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GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.

The retinoid X receptor (RXR) is a pleiotropic nuclear receptor transcription factor that interacts with a variety of nuclear receptor dimeric partner. RXR binds cognate response elements as a homodimer in the presence of its ligand, 9-cis retinoic acid, or as a heterodimer with other members of the nuclear hormone receptor superfamily including retinoic acid receptors (RAR), thyroid hormone receptors (TR), vitamin D receptors and peroxisome proliferators-activated receptors (PPAR). The RXR family includes three different isoforms; RXR a, b, g . Human RXR a gene is localized on 9q34.9 and encodes two major isoforms (RXR a1, RXR a2). The DNA binding domain of RXR (111-228aa) was purified by using conventional column chromatography techniques.

C1QBP having the accession number of NP_001203 binds to the globular "heads" of c1q thus inhibiting c1 activation. C1QBP interacts with a wide range of ligands and is implicated in cell signaling. C1QBP associates with C1r and C1s in order to yield the first component of the serum complement system. C1QBP protein has been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein.
C1QBP is a new marker of tumor cells and tumor-associated macrophages/myeloid cells in hypoxic/metabolically deprived areas of tumors.
Mitochondrial C1QBP is a critical mediator of p14ARF-induced apoptosis.
C1QBP functions as a chemotactic factor for immature dendritic cells, and migration is mediated through ligation of both C1QBP and cC1qR/CR.
C1QBP overexpression successfully blocks mRNA accumulation from the adenovirus major late transcription unit (MLTU) and stimulates RNA polymerase II carboxy-terminal domain phosphorylation in virus-infected cells.
C1QBP binds with Hepacivirus core protein on CD8+ and CD4+ positive t-cells and inactivates lck and akt.

TAF9 is a universal transcription factor which enables the preinitiation complex assembly by direct interactions with the TATA promoter element. TAF9 is a multisubunit complex consisting of a small TATA-binding polypeptide and other TBP-associated factors (TAFs) and performs as a channel for regulatory signals.

IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

Vanin 1 (VNN1) belongs to the vanin family of proteins, which share extensive sequence similarity with each other, and also with biotinidase. This family includes secreted and membrane-associated proteins, a few of which have been described to participate in hematopoietic cell trafficking. No biotinidase activity has been established for any of the vanin proteins; nevertheless, they possess pantetheinase activity, which may have a role in oxidative-stress response. VNN1 protein, like its mouse homolog, is probably a GPI-anchored cell surface molecule. The mouse VNN1 protein is expressed by the perivascular thymic stromal cells and regulates migration of T-cell progenitors to the thymus. VNN1 is an amidohydrolase which hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5).

Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

EIF1 is important for scanning and plays a role in initiation site selection. EIF1 promotes the assembly of 48S ribosomal at the authentic initiation codon of a conventional capped mRNA.

Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

C1QTNF3 also called Cartducin is a novel angiogenic factor in the formation of neointima following angioplasty. C1QTNF3 a paralog of Acrp30 (adiponectin). C1QTNF3 is a secretory protein produced by chondrogenic precursors & proliferating chondrocytes, and belongs to a novel C1q family of proteins. Cartducin promotes the growth of mesenchymal chondroprogenitor cells & chondrosarcoma-derived chondrocytic cells in vitro. Cartducin stimulates mesenchymal chondroprogenitor cell proliferation through extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways. C1QTNF3 promotes proliferation & the migration of endothelial cells.

IL-12 is a heterodimeric cytokine that stimulates the production of IFN gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.

Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.

S100A13 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. 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. S100A13 is extensively expressed in various types of tissues with an elevated expression level in the thyroid gland. In smooth muscle cells, S100A13 co-expresses with other family members in the nucleus and in stress fibers, suggesting diverse functions in signal transduction.

RPS3A is a member of the S3AE family of ribosomal proteins. Ribosomes, the organelles which catalyze protein synthesis, composed of a large 60S subunit and a small 40S subunit. Together these subunits consist of 4 RNA classes and around 80 structurally diverse proteins. RPS3A, a component of the 40S subunit, is a ribosomal protein that is situated in the cytoplasm. Interference of the gene encoding rat ribosomal protein S3a, in v-fos-transformed rat cells cause a degeneration of the transformed phenotype.

RASSF1A protein is a potential tumor suppressor like the RAS effector proteins. Presence or absence expression of this gene has been related with the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of this RASSF1A gene. The inactivation of RASSF1A was found to be associated with the hypermethylation of its CpG-island promoter region. RASSF1A required for death receptor-dependent apoptosis.

Acyl-CoA Thioesterase 8 (ACOT8) is a group of enzymes which catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), granting the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ACOT8 mediate Nef-induced down-regulation of CD4. ACOT8 contends with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 prefers medium-length fatty acyl-CoAs.

Ribosomes (the organelles that catalyze protein synthesis) consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS10 which is is located in the cytoplasm and a part of the S10E family of ribosomal proteins, is a ribosomal protein that is a component of the 40S subunit. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.

SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner.

IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.

Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
In mice, targeted mutations in FABP4 provide significant protection from IR in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages.