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Profilin-1 also known as Pfn1 is a ubiquitous actin monomer-binding protein which is a member of the profilin family. Pfn1 significantly enhances skin wound healing in-vitro as well as in-vivo which is mediated by purinergic receptors. Furthermore, Pfn1 is also active in endothelial cell migration and vessel sprouting. Pfn1 is considered to regulate actin polymerization in response to extracellular signals.

FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.

The SARS Nucleocaspid is a protein that has a crucial structural importance, by making the virions associates with the RNA genome and therefore create a nucleocapsid that has the specific helical form. There has been found 3 different domain structures to the nucleocapsid antigen. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins.

Integrins are heterodimeric integral membrane proteins consisting of an ? chain and a ? chain. CD11b is an I-domain including ? integrin combines with the ? 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as macrophage receptor also called MAC1. The ? M beta 2 integrin is crucial in the adherence of neutrophils and monocytes to stimulated endothelium, and also in the phagocytosis of complement coated particles. Multiple transcript variants encoding different isoforms have been found for this gene.

CD48, is a GPI-linked protein which belongs to the CD2 family of immunoglobulin superfamily molecules. CD48 is capable to transduce signals and can likewise trigger signaling through CD2 or 2B4. CD48 to CD2 interactions advocate T cell activation and class replacing to IgG2a in B cells. In addition, high affinity of CD48 to 2B4, interactions may either promote or inhibit NK cell as well as cytotoxic T cell (CTL) activation. CD48 does not contain a transmembrane domain, though it is held at the cell surface by a GPI anchor through a C-terminal domain which possibly split to produce a soluble form of the receptor.

YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

RND3 is a small GTPase which is part of the Ras superfamily that controls the association of the actin cytoskeleton in reaction to extracellular growth factors. RND3 activity causes a decrease in stress fibers and an increase in cell migration, at least in part through regulation of the Rho-dependent kinase ROCK1. RND3 inhibits DNA-damage induced apoptosis and cell cycle arrest. RND3 binds GTP and is resistant to Rho-specific GTPase-activating proteins.

Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described.
Protein phosphatase 2C(PP2C?) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.

PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. Inhibition of PPP1R14A results to increased myosin phosphorylation and enhances smooth muscle contraction in the absence of increased intracellular Ca(2+) concentration. Myosin phosphatase can reverse MYL (myosin light chain) phosphorylation to induce a state of relaxation. However, during agonist-induced contraction at constant Ca2+ concurrent inhibition of myosin phosphatase leads to increases in MYL phosphorylation and tension. These calcium-independent increases in myosin phosphorylation and tension are termed calcium sensitization. Human pregnancy is characterized by the increases of PKN1 expression and CPI-17 phosphorylation in the myometrium. PPP1R14A is mapped to chromosome 19q13.13-q13.2. PPP1R14A binds directly to protein kinase C and casein kinase I. PPP1R14A siRNA decreased the level of merlin phosphorylation and consequently Ras and ERK activity in human tumor cell lines. PKC/CPI-17 medi

The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

Lymphocyte Antigen 9, also known as LY9 is a member of the SLAM family of immunomodulatory receptors, LY9 interacts with the adaptor molecule SAP . LY9 plays a part in adhesion reactions between T lymphocytes and accessory cells via homophilic interaction. LY9 promotes T-cell differentiation into a helper T-cell Th17 phenotype which leads to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Furthermore it also promotes recruitment of RORC to the IL-17 promoter. LY9 is implicated in the maintenance of peripheral cell tolerance through serving as a negative regulator of the immune response. LY9 disables autoantibody responses as well as inhibits IFN-gamma secretion by CD4(+) T-cells. Moreover, LY9 negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Systemic Lupus Erythematosus is one of the diseases which are associated with LY9.

ULBP1 together with at least ULBP2 and ULBP3, is ligand for the NKG2D receptor. ULBPs stimulate various signaling pathways in primary NK cells, which result in cytokines and chemokines production. In CMV infected cells, ULBP1 cooperates with soluble CMV glycoprotein UL16 to inhibit the interaction with the NKG2D receptor providing a mechanism by which CMV infected cells escape the immune system. Additionally, UL16 retains ULBP1 to the ER and cis-Golgi apparatus to prevent it from reaching cell surface.

RAB1A belongs to the ras-related superfamily. Rab proteins have a central part in either in endocytosis or in biosynthetic protein transport. Rab1a protein controls vesicle traffic from the endoplasmic reticulum to the Golgi apparatus.

Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria In addition to its chemotactic and angiogenic property.

