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C1QTNF3 also called Cartducin is a novel angiogenic factor in the formation of neointima following angioplasty. C1QTNF3 a paralog of Acrp30 (adiponectin). C1QTNF3 is a secretory protein produced by chondrogenic precursors & proliferating chondrocytes, and belongs to a novel C1q family of proteins. Cartducin promotes the growth of mesenchymal chondroprogenitor cells & chondrosarcoma-derived chondrocytic cells in vitro. Cartducin stimulates mesenchymal chondroprogenitor cell proliferation through extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways. C1QTNF3 promotes proliferation & the migration of endothelial cells.

PLCXD3, also referred to asphosphatidylinositol Specific Phospholipase C X Domain Containing 3, contains 1 PI-PLC X-box domain. Creutzfeldt-Jakob Disease, is one of the diseases linked with PLCXD3. It is related to Ectoderm Differentiation, obsolete signal transducer activity and phosphoric diester hydrolase activity.

Protein Phosphatase 1, Regulatory Subunit 8 (PPP1R8) is the RNA-binding subunit of a key species of protein phosphatase-1 in the nucleus. The PPP1R8 enzyme is an inhibitor subunit of the main nuclear protein phosphatase-1 (PP-1). PPP1R8 has RNA-binding activity however it doesn’t cleave RNA and may target PP-1 to RNA-associated substrates. Two isoforms of the PPP1R8 protein are specific inhibitors of type 1 serine/threonine protein phosphatases which can bind but not cleave RNA. The third isoform of the PPP1R8 protein is deficient in of the phosphatase inhibitory activity nonetheless it is a single-strand endoribonuclease comparable to RNase E of E. coli.

Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.

Astyrosine-protein phosphatase non-receptor type 11 isoform 2 (PTPN11), is a member of the protein-tyrosine phosphatase family, non-receptor class 2 subfamily. PTPN11 takes part in signal transduction from the cell surface to the nucleus downstream of various cytosolic protein tyrosine kinases as well as receptors. PTPN11 deficient cells have poor mobility due to excessive phosphorylation of FAK as well as other proteins which interfere with the rotation of cell attachment points in the focal adhesion complex.

KH Domain RNA Binding also known as QKI is a RNA-binding protein which regulates pre-mRNA splicing, export of mRNAs from the nucleus, protein translation, and mRNA stability. QKI is involved inmyelinization and oligodendrocyte differentiation, and it may play a role in schizophrenia. Defects or deletions in the QKI are linked with astrocytic tumors and may be implicated in the pathogenesis of schizophrenia. Among the diseases associated with QKI are 6q terminal deletion syndrome, and schizophrenia.

Cysteine-rich PDZ-binding protein, also known as CRIPT, takes part in the cytoskeletal anchoring of DLG4 in excitatory synapses.

Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.

Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.

Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.

Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

APRT is part of the purine/pyrimidine phosphoribosyltransferase family. APRT enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). APRT produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in APRT causes 2,8-dihydroxyadenine urolithiasis. APRT catalyzes a salvage reaction resulting in the formation of AMP.

PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.

TATDN3 is a member of the great superfamily of metalloenzymes. TATDN3 binds 2 divalent metal cations per subunit.

FSCN1 is an actin-bundling protein that is responsible for rigidity to filopodial bundles to efficiently push the membrane forward during cytoskeleton remodeling and cell migration. FSCN1 takes part in the gathering of actin filament bundles present in microspikes, membrane ruffles, and stress fibers. FSCN1 is absent from most normal epithelia though is upregulated in multiple forms of human carcinoma, where its expression associates clinically with a poor prognosis. FSCN1 expression is abundantly found in neurons, glial cells, and endothelial cells.

CCAAT/enhancer binding protein(C/EBP) a is a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and that form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBPs differ significantly in their physiological functions and in their downstream target genes. For example, mice lacking C/EBPa die shortly after birth due to severe hypoglycemia and the absence of glycogen storage in liver, whereas knockout of C/EBPb causes defects in female reproduction.

CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.

Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

X-Prolyl Aminopeptidase-1, also known as XPNPEP1 is a member of the peptidase M24B family. XPNPEP1 encodes the cytosolic form of a metalloaminopeptidase which catalyzes the cleavage of the N-terminal amino acid adjacent to a proline residue. Furthermore, XPNPEP1 plays a role in degradation as well as maturation of tachykinins, neuropeptides and peptide hormones.

Regucalcin (RGN) is a member of the SMP-30/CGR1 family. Regucalcin is a Ca (2+)-binding protein which does not contain EF-hand motif of Ca (2+)-binding domain. RGN has a critical role in the keep of intracellular Ca2+ homeostasis due to activating of Ca2+ pump enzymes in the plasma membrane (basolateral membrane), microsomes (endoplasmic reticulum) and mitochondria of many cells. Moreover, RGN plays a multifunctional role in the regulation of cell functions in the liver, kidney cortex, heart and brain and a suppressor protein for cell signaling systems in many cell types.

Ribophorin 2 (RPN2) is a dolichyl-diphosphooligosaccharide protein glycosyltransferase subunit 2. The Ribophorin 2 protein is part of an N-oligosaccharyl transferase complex which links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. RPN2 is analogous in sequence to the yeast oligosaccharyl transferase subunit SWP1.