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ASB8 is a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex that facilitates the ubiquitination and consequent proteasomal degradation of objective proteins.

COMM domain-containing protein 9 (COMMD9), is a part of the COMMD family. The COMMD family is a group of evolutionary conserved proteins that share a common COMM domain at their extreme C-terminus, which provides an interface for protein-protein interactions. COMMD9 is a 198 amino acid ubiquitously expressed protein which contains one COMM domain and involved in signaling events all over the cell.

TXNDC17 is a disulfide reductase that takes part in several redox reactions using the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. TXNDC17 has peroxidase activity and assists to eliminate cellular hydrogen peroxide.

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.

Truncated BH3 interacting domain death agonist is a truncated form of the pro-apoptotic full-length BID. Truncated BH3 interacting domain death agonist is generated by Caspase-8 cleavage of BID. The truncated form of the protein translocates from the cytosol to mitochondria and transduces apoptotic signals.
BID is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.

Jumonji Domain Containing 6, also known as JMJD6 performs as a lysyl-hydroxylase which catalyzes 5-hydroxylation on specific lysine residues of target proteins for instance U2AF2/U2AF65 and LUC7L2, as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Additionally to peptidyl-lysine 5-dioxygenase activity, JMJD6 performs as an RNA hydroxylase, as proposed by its ability to bind single strand RNA. Furthermore, it acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) as well as histone H4 at 'Arg-3' (H4R3me), thus taking a part in histone code.

Josephin-1 (JOSD1) has minimal protease activity towards poly-ubiquitin chains (in vitro). JOSD1 functions as a deubiquitinating enzyme. Ubiquitin-binding sites in the Josephin domain are a factor in ubiquitin chain binding and cleavage.

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.

C-type lectin domain family 5-member A isoform 1 (CLEC5A) is part of the CTL/CTLD superfamily which carry various functions, for instance cell-cell signaling, cell adhesion, glycoprotein turnover, in addition to their inflammation & immune response abilities. CLEC5A operates as a cell attachment receptor for all 4 serotypes of Dengue virus in addition to Japanese encephalitis virus. CLEC5A binds to the dengue virus and it triggers signaling through the phosphylation of TYROBP, as a result no viral entrance occurs, however this interaction does stimulate proinflammatory cytokine release. CLEC5A preforms as a positive regulator of osteoclastogenesis and also a main regulator of synovial injury & bone erosion for the period of autoimmune joint inflammation.

Pleckstrin homology-like domain family A member 2 (PHLDA2) is a cytoplasmic protein, which is involved in fetal and placental growth. PHLDA2 is an apoptosis-related protein, which acts as a negative growth regulator and is expressed during normal human development. PHLDA2 is imprinted on placenta, liver and fetal tissues during embryogenesis and is removed once development is complete. The PHLDA2 gene is one of a number of genes in the imprinted gene domain of 11p15.5 which is considered to be an important tumor suppressor gene region. Changes in this region may be linked to the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. PHLDA2 is expressed in placenta (present in all cells of the villous cytotrophoblast) and adult prostate gland. Furthermore, PHLDA2 is expressed in adult brain and neuroblastoma, medullablastoma and glioblastoma cell lines and at low levels in adult liver and lung, and fetal liver.

TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

C-Type Lectin Domain Family 10, Member A (CLEC10A) is a part of the C-type lectin superfamily. CLEC10A is expressed in immature myeloid dendritic cells and alternatively activated macrophages. CLEC10A takes part in regulating adaptive and innate immune responses and also binds in a calcium dependent way to terminal galactose and N-acetylgalactosamine, linked to serine or threonine.

PDZ Domain Containing 11 (PDZD11) is a cytosolic protein which contains one PDZ (DHR) domain. PDZD11 displays a resemblance to members of the MALS / VELIS family of proteins. PDZD11 contains but one PDZ domain which seemingly interacts with the C-terminus of partner proteins. PDZD11 is ubiquitously expressed and targets calcium and copper ATPases to basolateral cell membranes. PDZD11 is a briefly interacting partner of the PMCA b-splice forms which have a role in their sorting to or from the plasma membrane.

Chromosome 10 Open Reading Frame 54, also known as C10ORF54 is part of the immunoglobulin superfamily. Like a transmembrane molecule, C10ORF54 is expressed in the bone on embryonic stem cells (ESCs), and on tumor cell surface as well. Accordingly, C10ORF54 supports the differentiation of ESC and ehhances BMP4 induced signaling in ESC, however C10ORF54 is also down regulated following to BMP4 exposure.

