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PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

M2 autoantigen is a key mark of antimitochondrial autoantibodies (AMA), a typical serological feature in patients suffering from primary biliary cirrhosis (PBC) which is a serious autoimmune liver disease accompanied by damage to intrahepatic bile ducts. Molecular definition of the M2 antigen has displayed it as no less than 3 separate target proteins. The M2 role is like the so-called E2 subunits (or dihydrolipoamide transferases) of different mitochondrial dehydrogenase complexes:
*pyruvate dehydrogenase complex.
*branched chain 2-oxo-acid dehydrogenase complex.
*2-oxoglutarate dehydrogenase complex.
Biochemically, these complexes catalyze the oxidative decarboxylation of various alpha-keto-acid substrates and systematically engage with a prosthetic lipoamide group; they are situated in the mitochondrial matrix in association with the inner membrane. The most well-known reactivity of AMA positive PBC sera is against PDC-E2. Some patients have AMA which reacts with PDC-E2 alone (95%), but most patients also show reactivity against OGDC-E2 (39-88%) and/or BCOADC-E2 (53-55%). Actually, patients can be found with reactivity only against OGDC-E2 and/or BCOADC-E2 and no PDC-E2 autoantibodies. These patients will be overlooked in assays based on natural source-derived, predominantly PDC-E2-containing M2 antigen preparations.

SULT1E1 catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. Decreased SULT1E1 expression is linked with estrogen-dependent endometrial carcinomas. Altered cellular proliferation was detected in cells stably expressing SULT1E1.

LCMT1 is a member of the LCMT family, methyltransferase superfamily. LCMT1 catalyzes the methylation of the carboxyl group of the C-terminal leucine residue (leu309) of the catalytic subunit of protein phosphatase-2A to form alpha-leucine ester residues.

Sulfotransferase 1C2 (SULT1C2) is a member the sulfotransferase1 superfamily. SULT1C2 catalyzes the transfer of sulfate from PAPS (3’-phosphoadenosine-5’-phosphosulfate) to phenol-containing compounds, including hormones and neurotransmitters. A short and a long isoform of SULT1C2 exist as a result of alternative splicing events. Sulfotransferase enzymes catalyze the sulfate conjugation of various hormones, neurotransmitters, drugs, and xenobiotic compounds.

Sulfotransferase 1A2 (SULT1A2) belongs to the sulfotransferase family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.

PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1 is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

RNA methyltransferase-like protein 1, also known as RNMTL1 is a member of the RNA methyltransferase TrmH family. RNMTL1 is probable RNA methyltransferase and expressed at an equal level in normal liver and hepatocarcinoma.

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.

Carbohydrate Sulfotransferase 5 (CHST5) is a Golgi-embedded enzyme that is found in B cells, T cells and intestinal epithelium and is also mediates sulfation of keratan in cornea. CHST5 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine residues of keratan. CHST5 works on the non-reducing terminal GlcNAc of short andlong carbohydrate substrates that have poly-N-acetyllactosamine structures.

HAT1 is a type B histone acetyltransferase that participates in the rapid acetylation of newly synthesized cytoplasmic histones, which are in turn imported into the nucleus for de novo deposition onto nascent DNA chains. Histone acetylation, mainly of soluble histone H4 at ''Lys-5'' and ''Lys-12'' and acetylates histone H2A at ''Lys-5''. HAT1 takes part in replication-dependent chromatin assembly. HAT1 acetylates soluble but not nucleosomal histone H4 at lysines 5 and 12, and to a lesser degree, histone H2A at lysine 5. HAT1 has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG.

Set 7/9 is a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet). The methylation of lysine residues of histones plays a critical role in the regulation of chromatin structure and gene expression.
Acetylation, phosphorylation and methylation of the amino-terminal tails of histone are thought to be involved in the regulation of chromatin structure and function. The enzymes identified in the methylation of specific lysine residue on histones belong to the SET family with just one exception. Set7/9, unlike most other SET proteins, is exclusively a mono-methylase.

PRMT3, also known as protein arginine N-methyltransferase 3, is a member of the protein arginine methyltransferase family. PRMT3 catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. PRMT3 operates on 40S ribosomal protein S2 ,rpS2, which is the major in-vivo substrate, additionally PRMT3 is also involved in the proper maturation of the 80S ribosome.

GST family of enzymescomprises a long list of cytosolic, mitochondrial, and microsomalproteinsthat are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenousand xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminusof a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombindomain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.

GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.

GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called ''GST gene fusion system''. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector''s multiple cloning sites results in expression of a fusion protein - the protein of int

GSTT1 belongs to a superfamily of proteins which catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. GSTT1 is one of the GSTs’ four main classes: alpha, mu, pi and theta (which includes GSTT1 and GSTT2). GSTT1 is involved in activation and detoxification reactions and catalyzes the conjugation of industrial chemicals, such as epoxybutane, ethylene oxides, halomethane with glutathione. GSTT1 is found in erythrocytes, at low levels in the liver as well as in Clara and ciliated cells at the alveolar/bronchiolar junction in the lung. The GSTT1 gene is deficient in 38% of the population. The GSTTI enzyme deficiency might influence the individual risk for development of acquired aplastic anemia and acute myeloid leukemia. The presence or absence of the GSTT1 gene is concurrent with GSST1+ (the conjugator) and GSTT1- (the non-conjugator) phenotypes correspondingly. The GSTT1+ phenotype is able to catalyze the glutathione conjugation of dichloromethane. GSTT1-null genotypes are seen as having a higher risk of developing leukoplakia. Germline genetic polymorphism in GSTT1 is linked to breast cancer.

GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.

GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminus of a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombin domain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.

GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminus of a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombin domain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.

GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells. Mutations in UMPS are the reason of inherited orotic aciduria disease.