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Vesicle-Associated Membrane Protein 7 (VAMP7) is a member of the synaptobrevin family. VAMP7 is a transmembrane protein, which is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family. VAMP7 is involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. VAMP7 localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. VAMP7 is essential for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. It is also necessary for calcium regulated lysosomal exocytosis. In addition, VAMP7 is involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Furthermore, VAMP7 is needed for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells.

Synovial Sarcoma, X Breakpoint 1 (SSX1) is a member of a family of highly homologous synovial sarcoma X (SSX) breakpoint proteins. SSX proteins are localized to the nucleus and expressed in testis and some types of cancers and, hence, they are classified as C/T (cancer/testis) antigens. These proteins may serve as transcriptional repressors. SSX1 genes are involved in the t (X;18) translocation typically found in all synovial sarcomas. This translocation leads to the fusion of the synovial sarcoma translocation gene on chromosome 18 to one of the SSX genes on chromosome X. These hybrid proteins are most likely responsible for transforming activity.

Endophilin-B2 (SH3GLB2) belongs to the endophilin B subgroup. The endophilins comprise a family of proteins that relates with amphiphysin, synaptojanin and dynamin and are involved in presynaptic vesicle trafficking at nerve terminals.The expression patterns of the endophilins are coherent with their cellular functions at the neuronal synapse. SH3GLB2 is ubiquitously expressed however presents highest levels in brain, adult lung, ovary, and spinal cord.Low levels of SH3GLB2 are found in Down syndrome and reflect brain dysgenesis.

ATPase Transporting, Lysosomal V1 Subunit F (ATP6V1F) is a component of vacuolar ATPase (V-ATPase); it is a multi-subunit enzyme, which mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is required for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is comprised of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain contains 3 A and 3 B subunits, 2 G subunits as well as the C, D, E, F, and H subunits. The V1 domain has the ATP catalytic site. The V0 domain consists of 5 different subunits: a, c, c', c', and d.

GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.

Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.

SARS Associated Coronavirus Spike is a causative agent of SARS virus. Diseases caused by Coronaviruses are usually controlled by CD8 T cells. The spike antigen is one of the main surface proteins on Coronavirus, therefore one of the main proteins that are candidates for vaccines.

Chemokine (C motif) ligand (XCL1) is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose geneis found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.

Sjogren syndrome/scleroderma autoantigen 1, SSSCA1 is involved in mitosis. SSSCA1 is a centromere-associated protein which can induce anti-centromere antibodies. In addition SSSCA1 is recognized by a subset of anti-centromere antibodies from patients with sclerodermaand Sjogren's syndrome.

SRP14 is a ribonucleoprotein complex which mediates the directing of proteins to the endoplasmic reticulum. The “Alu domain” of SRP is comprised of the heterodimer of the SRP9 and SRP14 proteins that are bound to the 5' and 3' terminal sequences of SRP RNA. SRP9/14 binding may be critical to the transcription, maturation, nucleolus localization and transport of SRP RNA.

MOB3B is similar to yeast Mob1 protein which binds Mps1p, a protein kinase vital for spindle pole body duplication and mitotic checkpoint regulation. MOB3B is situated on the opposite strand as the INF kappa precursor (IFNK) gene.

PEA15 (Phospho-enriched protein in astrocytes 15kDa) is a death effector domain (DED)-containing protein mainly expressed in the central nervous system, principally in astrocytes. PEA15 is implicated in the regulation of various cellular processes including apoptosis, proliferation, glucose transport, adhesion and migration. Increased PEA15 levels have an affect tumorigenesis and cancer progression, therefore it is overexpressed in breast cancers and gliomas as well as in type 2 diabetes. PEA15 blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. PEA15 also inhibits RPS6KA3 activities by holding it in the cytoplasm. In addition, PEA15 inhibits both TNFRSF6 and TNFRSF1A mediated CASP8 activity and apoptosis.
PEA15 is ubiquitously expressed. PEA15 is most abundant in tissues such as the heart, brain, muscle and adipose tissue which use glucose as an energy source. Lower PEA15 expression is in glucose-producing tissues. Higher levels of PEA15 expression are found in tissues from individuals with type 2 diabetes than in controls.
PEA15 expression is a significant prognostic marker in ovarian cancer.

CRAHSP1 is a serine phosphoprotein initially identified as a physiological substrate for the Ca2+-calmodulin regulated protein phosphatase calcineurin (PP2B). CRAHSP1 interacts with the STYX/dead phosphate protein in developing spermatids and is a paralog of the brain-specific mRNA-binding protein PIPPIN. It is believed to have a common role in calcium-mediated signal transduction resulting from phosphorylation on serine residues.

Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

ROBLD3 is a member of the GAMAD family. ROBLD3 is an adapter protein which enhances the efficiency of the MAP kinase cascade and facilitates the activation of MAPK2. ROBLD3 compels the recruitment of MP1 to late endosomes where they form a very stable heterodimeric complex required for ERK activation on endosomes. In humans, a mutation in the ROBLD3 gene has been associated with a primary immunodeficiency syndrome, and suggests a role for the ROBLD3 protein in endosomal biogenesis.

Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

Proteasome 26S Subunit, Non-ATPase 13 (PSMD13) is a part of the proteasome subunit S11 family and contains one PCI domain. PSMD13 plays a role as a regulatory subunit of the 26S proteasome which takes part in the ATP-dependent degradation of ubiquitinated proteins.

PSMD9 is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. PSMD9 acts as a chaperone through the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex compilation, PSMD9 is part of an intermediate PSMD9:PSMC6:PSMC3 module, also called modulator trimer complex. PSMD9 is released during the further base assembly process.

HscB Iron-Sulfur Cluster Co-Chaperone (HSCB) is a member of the hscB family and contains 1 J domain. HSCB is expressed in the lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart and localized to mitochondria and cytoplasm. HSCB may function as a co-chaperone in iron-sulfur cluster assembly in mitochondria, it also interacts with ISCU and HSPA9.

Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.

Translocase of Inner Mitochondrial Membrane 8 Homolog A (TIMM8A) takes part in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial. TIMM8A plays a role as a chaperone-like protein which protects the hydrophobic precursors from aggregation and leads them through the mitochondrial intermembrane space. TIMM8A is essential for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Defects in TIMM8A cause Jensen syndrome. TIMM8A and TIMM13, forms a 70 kDa heterohexamer.

KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.