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DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.

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).

SPRY domain-containing SOCS box protein 1 (SPSB1) belongs to the SOCS box protein subfamily. SPSB1 includes a central SPRY domain and a C-terminal SOCS box. Even though, some of the SOCS protein subfamilies function as adaptors for a large family of ubiquitin-protein isopeptide ligases to regulate certain signaling pathways, the function of the SSB subfamily remains to be determined. SPSB1 may have an imperative role in enhancing the HGF-induced Erk-Elk-1-SRE pathway. SPSB1 overexpression exhibited no effect on the basal level or epidermal growth factor-induced SRE-luciferase activity.

Killer cell immunoglobulin-like receptor 2DL5A (KIR2DL5A) is a type I transmembrane glycoprotein which is a member of the killer cell Ig-like receptor (KIR) family.KIR2DL5A is detected on the cell surface as a monomer which, upon tyrosine phosphorylation, recruits the Src homology region 2-containing protein tyrosine phosphatase-2. Therefore, KIR2DL5A is an inhibitory receptor gathering a combination of genetic, structural, and functional features unique among KIR, suggesting that KIR2DL5A plays a specialized role in innate immunity.

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.

Motile Sperm Domain Containing 1, also known as MOSPD1 is a protein coding gene which owns one MSP domain.

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.

KCTD4 also known as Potassium Channel Tetramerisation Domain Containing 4 has an N-terminal homodimerization domain which contains multiple copies of kelch repeats and C2H2-type zinc fingers. Proteins which include BTB domains are consider being involved in transcriptional regulation through control of chromatin structure and function. In addition, KCTD4 is a 259 amino acid protein which contains one BTB domain, a possible role as a transcriptional regulator may be suggested.

Fibronectin Type III Domain Containing 5 (Irisin) is a newly discovered hormone, secreted into circulation by muscle, which acts on white adipocytes and promotes WAT “browning”. r-Irisin can reduce body weight and cause induction of brown adipocyte in vivo, including a capacity for thermogenic energy expenditure mediated by uncoupling protein 1 (UCP-1). Irisin mature protein is comprised of 110 amino acid residues and two potential glycosylation sites. High levels of Irisin can be found in the heart whereas Very low expression is found in the colon, pancreas and spleen, if any.

PIH1 Domain Containing 2, also known as PIH1D2 is a member of the PIH1 family.PIH1D2 was present in the common ancestor of chordates. There are 45 Species with no ortholog for PIH1D2. In addition, no disorders were found for PIH1D2 Gene.

Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

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.

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.

FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.

Regulation of nuclear pre-mRNA domain-containing protein 1B (RPRD1B) interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. RPRD1B stimulates binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. RPRD1B inhibits RNA polymerase II from reading through the 3' end termination site and may allow it to be drafted back to the promoter through promotion of the formation of a chromatin loop. In addition, RPRD1B enhances the transcription of several other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. RPRD1B also promotes cell proliferation.

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. KIR2DL3 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, cl-6, NKAT2 or KIR-K7), which recognizes class I MHC molecules (HLA-Cw1, -Cw3, -Cw7, and Cw8). KIR2DL3 inhibits the activity of NK cells thus preventing cell lysis.

Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

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.

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

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.

Cold shock domain-containing protein C2 (CSDC2) is RNA-binding factor that binds specifically to the very 3'-UTR ends of both histone H1 and H3. 3 mRNAs encompass the polyadenylation signal. The CSDPs (cold shock domain containing proteins) are one group of the evolutionarily conserved nucleic acid-binding proteins extensively distributed in bacteria, plants, animals, and involved in a variety of cellular processes, including adaptation to low temperature, cellular growth, nutrient stress and stationary phase. CSDC2 has a central role in the negative regulation of histone variant synthesis in the developing brain.

DnaJ (Hsp40) Homolog, Subfamily C, Member 12 (DNAJC12) belongs to the DnaJ/Hsp40 family. DnaJ/Hsp40 family members are linked with complex assembly, protein folding, and export. DnaJ/Hsp40 proteins are extremely conserved throughout evolution and function as co-chaperones regulating protein folding, transport, translational initiation and gene expression. DnaJC12 has a role in protein folding and export and is believed to be involved in estrogen control and the development of breast cancer. DNAJC12 is expressed at high levels in the brain, heart, and testis, and at reduced levels in the kidney and stomach.

WFDC12 belongs to the WFDC (WAP-type four-disulfide core) domain family. The WAP signature motif or WFDC domain has four disulfide bonds created by eight cysteines at the core of the protein, which operates as a protease inhibitor.

C-type Lectin Domain Family 4, Member M (CLEC4M) is a type II integral membrane proteinand A pathogen-recognition receptor which takes part in peripheral immune surveillance in liver. CLEC4M mediates the endocytosis of pathogens which than degraded in lysosomal compartments. CLEC4M is a receptor for ICAM3, binding to mannose-like carbohydrates and also recognizes various evolutionarily divergent pathogens with a large impact on public health, including tuberculosis mycobacteria, and viruses which among them are Ebola, hepatitis C,influenza A, HIV-1, West Nile virus and the SARS-CoV acute respiratory syndrome coronavirus.