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Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.

Nuclear factor (erythroid-derived 2)-like 2 (NRF2) is bZIP transcription factors which heterodimerize with Maf proteins to bind Mare sequences. In addition, the NRF proteins bind the antioxidant response element (ARE) and are associated with the regulation of detoxification enzymes and the oxidative stress response. NRF2 is extensively expressed and is assumed to translocate to the nucleus after treatment with xenobiotics and antioxidants, which stimulate its release from its repressor protein, Keap1.

TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of GMCSF is found extracellularly as a homodimer. GMCSF has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.

TRAIL Receptor-1 (DR4) and TRAIL Receptor-2(DR5) are members of the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain", which is capable of activating the cell's apoptotic machinery. These receptors are activated by binding to either membrane anchored or soluble TRAIL/Apo2L.

Signal-regulatory protein beta-1 isoform 1 or SIRPB1, is an immunoglobulin-like cell surface receptor which is a part of the SIRP superfamily. SIRPB1 is a cell membrane receptor that takes part in the negative regulation of tyrosine kinase-coupled signaling pathway. SIRPB1 is engaged in the activation of tyrosine kinase SYK, SIRP alpha molecules (activates SHP-1 and SHP-2 protein tyrosine phosphatases), etc.

The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.

GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.

MCSFR which is also familiar as CSF1R, is part of the type3 subfamily of receptor tyrosine kinases. MCSFR is expressed mainly on cells of the monocyte and macrophage lineage, stem cells, and in the growing placenta. Most of the biological effects of this cytokine are mediated by MCSFR. MCSFR contains an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Originally CSF1 and this receptor were implicated as vital for normal trophoblastic implantation as well as monocyte development. The role of CSF1/CSF1R in normal mammary gland development is actually very interesting since this connection has also been discovered in the biology of breast cancer with the results of abnormal expression of CSF1 and its receptor. Likewise, in Alzheimer's disease and after brain injuries an increased level of CSF1R was found in the microglia, which causes the microglia to become more active.

NADH Dehydrogenase 1 Beta Subcomplex 4 (NDUFB4) is a member of the complex I NDUFB4 subunit family. NDUFB4 is a non-catalytic subunit of the multisubunit NADH:ubiquinone oxidoreductase, which is the first enzyme complex in the mitochondrial electron transport chain (complex I). Mammalian complex I is comprised of 45 different subunits and transfers electrons from NADH to ubiquinone.

GNB3 belongs to the WD repeat G protein beta family. GNB3 is an important regulator of alpha subunit, as well as of certain signal transduction receptor and effector. A single-nucleotide polymorphism (C825T) in GNB3 is linked with essential hypertension and obesity. In addition, this polymorphism is also linked with the occurrence of the splice variant GNB3-s, which seems to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites. Further splice variants may exist for GNB3, however they have not been fully described. Among the diseases associated with GNB3 are syncope, and aortic coarctation.

Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.

TRAIL Receptor-1 (DR4) and TRAIL Receptor-2(DR5) are members of the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain", which is capable of activating the cell's apoptotic machinery. These receptors are activated by binding to either membrane anchored or soluble TRAIL/Apo2L.

SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

PSMB6 belongs to the proteasome B-type family (T1B family) which is a 20S core beta subunit in the proteasome. The PSMB6 is not present in the immunoproteasome and is replaced by PSMB9. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. The core structure is comprised of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits.

Activating transcription factor 4 (ATF4) is a member of a family of DNA-binding proteins which includes the AP-1 family of transcription factors, cAMP-response element binding proteins and CREB-like proteins. The ATF4 gene encodes a transcription factor which was initially identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1.

Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.

NAGK is a member of the eukaryotic-type N-acetylglucosamine kinase family. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a key component of complex carbohydrates, from lysosomal degradation or alimentary sources into GlcNAc 6-phosphate. NAGK is a prominent salvage enzyme of amino sugar metabolism in mammals. NAGK cooperates with STK16 and LNX1 and has ManNAc kinase activity.

NDRG2 belongs to the N-myc downregulated gene family that is a part of the alpha/beta hydrolase superfamily. NDRG2 takes part in dendritic and neuronal cell differentiation and outgrowth and is found in large quantities in heart, dendritic cells, brain, salivary gland and skeletal muscle and in small quantities in kidney and liver. In Alzheimer Disease (AD)-affected patients NDRG2 is found in brain lesions and is believed to be related to the progression of AD.

BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.