JmjC domain-containing protein 7 (JMJD7) is a member of the JMJD family. JMJD7 encodes highly conserved proteins with a JmjC domain, which are part of the cupin metalloenzyme superfamily. JMJD7 was first thought to be an alternatively spliced isoform of PLA2G4B. It is derived from JMJD7 which is located upstream of PLA2G4B. Most tissues also express read-through transcripts from JMJD7 into the downstream PLA2G4B gene, some of which may encode fusion proteins combining the N-terminus of JMJD7 with PLA2G4B protein.

TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

Ras association domain-containing protein 3 (RASSF3) is a ubiquitously expressed protein found in normal and cancerous tissues. RASSF3 is a member of RASSF family whose members contain a highly conserved Ras association domain (Ral GDS/AF-6 or RA) and function as Ras effectors/tumor suppressors. RASSF3 contains an N-terminal RA domain and a coiled-coil SARAH domain and may have 3 isoforms (RASSF3A, RASSF3B and RASSF3C) due to alternative splicing. RASSF3B and RASSF3C are shorter than RASSF3A and do not contain the RA and SARAH domain.

Human norovirus is classified into two groups, group 1& group 2. Norwalk virus is the species which belongs to group 1 and was discovered in 1968 at Ohio. Norovirus is a familiar virus which causes human gastroenteritis with the following symptoms vomiting, diarrhea and sickness. CDC report revealed that there are 19-21 million Americans infected by Nororvirus annually with 800 deaths, 1 in 15 people with infection. Around the world, this virus affects about 267 million people and causes over 200,000 deaths each year; these losses are mostly in less developed countries and in the very young, elderly and immuno-suppressed population, though, most cases are self-limited with a full recovery within just a few days. Norovirus is extremely contagious and can spread from human to human through infected food, water or contaminated surfaces. The outbreaks usually occur from November-April, while the peak is in January. Norovirus is a positive sense RNA virus with 7.5 kb nucleotides, encoding a major structural protein VP1 with 50-55kDa. The full length of VP1 capsid comprises the internal N-terminal, Hinge, shell (S) and protruding (P) domains. P domain from 225 to 520 forms P1- P2-P1 structure. Moreover, P domain has a receptor binding region which recognizes human histo-blood group antigens (HBGAs). P domain expressed in bacteria can spontaneously form a P dime as well as a P particle aggregated by 12 P dimmers. P particle displays an increased binding activity to HBGAs higher than virus-like particle (VLP) formed by the full-length capsid. For norovirus vaccine development, we consider P domain as a good candidate.

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.

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.

TTC32 contains 3 TPR repeats. The tetratricopeptide repeat (TPR) is a structural motif. TPR is observed in organized 3–16 motifs, which form scaffolds to mediate protein–protein interactions and frequently the assembly of multiprotein complexes. TPR-containing proteins include the anaphase-promoting complex subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the major receptor for peroxisomal matrix protein import PEX5, the PKR protein kinase inhibitor and mitochondrial import proteins.

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 extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
The three Ig-domain from of inhibitory killer cell Ig-like receptor 1(KIR3DL1, NKB1, nkat3, p70KIR) is a NK cell receptor for polymorphic HLA-B determinant. KIR3DLl recognizes the Bw4 determinant defined by sequence motifs at positions 77-83 of the HLA-B heavy chain. The cytoplasmic tail of KIR, which contains two immunoreceptor tyrosine-based inhibition motifs (ITIMs), mediates inhibitory signal transduction that prevents killer cell-mediated cytotoxicity. A His-tag fusion protein of KIR3DL1 cytoplasmic tail (361-444aa) was overexpressed as insoluble protein aggregates (inclusion bodies).

Haloacid dehalogenase-like hydrolase domain-containing protein 3 (HDHD3) is a member of the HAD-like hydrolase superfamily. This family of hydrolase enzymes includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases.

C-type Lectin Domain Family 2, Member B (CLEC2B) belongs to the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of the CTL/CTLD family share a common protein fold and have various functions, such as cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response. The CLEC2B gene is closely connected to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. CLEC2B is expressed preferentially in lymphoid tissues, and in most hematopoietic cell types.