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SAR1B is a small GTPase that functions as a homodimer. GTP-Binding Protein SAR1B (SAR1b) is involved in transport from the endoplasmic reticulum to the Golgi apparatus and also in the selection of the protein cargo and the assembly of the COPII coat complex. The SAR1B protein is activated by the guanine nucleotide exchange factor PREB. SAR1B gene defects are a cause of chylomicron retention disease (CMRD), also known as Anderson disease (ANDD).

Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.

Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and aid in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) comprised of a small 28S subunit and a large 39S subunit. Among different species, the proteins comprising the mitoribosome vary greatly in sequence, and sometimes in biochemical properties, thus preventing simple recognition by sequence homology. Mitochondrial Ribosomal Protein L2 (MRPL2) is a 39S subunit protein which is a member of the EcoL2 ribosomal protein family.

Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

NAP1L1 is a member of the nucleosome assembly protein (NAP) family. NAP1L1 protein plays a part in DNA replication, modulating chromatin formation and regulation of cell proliferation.

Heat Shock Factor Binding Protein 1-Like 1 (HSBP1L1) is a part of a family of eukaryotic proteins known as nucleotide exchange factors for HSP 70. HSBP1L1 is a protein coding gene whose expression is regulated mainly at the transcription level.

Surfactant pulmonary-associated protein D (SFTPD) belongs to the collectin family of C-type lectins, which is synthesized in many tissues including respiratory epithelial cells in the lung, and contains one C-type lectin domain and one collagen-like domain. SFTPD has humoral molecules of the innate immune system, and is deemed a functional candidate in chronic periodontitis. Moreover, SFTPD is involved in the development of acute and chronic inflammation of the lung. A number of human lung diseases are characterized by decreased levels of bronchoalveolar SFTPD. SFTPD contributes to the lungs defense against inhaled microorganisms, organic antigens and toxins. SFTPD interacts with complexes such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. In addition, SFTPD participates in the extracellular reorganization or turnover of pulmonary surfactant. SFTPD binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.

DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.
DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques.

ASB13 belongs to the ankyrin repeat and SOCS box-containing (ASB) family of proteins which contains ankyrin repeat sequence and a SOCS box domain. ASB13 is a protein coding gene that plays a role as a substrate-recognition part of a SCF-like ECS E3 ubiquitin-protein ligase complex which arbitrates the ubiquitination and subsequent proteasomal degradation of target proteins.

A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.

IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

B-Raf Proto-Oncogene, also known as BRAF is a member of the raf/mil family of serine/threonine protein kinases. BRAF participates in regulating the MAP kinase/ERKs signaling pathway, which eventually have an effect on cell division, differentiation, and secretion. Mutations in BRAF have been associated with cardiofaciocutaneous syndrome, which is a disease characterized by heart defects, mental retardation and a distinctive facial appearance. In addition, mutations in BRAF have also been associated with different cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, as well as adenocarcinoma of lung.

CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.

TRAF2 protein is related with transduce signals from members of the TNFR superfamily. TRAF2 is located in the cytoplasm binds to TRAF1, TRAF2, or TRAF3, thus inhibiting TRAF function by sequestering the TRAFs in a suppressed state in the cytoplasm. Overexpression of TANK inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and inhibits LMP1-mediated NF-kappa-B activation by blocking the association of TRAF2 with LMP1. TRAF2 is necessary for the cellular response to TNF-alpha by connecting upstream signalling molecules to the IKKs and p65.

Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

Filamin is a large (270kd) dimeric actin crosslinking protein from a variety of sources, which helps to stabilize the 3D cortical actin network. The fundamental structure of filamin is well conserved and consists of an actin binding domain at the N-terminus followed by a C-terminal rod domain consisting of numerous repeat segments ranging from 4 in C. elegans to 24 in mammalian cells. Each repeat in the rod domain consists of roughly 100 residues and forms an immunoglobulin like fold. Such immunoglobulin folds have been found in a variety of proteins and are responsible for protein-protein interactions. Filamin Human actin-binding protein (ABP), aka filamin, crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Mammalian filamin interacts directly with at least 30 proteins such as transmembrane receptors, second messenger-associated proteins, protein kinases, phosphatases and cytoskeletal proteins and these interactions have been shown to require one or more of the repeat elements in the rod domain.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

TSTA3 is a NADP(H)-binding protein. TSTA3 catalyzes the two-step epimerase and the reductase reactions in GDP-D-mannose metabolism, converting GDP-4-keto-6-D-deoxymannose to GDP-L-fucose. GDP-L-fucose is the substrate of numerous fucosyltransferases that take part in the expression of several glycoconjugates, including blood group ABH antigens and developmental adhesion antigens.
Mutations in TSTA3 result in leukocyte adhesion deficiency, type II.

GRB2 is widely expressed and binds the EGFR and contains one SH2 domain and two SH3 domains which form a complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. GRB2 is related to the Sem5 gene of C.elegans, which is takes part in the signal transduction pathway. GRB2 is an adaptor protein that provides an important link between cell surface growth factor receptors and the Ras signaling pathway. Inhibition of GRB2 activity damages developmental processes in a variety of organisms and blocks transformation and proliferation of different cell types.

Colipase (CLPS) is a protein co-enzyme essential for optimal enzyme activity of pancreatic lipase. CLPS is secreted by the pancreas as an inactive form, procolipase, which is then activated in the intestinal lumen by trypsin. CLPS prevents the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. CLPS allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. CLPS binds to the C-terminal, non-catalytic domain of lipase, thus stabilizing an active conformation and significantly increasing the whole hydrophobic binding site.

Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

Purine-Rich Element Binding Protein B (PURB) is a single-stranded DNA-binding protein which takes part in the dendritic transport of a subset of mRNAs. PURB operates as repressor in myoblasts and fibroblasts in the control of vascular smooth muscle alpha-actin gene transcription. PURB binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in various eukaryotes from yeasts through humans.

Granzyme-B (GZMB) is essential for target cell lysis in cell-mediated immune responses. GZMB is related to an activation cascade of caspases responsible for apoptosis execution. GZMB cuts caspase-3, -7, -9 and 10 to activate enzymes mediating apoptosis.