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GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.

Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. TPK1 is found in the heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. TPK1 gene defects cause the thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5), which is an autosomal recessive metabolic disorder due to an inborn error of thiamine metabolism.

Thiosulfate Sulfurtransferase Like Domain Containing 3, also known as TSTD3 contains 1 rhodanese domain which is characterized by an active site cysteine residue that has the ability to bind sulfane sulfur and catalyse sulfur transfer.

Ubiquinone biosynthesis protein COQ9 (COQ9) represents a mitochondrial ubiquinone biosynthesis gene. The COQ9 protein is likely required for biosynthesis of coenzyme Q10, since mutations at this locus have been linked with autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency.

TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.

UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.

TRAF-interacting protein with FHA domain-containing protein A (TIFA) is an adapter protein that mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, triggering the downstream activation of NF-kappa-B and AP-1 pathways. The TIFA protein stimulates the oligomerization and polyubiquitination of TRAF6, leading to the activation of TAK1 and IKK through a proteasome-independent mechanism.

Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

Ubiquitin thioesterase OTUB2 (OTUB2) is a member of the peptidase C65 family. OTUB2 functions as a hydrolase which can remove conjugated ubiquitin from proteins in vitro and may thus play a key regulatory role at the level of protein turnover by preventing degradation.

Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain. Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.

Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.

Ubiquitin-like modifier activating enzyme 5 (UBA5) is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates an ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.

Ubiquitin Conjugating Enzyme E2Z, also known as UBE2z, is a protein coding gene which is a part of the ubiquitin-conjugating enzyme family. UBE2z catalyzes the covalent attachment of ubiquitin to various proteins. UBE2z takes part in in apoptosis regulation and is also a specific substrate for UBA6, not charged with ubiquitin by UBE1.

COPZ1 is a member of the adaptor complexes small subunit family. Coatomer is an oligomeric complex which contains as a minimum the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The zeta subunit has a part in regulating the coat assembly and, therefore, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.

NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

Bestrophin 1 (BEST1) is a part of the bestrophin gene family and is also forms calcium-activated chloride-ion channels in epithelial. This small gene family is characterized by proteins with a highly conserved N-terminus with 4-6 transmembrane domains. BEST1 is extremely permeable to bicarbonate.

FBL is a significant small nucleolar protein in eukaryotes, which has an essential role in pre-rRNA processing during ribosomal biogenesis. Fibrillarin is a component of several ribonucleoproteins including a nucleolar small nuclear ribonucleoprotein (SnRNP) and one of the two classes of small nucleolar ribonucleoproteins (snoRNPs). Fibrillarin contains an N-terminal repetitive domain which is rich in glycine and arginine residues, like fibrillarins in other species. Fibrillarin’s central region is similar to an RNA-binding domain and contains an RNP consensus sequence. FBL is linked to the U3, U8, and U13 small nuclear RNAs and is positioned in the dense fibrillar component (DFC) of the nucleolus. Antisera from roughly 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.

Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

UBE2L6 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2L6 enzyme is very similar in its primary structure to the enzyme encoded by UBE2L3 gene. UBE2L6 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2L6 functions in the e6/e6-ap-induced ubiquitination of p53/tp53.

Microtubule-associated proteins 1A/1B light chain 3 beta 2 (MAP1LC3B2) is a member of the MAP1LC3 family. MAP1LC3B2 is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and essential for neurogenesis. The MAP1LC3B2 protein is possibly involved in formation of autophagosomal vacuoles (autophagosomes). MAP1LC3B2 is expressed primarily in the heart, testis, brain and skeletal muscle.

DYNLT3 belongs to a subclass of dynein light chains. The DYNLT3 protein homodimerizes and forms the light chain component of the cytoplasmic dynein motor protein complex. DYNLT3 functions as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex which are believed to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. DYNLT3 may also work independently of dynein as a transcriptional modulator. DYNLT3 is required for the effective progression through mitosis.

EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.

Sorting nexin 3 (SNX3) belongs to the large family of hydrophilic proteins, which interact with various receptor types and are involved in intracellular trafficking. SNX3 interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. SNX3 comprises a distinct subgroup of nexins, which share less sequence similarity outside of the PX domain and have significantly different binding affinities for the tyrosine kinase receptors.