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GOLGA7 is part of the ERF4 family. This protein is involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. GOLGA7 is palmitoylated on Cys-69 and Cys-72; that is required for Golgi localization and interaction with GOLGA3.

YWHAZ accession number NP_ 663723 belongs to the 14-3-3 family of proteins which are in charge for checkpoint control, apoptotic & nutrient sensing pathways as well as signal transduction by binding to phosphoserine-containing proteins. The 14-3-3 protein family is found in both plants and mammals, and KCIP-1 protein is 99% identical to the mouse, rat and sheep orthologs. KCIP-1 interacts with IRS1 protein, signifying a role in regulating insulin. 14-3-3 proteins are highly conserved and ubiquitously expressed. YWHAZ function as an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAZ binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

Bivalirudin directly inhibits thrombin by specifically binding as well to the catalytic site and to the anion-binding exosite of circulating and clot-bound thrombin. Bivalirudin is a specific and reversible direct thrombin inhibitor.
Thrombin, which is a serine protease, plays a central role in the thrombotic process; it cleaves fibrinogen into fibrin monomers and activates Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked structure which stabilizes the thrombus. Thrombin also activates Factors V and VIII, which promotes further thrombin generation, activates platelets, stimulating aggregation and granule release.

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Alveolar Soft Part Sarcoma Chromosome Region, Candidate 1 (ASPSCR1) contains a UBX domain and interacts with glucose transporter type 4 (GLUT4). ASPSCR1 is a tether, which sequesters the GLUT4 in intracellular vesicles in muscle and fat cells, and redistributes the GLUT4 to the plasma membrane. Translocation t(X;17)(p11;q25) of this ASPSCR1 with transcription factor TFE3 gene ends with a ASPSCR1-TFE3 fusion protein in alveolar soft part sarcoma and in renal cell carcinomas.

Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.

PPP1CC is vital for cell division and takes part in the regulation of protein synthesis, muscle contractility and glycogen metabolism. Additionally, PPP1CC has a role in long-term synaptic plasticity and regulation of ionic conductance, and has a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.

HLH (helix-loop-helix) proteins are a putative transcription factors family. Several HLH proteins take part in growth and development of an extensive range of tissues and species. NHLH1 functions as a DNA-binding protein and has a role in the regulation of cell-type determination in the developing nervous system.

Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.

DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

IFN-Induced Protein With Tetratricopeptide Repeats 3, also known as IFIT3 is a member of the IFIT family. IFN-induced antiviral protein which performs as an inhibitor of cellular and viral processes, cell migration, proliferation, signaling, as well as viral replication. Furthermore, IFIT3 is significantly induced upon RNA virus infection. Ectopic expression or alternatively knockdown of IFIT3 might, respectively, enhance or impair IRF3-mediated gene expression.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.

Protein modification with ubiquitin is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1) belongs to the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins. UE2G1 protein is involved in degradation of muscle-specific proteins.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

Intercellular Adhesion Molecule-5 or ICAM-5 is a glycoprotein, part of the immunoglobulin family and located in the cell membrane. We can find ICAM-5 in telencephalic neurons, in a couple of adhesion activity, firstly heterophilic binding amid neurons and leukocytes and secondly, homophilic binding amid neurons. ICAM-5 is expressed exclusively in telencephalic areas of the central nervous system. Similar to other ICAMs molecules, ICAM-5 adhere to LFA-1 which is a leukocyte integrin.

NTRK2 plays a role in the growth and the development of the central and the peripheral nervous systems using the regulation of neuron proliferation, migration, survival, differentiation, and synapse production. NTRK2 is a receptor for B-DNF and NT4. NTRK2 binds to neurotrophin-3 which regulates neuron survival through NTRK2. NTRK-2 activates numerous effectors such as SHC-1, SH2B-1, PLCG-1 and SH2B-2 that control overlapping signaling cascades.

Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

BPI encodes a lipopolysaccharide binding protein. BPI is related to human neutrophil granules and has bactericidal activity on gram-negative organisms.

CCDC101 is known as a subunit of the SAGA (Spt-Ada-Gcn5 acetyltransferase) histone acetyltransferase complex in Saccharomyces cerevisiae. CCDC101 is conserved from yeast to humans.