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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.

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.

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.

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.

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.

TBC1 Domain Family, Member 13, also known as TBC1D13, contains 1 Rab-GAP TBC domain. TBC1D13 acts as a GTPase-activating protein for Rab family protein.

TBC1D1 belongs to a family of proteins sharing a 180-200 a.a TBC domain having a role in regulating cell growth and differentiation of various tissues. These proteins share significant homology with TRE2, yeast Bub2, and CDC16. TBC1D1 function as a GTPase-activating protein for Rab family proteins. TBC1D1 is involved in the trafficking and translocation of GLUT4-containing vesicles. Among the diseases associated with TBC1D1 are tuberculous meningitis, and meningitis.

CARD18 belongs to the death-domain-fold superfamily which is induced by proinflammatory stimuli. CARD18 contains basically only a Caspase recruitment domain, inhibits generation of IL-1b by cooperating with caspase-1 and inhibiting connotation with RIP 2. The connotation of CARD18 to caspase-1 is enabled by the charge-charge interactions between the prodomain of caspase-1 and the surface charge of CARD18.

Caspase Recruitment Domain Family, Member 17 (CARD17) is a regulator of procaspase-1/CASP1 activation involved in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release throughout inflammation. CARD17 inhibits the release of IL1B in reaction to LPS in monocytes. Though, unlike CASP1, CARD17 do not induce NF-kappa-B activation.

IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

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.

C-type Lectin Domain Family 1 Member B, also known as CLEC1B. NK-Natural killer cells express multiple calcium-dependent (C-type) lectin-like receptors, for instance CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), which interact with major histocompatibility complex class I molecules and either inhibit or else activate cytotoxicity and cytokine secretion. CLEC1B is a C-type lectin-like receptor which is expressed in myeloid cells as well as in NK cells.

C-type lectin domain family 2, also referred to CLEC2D, is a receptor for KLRB1 which protects target cells against natural killer cell-mediated lysis.It has been shown that CLEC2Dinhibits osteoclast formation and bone resorption. The protein controls the release of interferon-gamma and contains a transmembrane domain near the N-terminus likewisethe C-type lectin-like extracellular domain.

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.

C-type lectin domain family 7 member A 1 or CLEC7A is a protein, that in the innate immune system, acts against fungal pathogens. CLEC7A can be found in the immune system response cells such as monocytes, macrophages & neutrophils, or in dendritic and T cells. The protein is enhanced by macrophages by using GM-CSF, IL-4, or IL-13, or diminishes by dexamethasone, IL-10 and LPS.

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.

Pleckstrin Homology Domain Containing Family F Member 2, also known as PLEKHF2, contains 1 FYVE-type zinc finger and 1 PH domain. PLEKHF2 takes part in early endosome fusion upstream of RAB5, regulates receptor trafficking and fluid-phase transport. PLEKHF2 increases cellular sensitivity to TNF-induced apoptosis.

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.

C-type Lectin Domain Family 1 Member B, also known as CLEC1B. NK-Natural killer cells express multiple calcium-dependent (C-type) lectin-like receptors, for instance CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), which interact with major histocompatibility complex class I molecules and either inhibit or else activate cytotoxicity and cytokine secretion. CLEC1B is a C-type lectin-like receptor which is expressed in myeloid cells as well as in NK cells.

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.

TBC1 domain family member 22B, also known as TBC1D22B acts as a GTPase-activating protein for Rab family protein. The Tre-2/Bub2/Cdc16 (TBC) domain is a conserved protein motif which consists of roughly 200 amino acids and functions as a specific Rab-GAP domain. The TBC domain has more than 40 distinct TBC domain-containing proteins which have been identified in humans.

GIPC2 is a 315 aa protein which is restricted to the cytoplasm and holds one PDZ domain. GIPC2 is expressed in large quantities in colon and kidney and in small quantities in adult liver. GIPC2 has a vital part in human gastric cancer by control of growth factor signaling or cell adhesion.

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.

TSC22 domain family protein 3 (TSC22D3) protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity which initiates the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, TSC22D3 has a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, TSC22D3 hinders anti-CD3-induced NFKB1 nuclear translocation. In vitro, TSC22D3 curbs AP1 and NFKB1 DNA-binding activities.