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SORD enzyme is part of of the zinc-containing alcohol dehydrogenase family that is broadly expressed in kidney and in the lens eye. SORD enzymatically catalyzes the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses.

LYVE-1 has been identified as a major receptor for HA (extracellular matrix glycosaminoglycan hyaluronan) on the lymph vessel wall. The deduced amino acid sequence of LYVE-1 predicts a 322-residue type I integral membrane polypeptide 41% similar to the CD44 HA receptor with a 212-residue extracellular domain containing a single Link module the prototypic HA binding domain of the Link protein superfamily. Like CD44, the LYVE-1 molecule binds both soluble and immobilized HA. However, unlike CD44, the LYVE-1 molecule colocalizes with HA on the luminal face of the lymph vessel wall and is completely absent from blood vessels. Hence, LYVE-1 is the first lymph-specific HA receptor to be characterized and is a uniquely powerful marker for lymph vessels themselves.

ANPEP or aminopeptidase N, is an enzyme, found in the small-intestinal and renal microvillar membrane and other plasma membranes. The enzyme has a critical part in the digestion of peptides after their hydrolysis by gastric and pancreatic proteases. ANPEP is also part ofthe processing of different peptides as well as peptide hormones, neuropeptides & chemokines. The protein takes part in angiogenesis, enhancing cholesterol crystallization &amino acid transport by formatting with SLC6A19 transport protein and regulating its activity.

GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

17-beta-hydroxysteroid dehydrogenase 14 (HSD17B14) is a member of the 17-beta-HSD family of proteins, which regulate the availability of steroids within various tissues throughout the body. 17-beta-hydroxysteroid dehydrogenases (HSD17B14) are mainly involved in metabolism of steroids at the C17 position and also of other substrates, such as fatty acids, prostaglandins, and xenobiotics. HSD17B14 exists as a homotetramer that localizes to the cytoplasm and is highly expressed in the brain, placenta, liver and kidney.

Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.

HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

E3 ubiquitin-protein ligase SIAH1 (SIAH1) belongs to the SIAH (seven in absentia homolog) family. SIAH1 is a tumor suppressor protein, which is expressed in intestinal epithelium and activated during apoptosis. SIAH1 is involved in ubiquitination and proteasome-mediated degradation of specific proteins. SIAH1 is comprised of an N-terminal RING-finger domain (required for proteolysis) and a cystein-rich C-terminal domain (which regulates oligomerization and SIAH binding to target proteins). SIAH1 causes indirect degradation of beta-catenin by way of creation of a complex with Siah-interacting protein (SIP), Skp1 and Ebi.

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.

UBE2D3 enzymes are human homologs of the yeast UBC4/5 family and play many important regulatory roles in inflammation and cancer. UbcH5a mediates the degradation of a myriad of short-lived regulatory proteins (such as p53 in the presence of E6/E6-AP or MDM2, c-Fos, I?B?, p105) and abnormal proteins. UBE2D3 has 88% and 89% sequence identity with UbcH5a and UbcH5b respectively.

MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highy expressed in the adrenal system, small intestine, heart and pancreas.

Dimethylarginine dimethylaminohydrolase 1, is a part of the Dimethylarginine Dimethylaminohydrolase gene family. DDAH1 participates in nitric oxide generation by regulating cellular concentrations of methylarginines, that in turn inhibit nitric oxide synthase activity. Deficiency of DDAH1 results in ADMA (asymmetric dimethylarginine) increase and a decrease in cGMP generation.

DTD2 is e member of the DTD family. DTD2 protein hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) as a defense mechanism against a harmful effect of D-tyrosine.

Dual Specificity Phosphatase 26 (DUSP26) inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. DUSP26 also induces activation of MAP kinase p38 and c-Jun N-terminal kinase. DUSP26 inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a decrease in its DNA-binding activity.

7-methylguanosine phosphate-specific 5'-nucleotidase (NT5C3B) includes transferase activity and nucleotide binding. Among NT5C3B’s related super-pathways are adenosine nucleotides degradation II and Pyrimidine metabolism. NT5C3B hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP guards cells against undesired retrieval of m(7)GMP and its incorporation into nucleic acids. In addition, NT5C3B has weak activity for CMP.

Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.

GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

UCHL5 is a member of the peptidase C12 family. UCHL5 protein is a protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains, and deubiquitinating enzyme related to the 19S regulatory subunit of the 26S proteasome.

MMP-1 can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

MGMT is an enzyme that repairs O-6-methylguanine, a mutagenic DNA base damaged by endogenous and environmental alkylating agents and takes part in the cellular defense against the biological effects of O-6-methylguanine in DNA. MGMT repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. abnormal MGMT expression correlates with the prognosis in human solid cancers. MGMT decrease of expression is correlated with methylation. The human MGMT is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage. MGMT promoter hypermethylation plays an important role in the early steps of colorectal carcinogenesis. Abnormal promoter hypermethylation of MGMT gene is associated with oral squamous cell carcinomas.

Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in DOPA synthesis.

Glutamate dehydrogenase 1, mitochondrial precursor (GLUD1) is a member of the Glu/Leu/Phe/Val dehydrogenases family. GLUD1 is a mitochondrial glutamate dehydrogenase, which converts L-glutamate into alpha-ketoglutarate. GLUD1 has a pivotal role in nitrogen metabolism in plants and animals. GLUD1 is observed in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate. The GLUD1 enzyme has a vital role in regulating amino acid induced insulin secretion. GLUD1 gene mutations cause hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 enzyme is allosterically activated by ADP and inhibited by GTP and ATP.

Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.