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Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. G

Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) is a part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.

Somatostatin (also known as growth hormone inhibiting hormone (GHIH) or somatotropin release-inhibiting hormone (SRIF) is a peptide hormone that regulates the endocrine systemand affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. Somatostatin has two active forms produced by alternative cleavage of a single preproprotein: one of 14 amino acids, the other of 28 amino acids.

Protein-L-Isoaspartate O-Methyltransferase 1, also known as PCMTD1, is a part of the methyltransferase superfamily and is situated in the cytoplasm.

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.

Vanin 1 (VNN1) belongs to the vanin family of proteins, which share extensive sequence similarity with each other, and also with biotinidase. This family includes secreted and membrane-associated proteins, a few of which have been described to participate in hematopoietic cell trafficking. No biotinidase activity has been established for any of the vanin proteins; nevertheless, they possess pantetheinase activity, which may have a role in oxidative-stress response. VNN1 protein, like its mouse homolog, is probably a GPI-anchored cell surface molecule. The mouse VNN1 protein is expressed by the perivascular thymic stromal cells and regulates migration of T-cell progenitors to the thymus. VNN1 is an amidohydrolase which hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5).

ERO1-like protein alpha (ERO1L) is an essential oxidoreductase, which oxidizes proteins and is necessary for the folding of immunoglobulins. ERO1L covalently binds with PDI (protein disulfide-isomerase) and jointly they generate disulfide bonds between proteins in the endoplasmic reticulum. ERO1L is stimulated by hypoxia, proposing that ERO1L is regulated through the HIF (hypoxia inducible transcrip-tion factor) pathway. At low levels ERO1L is ubiquitously expressed, however at high levels it is expressed in the upper digestive tract and esophagus. In addition, ERO1L is involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thus having a role in retrotranslocation of the toxin. Furthermore, ERO1L plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.

Bromodomain Containing 3 (BRD3) was classified based on its homology to the gene encoding the RING3 protein, which is a serine/threonine kinase. The BRD3 protein localizes to 9q34, a region which contains a number of major histocompatibility complex (MHC) genes. The function of the BRD3 protein is unknown.

Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

GLRX5 is small redox enzyme of approximately 100 amino acids which uses glutathione as a cofactor. GLRX5 is a mitochondrial protein, which is evolutionarily conserved. GLRX5 is oxidized by substrates, and reduced non-enzymatically by glutathione. GLRX5 is involved in the biogenesis of iron-sulfur clusters that are required for normal iron homeostasis. GLRX5 is necessary for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. Defects in the GLRX5 gene are a cause of anemia sideroblastic pyridoxine-refractory autosomal recessive (PRARSA).

GREM2 which is a member of the BMP (bone morphogenic protein) antagonist family takes part in regulating organogenesis, body patterning, and tissue differentiation. GREM2 is an antagonist of BMP and like BMPs, BMP antagonists contain cystine knots and typically form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, is characterized by a C-terminal cystine knot with an 8-membered ring.

DCUN1D4 holds 1 DCUN1 domain.

UFD1L forms a complex with two other proteins, nuclear protein localization-4 and valosin-containing protein, and this complex is necessary for the degradation of ubiquitinated proteins. In addition, this complex controls the disassembly of the mitotic spindle and the formation of a closed nuclear envelope after mitosis. Mutations in this gene have been associated with Catch 22 syndrome as well as cardiac and craniofacial defects. Alternative splicing results in multiple transcript variants encoding different isoforms. A related pseudogene has been identified on chromosome 18.

MAK16 is a member of the MAK16 family.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

MED7 is a member of the Mediator complex subunit 7 family. The activation of gene transcription is a multistep course which is initiated by factors which identify transcriptional enhancer sites in DNA and collaborate with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The gene encode a subunit of the CRSP (cofactor required for SP1 activation) complex, that, together with TFIID, is needed for effective activation by SP1. Additionally, MED7 is also an element of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins that cooperate with TR and enables TR function on DNA templates in conjunction with initiation factors and cofactors.

Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

NCK1 is an adapter protein which binds with tyrosine-phosphorylated growth factor receptors or their cellular substrates. NCK1 maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. NCK1 is involved in the DNA damage response, for efficient activation of downstream effectors, such as that of CHEK2. NCK1 is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. NCK1 is located in the cytoplasm and is an adaptor protein that participates in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.

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.

Cell Cycle Exit And Neuronal Differentiation 1, also known as CEND1, is a neuron-specific protein. CEND1 take part in cell cycle control and neuronal differentiation mechanisms during neonatal SVZ neurogenesis and turn out to be crucial for the transition from neuroblasts to mature neurons when reaching high levels. The similar protein in pig enhances neuroblastoma cell differentiation in vitro and involved in neuronal differentiation in vivo. Multiple pseudogenes have been reported for this gene. The disease neuroblastoma has been associated with CEND1.

QPRT is a key enzyme in the catabolism of quinolinate. QPRT is in between the tryptophannicotinamide adenine dinucleotide (NAD) pathway, resulting in the production of nicotinic acid, carbon dioxide and pyrophosphate. Rise of QPRT levels in the brain is related to the pathogenesis of neurodegenerative disorders such as epilepsy, Alzheimer's disease, and Huntington's disease.

Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.