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GF-like family receptor 1 (IGFLR1) is encoded by a gene mapping to human chromosome 19. IGFLR1 which is cell membrane receptor for the IGF-like family proteins binds IGFL1 and IGFL3 with a higher affinity and may as well bind IGFL2.

Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

ERCC1 polypeptide is essential for nucleotide excision repair (NER) of damaged DNA and is homologous to Saccharomyces cerevisiae RAD10, which takes part in repair and mitotic intra-chromosomal recombination. NER mechanism includes dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision.

UNG is a member of the Uracil-DNA glycosylase family. One of his functions is to prevent mutagenesis by eliminating uracil from DNAmolecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil basesare formed as a result of cytosine deamination or misincorporation of dUMP residues. After a mutation is formed, the mutagenicthreat of uracil propagates through any subsequent DNA replication steps. Among the diseases associated with UNG are: congenital rubella, and immunodeficiency with hyper igm type 4.

USP15 belongs to the ubiquitin specific protease (USP) family of deubiquitinating enzymes which has a vital role in ubiquitin-dependent processes through polyubiquitin chain disassembly and hydrolysis of ubiquitin-substrate bonds. USP15 connects with the COP9 signalosome, and takes part in transforming growth factor beta signalling through deubiquitination of receptor-activated SMAD transcription factors. Alternatively spliced transcript variants encoding multiple isoforms of this gene are known, and a pseudo gene of USP15 is sited on the long arm of chromosome 2.

Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

USP14 belongs to the ubiquitin-specific processing (UBP) family of proteases which is a deubiquitinating enzyme (DUB) containing His and Cys domains. USP14 placed in the cytoplasm and cuts the ubiquitin from ubiquitin-fused precursors and ubiquitinylated proteins.a mutation which results in reduced expression of the ortholog of USP14 in mice inhibits growth, develop severe tremors by 2 to 3 weeks of age followed by paralysis and death by 6 to 10 weeks of age.

The Argonaute protein is part of the RISC or RNA-induced silencing complex, as so, the protein has a key part in the slicing processes of RNA. The RNA interference (RNAi) is being held by RISC. Small non-coding RNA fragments bond to the Argonaute proteins, through base pairing, eventually leads to the cleavage of messenger RNA or translation suppression.

Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.

Protein modification with ubiquitin is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1) belongs to the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins. UE2G1 protein is involved in degradation of muscle-specific proteins.

Tubulin Polyglutamylase Complex Subunit 2 (TPGS2) is a component of the neuronal polyglutamylase complex, which takes part in post-translational addition of glutamate residues to C-terminal tubulin tails. Alternatively spliced transcript variants encoding multiple isoforms have been monitored for TPGS2.

Melanoma-associated antigen D1 (MAGED1) belongs to the melanoma antigen gene (MAGE) family and expressed in virtually all normal adult tissues. MAGED1 is involved in the p75 neurotrophin receptor mediated programmed cell death pathway. MAGED1 is involved in Prader-Willi syndrome including hyperphagia, repetitive and compulsive behaviors, and cognitive impairment. MAGED1 is involved in the apoptotic response following NGF (nerve growth factor) binding in neuronal cells. MAGED1 hinders cell cycle progression, and facilitates NGFR-mediated apoptosis. MAGED1 functions as a regulator of the function of DLX family members. MAGED1 has a role in the circadian rythm regulation.

Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

E.Coli Uracil DNA Glycosilase (UNG) catalyses the release of free Uracil from Uracil-containing DNA. UNG efficiently hydrolyzes uracil from signle-stranded or double-stranded DNA, but not from oligomers (6 fewer bases).

SMAD2 is part of the SMAD family of proteins that mediate signal transduction by the TGF-beta/BMP-2/4 cytokine superfamily from receptor Ser/Thr protein kinases at the cell surface to the nucleus. Phosphorylated SMAD2 is then able to form a complex with SMAD4 or SARA. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression. SMAD2 mediates the signal of the TGF-beta, and therefore regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. SMAD2 is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein.
TGF-beta 1 acts on adjacent stromal cells to turn on SMAD2 signalling that could lead to stromal decidualization. SMAD2 is the downstream signal transducers of TGF-beta-1 in human dental pulp cells.

NPM2 is a member of nucleoplasmin family. NPM2 is a core histones chaperone which takes part in chromatin reprogramming, particularly throughout fertilization and early embryonic development. NPM2 also takes part in sperm DNA decondensation during fertilization.

Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

PSMB5 belongs to the proteasome B-type family that has a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is substituted by catalytic subunit 3i (proteasome beta 8 subunit). A fundamental function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB5 exhibits an ATP dependent proteolytic activity and is involved in an ATP/ubiquitin dependent non lysosomal proteolytic pathway.

SMAD3 is part of the SMAD family of proteins that mediate signal transduction by the TGF-beta/activin/BMP-2/4 cytokine superfamily from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD3 has a role as a transcriptional modulator activated by TGF-Beta and is involved in the regulation of carcinogenesis. SMAD3 mutations are related with the pathogenesis of human osteoarthritis. SMAD3 expression take part in tumor suppression in the premature stages of gastric carcinogenesis. SMAD3 is involved in nuclear translocation of beta-catenin.

Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.

Olfactory marker protein (OMP) which is expressed in the cytoplasm of olfactory chemosensory neurons in the nasal neuroepithelium, is associated in a unique way with the mature olfactory receptor neurons in numerous vertebrate species. OMP have a modulatory part in the odor detection/signal transduction cascade ant its expression is a sign of mature vertebrate olfactory receptor neurons (ORNs). OMP is also a potent enhancer of mitosis in fetal olfactory epithelial cells and it promotes an increase in uptake of tritiated thymidine in liver.