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Four And A Half LIM Domains 2 (FHL2) belongs to the four-and-a-half-LIM-only protein family. Family members are comprised of 2 highly conserved, tandemly arranged, zinc finger domains with 4 highly conserved cysteines binding a zinc atom in each zinc finger. The FHL2 protein is assumed to play a part in the assembly of extracellular membranes. Furthermore, FHL2 is down-regulated during transformation of normal myoblasts to rhabdomyosarcoma cells and the FHL2 functions as a link between presenilin-2 and an intracellular signaling pathway.

SARS Coronavirus is an enveloped virus containing 3 outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein takes part in virus infection cycle and is the primary target of neutralizing antibodies.

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.

SARS Coronavirus is an enveloped virus containing 3 outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein takes part in virus infection cycle and is the primary target of neutralizing antibodies.

Methyl-CpG-binding domain protein 3 (MBD3), belongs to the MBD family of transcriptional repressors. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 includes a family of nuclear proteins related by the presence of a methyl-CpG binding domain (MBD) in each protein. Nevertheless, not like the other family members, MBD3 is not capable of binding to methylated DNA. MBD3 is a subunit of the NuRD, a multisubunit complex having nucleosome remodeling and histone deacetylase activities. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.

WDR5, also designated BMP-2-induced gene 3 kb or BIG-3, belongs to the family of WD-40 repeat proteins, and is essential for vertebrate development, Hox gene activation and global H3K4 trimethylation. This protein is expressed in osteoblasts, chondrocytes, osteocytes and marrow stromal cells. WDR5 may play a role in its function of accelerating osteoblast differentiation.

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.

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.

Zinc Binding Alcohol Dehydrogenase Domain Containing 2, also known as ZADH2, is a protein coding gene which is a part of the zinc-containing alcohol dehydrogenase family.

Iron-sulfur cluster assembly enzyme (ISCU) belongs to the nifU family. Iron-sulfur (Fe-S) clusters are required for several mitochondrial enzymes and other subcellular compartment proteins. ISCU interacts with ISCS (a cysteine desulfurase) to sequester inorganic sulfur for Fe-S cluster assembly. The ISCU-ISCS protein complex localizes in both mitochondria and cytosol, implying that Fe-S cluster assembly occurs in multiple subcellular compartments in mammalian cells.

Charged Multivesicular Body Protein 5 (CHMP5) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins comprise the ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and development of endocytic multivesicular bodies (MVBs). Certain CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP the CHMP1A, is essential for both MVB formation and regulation of cell cycle progression.

TMED10, which has a GOLD domain, belongs to the EMP24/GP25L/p24 family. TMED10, a type I membrane protein is restricted to the plasma membrane and golgi cisternae and takes part in vesicular protein transferring. Additionally, TMED10 is a fragment of the heteromeric secretase complex and controls the complex's gamma- secretase activity without influencing its epsilon-secretase activity. Alterations in TMED10 are linked to early-onset familial Alzheimer's disease. TMED10 has a pseudogene on chromosome 8.

GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.

Nedd4 Family Interacting Protein 1 (NDFIP1) is a part of a small group of evolutionarily conserved proteins having 3 ransmembrane domains. NDFIP1 is a possible target for ubiquitination by the Nedd4 family of proteins. NDFIP, which is a member of a family of integral Golgi membrane proteins, also modulates EGFR signaling through multiple pathways.

Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome.

GLOD4 is a part of the glyoxalase system which is a group of enzymes that is in charge of the detoxification of methylglyoxal and other reactive aldehydes that are usually produced in metabolism. The mitochondrial protein GLOD4 is known to interact with NUDT9.

CD209 (a member of the C-typelectin family) is Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) andtakes part in initiation of primary immune response.CD209has a high affinity for theICAM3 molecule and binds various microorganisms by recognizing high-mannose-containing glycoproteins ontheir envelopes and especially functions as receptor for several viruses such as HIV and Hepatitis C. Along with other C-typelectins, CD209is involved in recognition of tumors by dendritic cells.CD209also initiatesnatural immunity bymodulating toll-like receptors.

Zinc Finger, AN1-Type Domain 5, also known as ZFAND5 is implicated in protein degradation through the ubiquitin-proteasome system. ZFAND5 performs by anchoring ubiquitinated proteins to the proteasome and takes part in ubiquitin-mediated protein degradation during muscle atrophy. Furthemore, ZFAND5 plays a role in the regulation of NF-kappa-B activation as well as apoptosis. ZFAND5 inhibits NF-kappa-B activation as well as tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation.

Ankyrin Repeat Domain 54 (ANKRD54), which is also known as LIAR contains 4 ANK repeats. ANKRD54 plays a vital role in regulating intracellular signaling events related with erythroid terminal differentiation. ANKRD54 interacts with LYN through ankyrin repeat region and the SH3-domain in an activation-independent status of LYN. ANKRD54 creates a multiprotein complex with LYN and HCLS1.

ZMAT3 is a protein with a nuclear localization signal and 3 zinc finger domains. The mRNA and the protein of this gene are upregulated by wildtype p53. When overexpressed, ZMAT3 can produce tumor cell growth, indicating that ZMAT3 takes part in the p53-dependent growth regulatory pathway. Alternative splicing of ZMAT3 produce two transcript variants encoding two isoforms differing in only one amino acid.

OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.

Epidermal Growth Factor­like Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7, also known as CHCHD7 is a newly recognized member of a multifamily of proteins which contains a conserved (coiled coil 1)-(helix 1)-(coiled coil 2)-(helix 2) domain. The biological function of CHCHD7 is unknown and the gene has up till now not been connected with neoplasia. In addition, CHCHD7 & PLAG1 are located head-to-head about 500 bp apart in 8q12. Molecular analyses of twenty seven tumors exposed CHCHD7-PLAG1 fusions in three tumors, two of them had t(6;8) and t(8;15) translocations as a singular anomalies and one a normal karyotype.

NMRAL1 is a redox sensor protein which goes through reformation and subcellular rearrangement in reaction to alterations in intracellular NADPH/NADP+ levels. When the NADPH concentration is low the protein is found mostly as a monomer, and binds argininosuccinate synthase (ASS1), which takes part in nitric oxide synthesis. Association with ASS1 defects NMRAL1 activity and diminishes the production of nitric oxide, which then inhibits apoptosis. When the NADPH concentration is normal , the protein is found as a dimer and hides the binding site for ASS1.