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NCK1 is an adapter protein which binds with tyrosine-phosphorylated growth factor receptors or their cellular substrates. NCK1 maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. NCK1 is involved in the DNA damage response, for efficient activation of downstream effectors, such as that of CHEK2. NCK1 is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. NCK1 is located in the cytoplasm and is an adaptor protein that participates in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.

Semaphorin-4D (CD100) is a member of the semaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domain. CD100 is the cell surface receptor forPLXN1B and PLXNB2 which plays a central role in cell-cell signaling. CD100 stimulates the migration of cerebellar granule cells and of endothelial cells, regulates dendrite and axon branching and morphogenesis. In addition, CD100 has a role in the immune system; it promotes signaling via SRC and PTK2B/PYK2, which subsequently mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.

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.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells. The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes. The KIR proteins are categorized by the number of

TBC1 domain family member 22B, also known as TBC1D22B acts as a GTPase-activating protein for Rab family protein. The Tre-2/Bub2/Cdc16 (TBC) domain is a conserved protein motif which consists of roughly 200 amino acids and functions as a specific Rab-GAP domain. The TBC domain has more than 40 distinct TBC domain-containing proteins which have been identified in humans.

Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

TMEFF1 is a type I transmembrane glycoprotein which includes 2 follistatin modules and an EGF domain in its extracellular domain, a transmembrane domain and a short cytoplasmic tail. The extracellular domain of TMEFF1 can be released as a soluble protein. TMEFF1 is primarily expressed in brain, but is downregulated in brain neoplasms. TMEFF1 selectively regulates nodal but not activin signaling through direct binding to the nodal co-receptor, Cripto. TMEFF inhibits NODAL and BMP signaling through neural patterning and also a possible tumor suppressor in brain cancers.

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.

CUB Domain Containing Protein 1, also known as CDCP1 is a transmembrane protein which contains three extracellular CUB domains. CDCP1 is implicated in cell adhesion and cell matrix association. In addition, CDCP1 takes part in the regulation of anchorage versus migration or proliferation versus differentiation through its phosphorylation. CDCP1 is also a novel marker for leukemia diagnosis as well as for immature hematopoietic stem cell subsets. Furthermore, the extracellular region of human CDCP1 shares amino acid identity sequence with the mouse CDCP1.

ACOT11 belongs to the acyl-CoA thioesterase family which catalyses the transformation of activated fatty acids to the equivalent non-esterified fatty acid and coenzyme A. Expression of a mouse homolog in brown adipose tissue is induced by low temperatures and inhibited by high temperatures. Obesity-resistant mice demonstrated High levels of expression compared with obesity-prone mice, indicating BFIT takes part in acyl-CoA thioesterase 11 in obesity. BFIT has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.

PTB domain-containing engulfment adapter protein 1 (GULP1) is an evolutionarily conserved adaptor protein essential for efficient phagocytosis of apoptotic cells by phagocytes. Furthermore, GULP1 helps modulate cellular glycosphingolipid and cholesterol transport. In addition, GULP1 may have a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increased cytoplasmic levels of GULP1 are linked with increases in cellular levels of GTP-bound ARF6.

CRADD is a 22kDa, widely-expressed cytosolic adaptor/signaling protein that induces cell apoptosis/cell death in numerous tissues. CRADD is a death domain (CARD) that recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes TNFR1A, RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.

Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.

Binding immunoglobulin protein (BiP or HSPA5) is a member of the family of ~70kDa heat shock proteins (HSP 70). HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis.

Killer Cell Lectin-like Receptor Subfamily G, Member 1 (KLRG1) is a member of the killer cell lectin-like receptor (KLR) family, which is a group of transmembrane proteins preferentially expressed in NK cells. Natural killer (NK) cells are lymphocytes which mediate lysis of certain tumor cells and virus-infected cells without previous activation. NK cells can also regulate specific humoral and cell-mediated immunity. The cell surface expression of KLRG1 is up-regulated by MHC class I molecules expression.

CD207 (C-type lectin domain family 4 member K) is expressed in Langerhans cells which are immature dendritic cells of the epidermis and mucosa. Moreover, CD207 is expressed in several other dendritic cell types including dermal CD103+ DCs and splenic CD8+ DCs. Langerin is localized in the Birbeck granules, the organelles present in the cytoplasm of Langerhans cells and comprised of superimposed and zippered membranes. CD207 is a C-type lectin with mannose binding specificity, and it has been suggested that mannose binding by the CD207 protein leads to internalization of antigen into Birbeck granules thus providing access to a nonclassical antigen-processing pathway.

Human Factor IX also called Christmas-Factor is a glycoprotein, which is synthesized in the liver and belongs to the serine proteases system and is part of the S1 peptidase family.
Lack of Factor-IX causes Hemophilia-B meaning Christmas Disease. Factor-IX has a N-terminus region which contains 12xGla residues which asist the calcium dpendant binding of Factor-IX to the phospholipid surface. Factor-IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage yields the intermediate IXa, which is subsequently converted to the fully active form IXab.
Factor-IX binds initially to exosites on the factor XIa heavy chain, followed by interaction at the active site with subsequent bond cleavage. Coagulation factor IX is activated by interaction with the erythrocyte membrane, causing intrinsic coagulation. Chaperones & lectins act simultaniously to guarantee the proper folding of Factor-IX and the retention of mutant molecules. Human Factor IX, activated by either the Contact or Tissue Factor Pathway, is responsible for the activation of Factor X to Xa.

Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal and breast cyst fluids. It is identical in amino acid sequence to tumor-derived lipid mobilizing factor (LMF), a protein associated with the dramatic loss of adipose body stores in cancer cachexia, and has been shown to stimulate lipolysis by adipocytes in vivo and in vitro. A role for ZAG has been proposed in the regulation of body weight, and age-dependent changes in genetically influenced obesity, and also it regulates melanin production by normal and malignant melanocytes. It has also recently been classified as a novel adipokine in that it is produced by both white and brown fat adipocytes and may act in a local autocrine fashion in the reduction of adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexiainducing conditions, and its possible normal role in body fat store homeostasis is deserving of understanding in its own right. ZAG exhibits a class I major histocompatibility complex (MHC) fold but is a soluble protein rather than being anchored to plasma membranes and does not associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG has an open apical groove, and X-ray crystallography of human derived ZAG revealed an unidentifiable electron density in a similar position to that occupied by antigenic peptides in classical MHC proteins and glycolipids in isoforms of CD1. This presumptive ligand is not a peptide, and the groove is too small to hold a glycolipid such as is presented by CD1 isoforms. By analogy with all other MHC class I-related proteins that have an open apical groove [some do not ], occupancy by a ligand is probably crucial to ZAG's biological function. Despite all of the structural and biochemical evidence that ZAG binds a ligand, none has so far been found by extraction from protein isolated from biological fluids. This difficulty could be because the ligand is labile, heterogeneous, or readily lost during purification procedures. Knowing more about how ZAG interacts with the compounds it has been found to bind, both natural and artificial, will inform searches for the elusive ligand(s) and its/their role in ZAG's signaling function.

Grancalcin is calcium-binding protein which is particularly abundant in human neutrophils. GCA is a member of the penta EF-hand (PEF) subfamily of EF-hand proteins, who also comprises calpain, sorcin, peflin, and ALG-2. GCA undergoes essential conformational changes upon binding of calcium, which subsequently exposes hydrophobic amino acid residues, that direct the protein to hydrophobic surfaces. GCA cooperates with L-plastin, a protein known to have actin bundling activity, which suggests that GCA has a part in the regulation of neutrophils adhesion.

Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.