads the sub-cellular localization of LKB1 by fixing it in the cytoplasm. The interaction between STRADA-LKB1 leads to phosphorylation of STRADA and enhanced autophosphorylation of LKB1.

PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.

Synaptojanin 2 Binding Protein (SYNJ2BP) contains 1 PDZ (DHR) domain which binds to isoform 2A of SYNJ2 (through the unique motif in the C-terminus) and interacts with MAPK12.

Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.

Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in b sheet (b-domain) and a smaller a-helical domain (a-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).