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FANK1 was localized in the nuclei of identical cells in the seminiferous epithelium. Depending on its nuclear localization, a gene ontology analysis proposes that FANK1 has a DNA binding activity therefor operates as a transcription factor. The extremely controlled expression of FANK1, suggests that it takes part in regulating gene expression in the transition from the meiotic phase to the haploid phase throughout spermatogenesis.

Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.

Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.

Developmentally-regulated GTP-binding protein 1 (DRG1) is a member of the GTP1/OBG family. DRG1 has a role in cell proliferation and differentiation, as well as in apoptosis, proposing a role in tumor formation and metastasis. Expression of the DRG1 was considerably reduced in breast tumor cells, particularly in patients with lymph node or bone metastasis as compared to those with localized breast cancer. The DRG1 protein is expressed at high levels in the heart, kidney and skeletal muscle and at lower levels in the brain, liver, placenta, lung, colon and spleen.

Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

Osteoclast-associated immunoglobulin-like receptor isoform 6 or OSCAR, is a receptor for surfactant protein D that can be found on human myeloid cells. OSCAR is part of the TNF-α release from human CCR2+ inflammatory monocytes process. The protein is involved in antigen presentation and activation of dendritic cells. Preosteoclasts or mature osteoclasts express the OSCAR protein. Patients that suffer from RA (rheumatoid arthritis) has upregulations on monocytes which present increased proosteoclastogenic potential.

Herpesvirus entry mediator or HVEM or tumour necrosis factor receptor superfamily member 14 or TNFRSF14, is part of the TNF receptors family that is a receptor located on the cell surface. The cytoplasmic area of this receptor can bind all sorts of TNF receptor associated factor (TRAF) protein. Those proteins can mediate pathways activating an immune response. The MITF is regulating TNFRSF14 gene expression.

SPARC protein, or secreted protein acidic and rich in cysteine, or osteonectin or basement-membrane protein 40 is a protein that is coded by the SPARC gene in humans. It is a glycoprotein located in bones, that binds to calcium. The osteonectin is secreted from osteoblasts cells when boas are formed, mineralized and promotes the formation and creation of mineral crystals. Asides from calcium, it has been shown that this protein can also bind to collagen.

Translocase of Inner Mitochondrial Membrane 8 Homolog A (TIMM8A) takes part in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial. TIMM8A plays a role as a chaperone-like protein which protects the hydrophobic precursors from aggregation and leads them through the mitochondrial intermembrane space. TIMM8A is essential for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Defects in TIMM8A cause Jensen syndrome. TIMM8A and TIMM13, forms a 70 kDa heterohexamer.

KLRC3 belongs to the NKG2 group that can be found mostly in natural killer (NK) cells and encodes a family of transmembrane proteins known for their C-type lectin domain and their type II membrane orientation (extracellular C terminus). The NKG2 gene family is situated inside the NK complex, a region which has quite a few C-type lectin genes mostly expressed on NK cells.

Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.

Mediator Complex Subunit 20 (MED20) is a subunit of the Mediator complex, which is a multiprotein coactivator of RNA transcription that interacts with DNA-bound transcriptional activators, RNA polymerase II, and general initiation factors. The Mediator functions as a link to transmit information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. Mediator is recruited to promoters by direct interactions with regulatory proteins and functions as a scaffold for the compilation of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR. Recombinant Human TNFR is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules.
It inhibits the activity of TNF in vitro and has been shown to affect several animal models of inflammation, including murine collagen-induced arthritis. TNFR inhibits binding of both TNF? and TNF? (lymphotoxin alpha [LT?]) to cell surface TNFRs, rendering TNF biologically inactive. Cells expressing transmembrane TNF that bind to TNFR are not lysed in vitro in the presence or absence of complement.
TNFR can also modulate biological responses that are induced or regulated by TNF, including expression of adhesion molecules responsible for leukocyte migration (i.e., E-selectin and to a lesser extent intercellular adhesion molecule-1 [ICAM-1]), serum levels of cytokines (e.g., IL-6), and serum levels of matrix metalloproteinase-3 (MMP-3 or stromelysin).

Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily, and the junctional adhesion molecule (JAM) family. JAM2 is a type I membrane protein which is localized at the tight junctions of both epithelial and endothelial cells. JAM2 functions as an adhesive ligand for interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs.

Troponin I, fast skeletal muscle (TNNI2), belongs to the troponin I gene family, and a part of the troponin complex including troponin T, troponin C and troponin I subunits. The troponin complex, along with tropomyosin, is responsible for the calcium-dependent regulation of striated muscle contraction. TNNI2 is also suppresses tumor growth in human ovarian carcinoma. Mutations in TNNI2 cause myopathy and distal arthrogryposis type 2B.

Fc Fragment Of IgG Receptor And Transporter also known as FCGRT is a transmembrane glycoprotein with structural homology to MHC class 1 proteins. FCGRT is widely expressed in endothelial and epithelial cells and takes a vital part in IgG homeostasis. Moreover, FCGRT is expressed in neutrophils in addition myeloid antigen presenting cells. FCGRT can enhance IgG-meditated phagocytosis as well as antigen presentation by heses cells, however it promotes the degradation of opsonizing IgG rather than returning it to the circulation.

Actin is a muscle protein localized in the I band of the myofibrils; acting along with myosin, it is responsible for contraction and relaxation of muscle. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans. Its other functions include cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.

AKAP7 is a member of the A-kinase anchoring protein (AKAP) family, a group of functionally related proteins which bind to a regulatory subunit (RII) of cAMP-dependent protein kinase A (PKA) and target the enzyme to specific subcellular sections. AKAP7 is expressed in heart, brain, pancreas, lung and skeletal muscle. AKAP7 binds PKA to the plasma membrane, and allows efficient coupling to the L-type calcium channel.

Replication Protein A2 (RPA2) is a single stranded DNA binding protein. Human RPA2 is a heterotrimeric protein containing subunits of 14, 32 and 70kDa. The RPA2 protein complex is highly conserved in eukaryotes and is crucial in DNA replication, homologous recombination and nucleotide excision repair. RPA2 C-terminus specifically interacts with the DNA repair enzyme UNG2 and repair factors XPA and Rad52, each of which functions in a different repair pathway. Additionally, RPA2 binds specifically to the SH2 domain of Stat3 in vivo, and overexpression of RPA2 corresponds to the augmented growth factor-stimulated tyrosine phosphorylation and transcription activities of Stat3.

SSR4 is a member of the TRAP-delta family. SSR4 is the delta subunit of the translocon-associated protein complex that participates in translocating proteins through the endoplasmic reticulum membrane. SSR4 positioned in the Xq28 region and organized in a compact head-to-head manner with the isocitrate dehydrogenase 3 (NAD+) gamma gene. Both genes are motivated by a CpG-embedded bidirectional promoter.

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

EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

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.

TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.