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SH3-Domain GRB2-Like 3, also known as SH3GL3, is a part of the endophilin family. SH3GL3 contains 1 BAR domain and 1 SH3 domain and takes part in endocytosis. SH3GL3 is a protein coding gene which drafts proteins with high curvature to membranes.

Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.

ATOX1 is a metal transport protein that is part of the ATX1 family. ATOX1 is a copper chaperone that takes part in cellular antioxidant defense and can bind and deliver cytosolic copper to the copper ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. ATOX1 plays a role as an antioxidant against superoxide and hydrogen peroxide, and consequently, takes an important part in cancer carcinogenesis. Because of ATOX1 cytogenetic location, the gene can be a good a candidate gene for 5q-syndrome.

Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

Programmed cell death 1 ligand 2 (PDCD1LG2) which takes part in the costimulatory signal, is necessary for T-cell proliferation. PDCD1LG2 is also involved in IFNG production in a PDCD1-independent way. The interaction with PDCD1 inhibits T-cell proliferation by preventing cytokine production and cell cycle progression.

TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

Calbindins are Ca-binding proteins belonging to the troponin C superfamily. CALB28K/Calbindin1/CALB1 (D28K/Spot35 protein or cholecalcin, rat 261 aa; mouse 261 aa; human 261-aa, chromosome 8q21.3-q22.1) was originally described as 27-kDA induced by vitamin D in the duodenum of chicken. In mammals, it is expressed in the kidney, pancreatic islets, and brain. In brain, its synthesis is independent of vitamin D. CABP28K contains 4 active and 2 inactive EF-hand Ca-binding domains. The gene for CABP28K is clustered in the same region as carbonic anhydrase. The neurons in the brains of patients with Huntington disease are CAB28K depleted. There are two types of CaBPs: the "trigger"- and the "buffer"-CaBPs. The conformation of "trigger" type CaBPs changes upon Ca2+ binding and exposes regions on protein that interact with target molecules, thus altering their activity. The buffer-type CABP are thought to control the intracellular calcium concentration. Calbindin D-28K is found predominantly in subpopulations of central and peripheral nervous system neurons, and in certain epithelial cells involved in Ca2+ transport such as distal tubular cells and cortical collecting tubules of the kidney, and in enteric neuroendocrine cells.

Cell Cycle Exit And Neuronal Differentiation 1, also known as CEND1, is a neuron-specific protein. CEND1 take part in cell cycle control and neuronal differentiation mechanisms during neonatal SVZ neurogenesis and turn out to be crucial for the transition from neuroblasts to mature neurons when reaching high levels. The similar protein in pig enhances neuroblastoma cell differentiation in vitro and involved in neuronal differentiation in vivo. Multiple pseudogenes have been reported for this gene. The disease neuroblastoma has been associated with CEND1.

Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).

Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.

Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.

Diphthamide biosynthesis protein 2 (DPH2) is a homodimer and each of its monomers can bind a [4Fe-4S] cluster. DPH2 is the target of ADP ribosylating diphtheria toxin (DT) and Pseudomonas exotoxin A (PE). DPH2 was identified by its ability to complement a diphthamide mutant strain, and thus serves in diphthamide biosynthesis. The loss of DPH2 pre-activates NF-kB and death receptor pathways and renders MCF7 cells hypersensitive to tumor necrosis factor.

Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

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.

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.

ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.

The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

CRABP1 is a member of special carrier proteins for members of the vitamin A family. It is believed that CRABP1 has an essential role in retinoic acid-mediated differentiation and proliferation processes. Though, CRABP1 is structurally similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. CRABP1 is constitutively expressed and is thought to have different functions in the cell than the related CRABP2. CRABP1 forms a beta-barrel structure which accommodates hydrophobic ligands in its interior. Loss of CRABP1 function as a result of hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma. Furthermore, frequent methylation-associated silencing of CRABP1 is linked to esophageal squamous-cell carcinoma.

4-1BBR is a member of the TNF-receptor superfamily. 4-1BB receptor contributes to the clonal expansion, survival, and development of T cells.4-1BBRcan also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.

EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase (EOGT) takes part in the regulation of Notch receptor. EOGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine/ threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). EOGT mainly glycosylates the Thr residue positioned between the fifth and sixth conserved cysteines of folded EGF-like domains.