CD21 is expressed strongly on mature B cells, follicular dentritic cells and weakly on immature thymocytes and T lymphocytes. In B-cell ontogeny, CD21 appears after the pre-B-stage, is maintained during peripheral B-cell development and is lost upon terminal differentiation into plasma cells. CD21 expression is also gradually lost after stimulation of B cells in vitro. CD21 functions as receptor for C3d, C3dg and iC3b Complement components, for EBV and for IFNalpha. CD21 binds to CD23 and associates with CD19, CD81 and Leu13 to form a large signal-transduction complex involved in B cell activation.

CD320 is a part of the low-density lipoprotein receptor family, having 2 low-density lipoprotein receptor type A domains divided by a complement-like cysteine-rich region. CD320 participates in cobalamin uptake and internalizes the complex by endocytosis. CD320 is also plays a role as costimulator to promote B cell and follicular dendritic cells responses. CD320 is also known to augment the proliferation of PC precursors generated by IL-10.

ILK1 (Integrin-linked kinase) is a serine/threonine protein kinase, containing 4 ankyrin-like repeats. ILK1 regulates a number of biological properties which include: anchorage-independent cell cycle progression, tumor cell invasion and apoptosis. ILK1 can also be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Furthermore, ILK1 phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
ILK1 interacts with the cytoplasmic domains of integrin ?1 and ?3 subunits in addition to several adaptors and signaling proteins, it also acts as a proximal receptor kinase regulating integrin-mediated signal transduction. ILK1 is a focal adhesion protein part of the complex ILK-PINCH. This complex is deemed to be one of the convergence points of integrin- and growth factor-signaling pathway. ILK1 is stimulated rapidly but briefly by both cell fibronectin interactions in a PI3-K-dependent manner, probably through the binding of PtdIns(3,4,5)P3 with a PH-like domain of ILK.
ILK1 over-expression has been documented in a wide variety of human malignancies.

BTF3L4 is a part of the NAC-beta family which contains 1 NAC-A/B (NAC-alpha/beta) domain and required for the initiation of transcription. BTF3L4 binds to polypeptide chains as they emerge from the ribosome and prevents their interaction with the SRP, which usually targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor which forms a stable complex with RNA polymerase II.

Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.

TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.

MAP2K1 is a member of the dual specificity protein kinase family, which plays a role as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, are recognized as extracellular signal-regulated kinases (ERKs), that act as an integration position for multiple biochemical signals. MEK1 is located upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As a key player of MAP kinase signal transduction pathway, MEK1 is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. MAP2K1 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a thr-glu-tyr sequence located in map kinases. MEK1 activates erk1 and erk2 map kinases.

PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. Inhibition of PPP1R14A results to increased myosin phosphorylation and enhances smooth muscle contraction in the absence of increased intracellular Ca(2+) concentration. Myosin phosphatase can reverse MYL (myosin light chain) phosphorylation to induce a state of relaxation. However, during agonist-induced contraction at constant Ca2+ concurrent inhibition of myosin phosphatase leads to increases in MYL phosphorylation and tension. These calcium-independent increases in myosin phosphorylation and tension are termed calcium sensitization.
Human pregnancy is characterized by the increases of PKN1 expression and CPI-17 phosphorylation in the myometrium. PPP1R14A is mapped to chromosome 19q13.13-q13.2.
PPP1R14A binds directly to protein kinase C and casein kinase I.
PPP1R14A siRNA decreased the level of merlin phosphorylation and consequently Ras and ERK activity in human tumor cell lines.
PKC/CPI-17 mediated pathway in histamine, triggeres cytoskeletal rearrangements causing lung microvascular barrier compromise.

Ras-related protein Rab-6B (RAB6B) is a member of the Rab6 family of the small GTPase superfamily. The Rab6 subfamily consists of 3 different isoforms: Rab6A, Rab6A' and Rab6B. Both Rab6A and Rab6A' are ubiquitously expressed while Rab6B is mainly expressed in brain. Rab6 is a main regulator in the retrograde transfer from endosomes via the Golgi to the ER and may act in retrograde tansport in neuronal cells.

Ras-related protein Rap-2b (RAP2B) is a part of RAS-related genes family. RAP2B has a threonine residue at aa 61Unlike normal ras proteins which have a nontransforming glutamine residue at that position. The threonine residue makes the intrinsic GTPase activity for Rap2B lower, by this means allows RAP2B to exist in the activated state for a longer period of time than normal ras proteins. RAP2B is a platelet protein which is activated by thrombin and involved in platelet activation. RAP2B may be a candidate oncogene which takes part in carcinogenesis through activation of NF-kappaB pathway.