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CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

Ras-related GTP binding C (RRAGC) is a monomeric guanine nucleotide-binding protein, or G protein. As a result of binding GTP or GDP, small G proteins act as molecular regulators in various cell processes and signaling pathways. RRAGC regulates the organization of the actin cytoskeleton and has an intrinsic GTPase activity. RRAGC is possibly necessary for the amino acid-induced relocalization of mTORC1 to the lysosomes and its succeeding activation by the GTPase RHEB, which is key step in the activation of the TOR signaling cascade by amino acids.

RNA 3'-Terminal Phosphate Cyclase (RTCA) encodes a part of the RNA 3'-phosphate cyclase family. RTCA takes part in RNA metabolism by catalyzing the ATP-dependent conversion of the 3'-phosphate of RNA substrates to a 2',3'-cyclic phosphodiester. RTCA is involved in some phases of cellular RNA processing.

ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

Enhancer of rudimentary homolog (ERH) is a ubiquitously expressed transcriptional coregulator which is highly conserved among eukaryotes. ERH may have a role in cell cycle regulation and pyrimidine biosynthesis. ERH has two casein kinase II phosphorylation sites which are thought to upset the ability of ERH to dimerize.

CUE Domain Containing 2 also known as CUEDC2 is a part of the CUEDC2 family and contains 1 CUE domain. CUEDC2 down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway and controls PGR protein levels through a parallel mechanism.

RHOC is a small signaling G protein/GTPase which is part of the Rac subfamily of the family Rho family of GTPases. RHOC rotats between inactive GDP-bound and active GTP-bound states and has a role as a molecular switch in signal transduction cascades. RHOC promotes reorganization of the actin cytoskeleton and regulates cell shape, attachment, and motility.

EDN3 interacts with endothelin receptor B, on the surface of cells. Throughout embryonic development, EDN3 takes part in neural crest cells that migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. EDN3 and EDN3R are necessary for the formation of nerves in the large intestine (enteric nerves) and melanocytes (produce melanin). Mutations in the EDN3 gene is linked with Waardenburg syndrome, type IV that is characterized by changes in skin, hair, and eye coloring. Mutations in the EDN3 gene is linked with Hirschsprung disease that causes severe constipation or intestinal blockage.

Ubiquinol-Cytochrome C Reductase Core Protein I (UQCRC1) is a member of the peptidase M16 family,UQCRC1/QCR1 subfamily. UQCRC1 is a part of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is component of the mitochondrial respiratory chain. UQCRC1 can mediate formation of the complex between cytochromes c and c1.

EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

The 23kDa two-domain periplasmic chaperone FIMC from E.coli is vital for the assembly of type-1 pili, which are filamentous, very oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces and persist in macrophages.

The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

PA2G4 belongs to the peptidase M24C family and functions as an RNA-binding protein involved in cellular proliferation and differentiation processes. PA2G4 is a component of pre-ribosomal ribonucleoprotein complexes, participating in ribosome assembly and regulating the later steps of rRNA processing. Also, PA2G4 interacts with ErbB-3 and may function as a modulator of the ErbB-3 mediated signal transduction pathway by regulating the effects of Neuregulin-1. Furthermore, PA2G4 is a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 is implicated in growth inhibition and the induction of differentiation of human cancer cells. In addition, PA2G4 mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). PA2G4 associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA.

CUE Domain Containing 1, also know as CUEDC1 contains 1 CUE domain. The CUE domain is structurally associated to the ubiquitin-binding UBA domain and exists as a domain-swapped dimer which makes additional contacts with ubiquitin, and as a result, binds ubiquitin with higher affinity. The CUE domain is discovered in proteins with diverse functions including protein sorting and degradation of misfolded proteins in the endoplasmic reticulum.

Cytochrome b-c1 complex subunit 2, mitochondrial (UQCRC2) is a member of the peptidase M16 family. UQCRC2 is a component of the ubiquinol-cytochrome c reductase complex (complex III), which is a part of the mitochondrial respiratory chain. UQCRC2 is essential for the compilation of the complex.

EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.

EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

Actin-related protein 2/3 complex subunit 3 (ARPC3) which Belongs to the ARPC3 family is one of 7 subunits of the human Arp2/3 protein complex. The Arp2/3 complex is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. ARPC3 which is localized to the cytoplasm and cytoskeleton, interacts with p20-ARC and takes part in the structural integrity of the protein complex.