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GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.

Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.

Pyrroline-5-carboxylate reductase 2 isoform 1 (PYCR2) is a member of the pyrroline-5-carboxylate reductase family. PYCR2 protein catalyzes the conversion of pyrroline-5-carboxylate to proline, which is the last step in proline biosynthesis. The three substrates of the PYCR2 enzyme are L-proline, NAD+, and NADP+, while its four products are 1-pyrroline-5-carboxylate, NADH, NADPH, and H+.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Syndecan 2 (SDC2) is a conserved family of heparan- and chondroitin-sulfate carrying transmembrane protein. Syndecan 2 is a cell membrane proteoglycan which modulates the activity and dynamics of some growth factor receptors and integrins. SDC2 is expressed in HSCs (hepatic stellate cells), a key cell type involved in matrix deposition in liver fibrotic disorders. SDC2 is implicated in the formation of specialized membrane domains and serves as a direct link between the extracellular environment and the organization of the cortical cytoplasm.

DNA Cytosine-5--Methyltransferase 3-Like (DNMT3L) is a nuclear protein with similarity to DNA methyltransferases, but is not believed to act as a DNA methyltransferase since it doesn’t contain the amino acid residues needed for methyltransferase activity. Nevertheless, DNMT3L stimulates de novo methylation by DNA cytosine methyltransferase 3 alpha and is assumed to be required for the formation of maternal genomic imprints. DNMT3L also mediates transcriptional repression as a result of interaction with histone deacetylase 1. DNMT3L is a catalytically inactive regulatory factor of DNA methyltransferases, which is vital for the function of DNMT3A and DNMT3B. DNMT3L activates DNMT3A and DNMT3B by binding to their catalytic domain. Furthermore, DNMT3L accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases.

NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.

BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.

KxDL Motif Containing 1 (KXD1) is a member of the KXD1 family. KXD1 is participating in endosomal cargo sorting. KXD1 contacts with the BLOC-1 complex and Interacts with BLOC1S1. KXD1 Interacts with DTNBP1/BLOC1S7 through coiled-coil domain.

LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

Thioredoxin Reductase 3 Neighbor, also known as TXNRD3NB is expressed in pancreas, esophagus, bone marrow and keratinocytes. TXNRD3NB shares overlapping exons with TXNRD3. In addition the initiation codon is found in exon 3 of the TXNRD3IT1 gene.

Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.

Spermine synthase (SMS) is amember of the spermidine/spermine synthase family. SMS is an enzyme which converts spermidine into spermine. The SMS enzyme is essential for normal viability, growth and fertility involved in polyamine metabolism. Defects in the SMS gene are the cause of Snyder-Robinson syndrome (SRS), also known as X-linked mental retardation Snyder-Robinson type. SRS is categorized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry, its transmission is X-linked recessive.

IMPA2 is a member of the inositol monophosphatase family. IMPA2 catalyzes the dephosphoylration of inositol monophosphate and has a significant role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain. IMPA2 is considered to have a role in schizophrenia and bipolar disorder.

Proteasome subunit beta type-2 (PSMB2) belongs to the proteasome T1B family, which is a 20S core beta subunit. The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. A crucial function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB2 is up-regulated in ovarian cancer cell lines.

WWOX is a proapoptotic protein and a tumor suppressor protein. WWOX is found in all eukaryotes and involved in the regulation of a broad range of cellular functions such as protein degradation, transcription, and RNA splicing. WWOX functions synergistically with TP53/p53 to control genotoxic stress-induced cell death. WWOX takes part in tumor necrosis factor (TNF)-mediated cell death. Loss of WWOX expression is associated with pancreatobiliary cancers. Reduced expression levels of WWOX protein is associated with the pathogenesis of basal-like differentiation in breast cancer. Loss of WWOX expression is associated with extrahepatic cholangiocarcinoma. WWOX gene alteration is an early genetic alteration contributes to oral carcinogenesis. WWOX induces apoptosis and inhibits human hepatocellular carcinoma cell growth through a mechanism enhanced by JNK inhibition.

Insulin-Degrading Enzyme (IDE) is a zinc metallopeptidase which degrades intracellular insulin, and thus terminates insulins activity, as well as playing a part in intercellular peptide signaling by degrading various peptides such as amylin, bradykinin, and kallidin. The preferential affinity of the IDE enzyme for insulin results in insulin-mediated inhibition of the degradation of additional peptides such as beta-amyloid. Deficiencies in IDE protein's function are linked with Alzheimer's disease and type 2 diabetes mellitus nevertheless mutations in the IDE gene have not been demonstrated to be causative for these diseases. Insulin-Degrading Enzyme localizes mainly to the cytoplasm however in some cell types it localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. In addition, IDE degrades amyloid formed by APP and IAPP. Furthermore, IDE plays a part in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

HEXA is the alpha subunit of the lysosomal enzyme beta-hexosaminidase which, combined with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules having N-acetyl hexosamines terminus. The two subunits composing Beta-hexosaminidase, alpha and beta, belong to the glycosyl hydrolases family and are encoded by distinct genes. Alpha subunit gene mutations can cause Tay-Sachs disease (GM2-gangliosidosis type I).

AKR1B10 efficiently reduces aliphatic and aromatic aldehydes, and it is less active on hexoses. AKR1B10 is highly expressed in adrenal gland, small intestine, and colon, and may play an important role in liver carcinogenesis. AKR1B10 is a monomeric protein that competently catalyzes the reduction of aromatic and aliphatic aldehydes and ketones. AKR1B10 is widely expressed in numerous human tissues, small intestine, colon and adrenal gland. AKR1B10 is pathogenically involved in diabetic complications and is overexpressed in human tumors, such as liver, breast, and lung cancer, AKR1B10 is involved in the development and progression of cancer.

Arsenic Methyltransferase (AS3MT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to trivalent arsenical and may have a role in arsenic metabolism. AS3MT methylates arsenite to produce methylarsonate, Me-AsO3H2, which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite which is also a substrate, is transformed into the much less toxic complex dimethylarsinate (cacodylate), Me2As(O)-OH.

LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.

DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
Beta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.