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Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.

CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

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.

VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.

43 kDa receptor-associated protein of the synapse (RAPSN), is expressed in the postsynaptic membrane of skeletal muscle. RAPSN is essential for the clustering of nicotinic acetylcholine receptors (nAChR). In addition RAPSN self-associates via at least two of its seven tetra-tricopeptide repeats (TPRs). RAPSN interacts with the large intracellular domain of the nAChR a subunit all the way through the hydrophobic surface of the coiled-coil domain. RAPSN modifies trafficking of AChR within the cell. Overexpression inhibits agrin-induced AChR clustering pathway. RAPSN also plays a role in postsynaptic congenital myasthenic syndromes.

Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid

EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.

TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.

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.
On November 2021, WHO designated a variant of concern, named Omicron. Omicron has several mutations that may have an impact on how it behaves (how easily it spreads, the severity of illness).

AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokinen family that is also called inducible T-cell alpha chemoattractant (I-TAC) and (IP-9). I-TAC is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells. The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.

EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three qu

Alpha-2-antiplasmin (SERPINF2) is a serine protease inhibitor. The main targets of SERPINF2 are plasmin and trypsin; however SERPINF2 also inactivates matriptase-3/TMPRSS7 and chymotrypsin.

Non-metastatic cells 1 or NME1 is a protein, found at first as a suppressor gene for candidate metastasis. The protein can be found in various types of tumor, potential of metastatic may increase or decrease as the protein’s levels changes. When the protein’s concentration is low, an aggressive carcinoma (colon, breast, gastric and melanoma) appears. High levels of NME1 have been linked to advanced thyroid cancer.

OAZ1 is a member of the ODC antizyme family. OAZ1 is auto-regulated expressed by polyamine-enhanced translational frame shifting. OAZ1 negatively controls polyamine synthesis by increasing the negative feedback loop regulating ornithine decarboxylase (ODC) activity. The OAZ1 protein inhibits ornithine decarboxylase and speeds up its detraction.

EPH Receptor A2 (EPHA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPHA2 is a protein which binds ephrin-A ligands. EPH and EPH-related receptors are associated with mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily normally have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. EPHA2 gene mutations are the cause of certain genetically-related cataract disorders.

FAS or tumor necrosis factor receptor superfamily member 6 or TNFRSF6, is part of the death receptor family, which is part of the TNF receptor protein family. TNFRSF6 has a crucial part in regulating viral infections. FAS protein can be found in almost all cell types, when its cognate ligand (FasL) can be found in activated T cells, NK cells & dendritic cells. The regulating protein of FasL & TRAIL on HCMV-infected dendritic enhances direct destruction of activated T lymphocytes. furthermore, subvertneutrophil function in HCMV retinitis can occur when FasL is activated in HCMV infected retinal pigment epithelial cells.

TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.

Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belongs to the CC chemokine family which is also known as monocyte chemotactic protein-1 (MCP-1). MCP 1 is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts. CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. MCP 1is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.