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CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

DNA repair protein complementing XP-A cells, (XPA), is a member of the XPA family. XPA protein takes a part in DNA excision repair. It Inductees repair by binding to damaged sites with different affinities depending on the photoproduct and the transcriptional state of the region. Defects in XPA is the reason of xeroderma pigmentosum complementation group A (XP-A), which is infrequent human autosomal recessive disease which characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight, also may cause to neurological abnormalities.

BCL2L2 promotes cell survival and blocks dexamethasone-induced apoptosis. BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. BCL2L2 is part of the BCL-2 protein family which form hetero- or homodimers and play an important role as anti and proapoptotic regulators. BCL2L2 causes reduced cell apoptosis under cytotoxic conditions. BCL2L2 is involved in the survival of NGF- and BDNF-dependent neurons. BCL2L2 plays an important role in adult spermatogenesis.

PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention. PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression. Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

TDP1 belongs to the phospholipase D family and contains two PLD phosphodiesterase domains. TDP1 is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks. Mutations in the TDP1 gene are linked to the disease spinocerebellar ataxia with axonal neuropathy (SCAN1).

BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.

PPCDC is a member of the HFCD (homo oligomeric flavin containing Cys decarboxylase) superfamily which takes a part in the biosynthesis of coenzyme A (CoA) from pantothenate (Vitamin B). The biosynthesis of CoA from pantothenate needs several steps: the phosphorylation of pantothenate, the conversion of 4’-hosphopantothenate to 4''-phosphopantetheine, the adenylation by phosphopantetheine adenylyltransferase to form dephospho-CoA and the phosphorylation by dephospho-CoA kinase to form CoA. PPCDC is a key player in this pathway. PPCDC converts 4''-phosphopantothenate into 4''-phosphopantetheine.

STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.

FAS / CD95 is a 36kDa transmembrane type I receptor, which belongs to the NF/NGF receptor super-family. It is a potent inducer of apoptosis in cells of the immune system upon interaction with its natural ligand, CD95L. Although the CD95/CD95L system could play a role in tumor regression, tumor cells seem to down-regulate CD95 expression as a mechanism of resistance to CD95L-induced killing by T lymphocytes and NK cells. The Fas antigen is expressed on the surface of various cell types, including activated T and B lymphocytes and T lymphoblastoid cell line. CD95 is also expressed in a broad panel of non-transformed cells outside the immune system.

SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.

CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

CD27 belongs to the TNF-receptor superfamily. CD27 is necessary for initiation and long-term maintenance of T cell immunity. CD27 binds to ligand CD70, and has a crucial role in regulating B-cell activation and immunoglobulin synthesis. The CD27 receptor transduces signals which result in the activation of NF-kappaB and MAPK8/JNK. Adaptor proteins TRAF2 and TRAF5 mediate the signaling process of CD27. CD27-binding protein (SIVA), which is a proapoptotic protein, can bind to the CD27 receptor and is believed to have a significant role in the apoptosis induced by CD27.

T-cell surface glycoprotein CD3 zeta chain (CD247) is a member of the CD3Z/FCER1G family. CD247 is T-cell receptor zeta, which along with T-cell receptor alpha/beta and gamma/delta heterodimers, and also with CD3-gamma, -delta and -epsilon, creates the T-cell receptor-CD3 complex. The zeta chain has a central role in coupling antigen recognition to several intracellular signal-transduction pathways. Low expression of the CD247 antigen causes impaired immune response.

Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.

TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.

Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.

CDC34 takes part in the control of cell cycle and DNA replication. Cdc34 in association with different E3 complexes, including SCF, targets many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. Cdc34 substrates that have been characterized include B-Myb, Wee1, MyoD, ATF5, p27Xic1, and p27Kip1. Additionally, substrates such as p21Cip1, E2F, cyclin E, and cyclin D are putative substrates of Cdc34 by virtue of their SCF requirement for proteolysis. Cdc34 is self-associate through a domain in the C-terminus, and is phosphorylated and ubiquitinylated in vivo. CDC34is useful for in vitro ubiquitinylation reactions.

Cyclin-dependent kinase 1 (CDK1) plays a significant part in the control of the eukaryotic cell cycle through modulating the centrosome cycle in addition to mitotic onset; CDK1 promotes G2-M transition and regulates G1 progress and G1-S transition using association with multiple interphase cyclins. CDK1 is essential in higher cells for the entry into S-phase and mitosis.

BAG3 Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG3 has anti-apoptotic activity. BAG proteins participate with Hip for their binding to Hsc70/Hsp70 ATPase domain and encourage substrate release. BAG proteins have about 45 amino acid BAG domain close to the C terminus however they differ noticeably in their N-terminal regions. BAG3 includes a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact particularly with the Hsc70 ATPase domain in vitro and in mammalian cells. They bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. BAG3 plays a role as a protein-refolding cochaperone of the bcl2 binding protein BAG family and as upregulated in response to persistent stress of cellular calcium balance dysregulation. BAG3 has been shown to diminish stress-induced apoptosis.

CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.