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D-gluconate kinase or idnk is a thermosensitive protein, consists of 187 a.a and part of the gluconokinase gntK/gntV protein family. Idnk enhances the conversion of ATP + D-gluconate => ADP + 6-phospho-D-gluconate. Idnk has a crucial part in determination of gender, removal of a certain portion of 9p may result in the making of male to female (reversal of sex), that leads to a female that has the genotype of male X, Y.

PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis RRM2 is regulated in a cell-cycle dependent method. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RRM2 Inhibits Wnt signaling.

Acyl-protein thioesterase 2 (LYPLA2) is lysophospholipase which acts on biological membranes to regulate the multifunctional lysophospholipids. LYPLA2 may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS.

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.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

Glutamate Decarboxylase 1 (GAD1) is one of several forms of glutamic acid decarboxylase. GAD1 is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for the GAD1 enzyme has been identified in the human pancreas since it has been detected as an autoantigen and an autoreactive T cell target type II diabetes. The GAD1 protein may also have a role in the stiff man syndrome. GAD1 enzyme deficiency leads to pyridoxine dependency with seizures. GAD1 also catalyzes the production of GABA.

GIMAP6 is a member of the GTPases of immunity-associated proteins (GIMAP) family. GIMAP proteins contain GTP-binding and coiled-coil motifs, and may play roles in the regulation of cell survival. Decreased expression of this gene may play a role in non-small cell lung cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, which is found in a cluster with seven additional GIMAP genes on the long arm of chromosome 7.

Alanyl-tRNA synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 108 kDa protein is an autoantigen recognized by PL-12 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop.

SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.

ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.

Peptidyl-tRNA hydrolase 2 (PTRH2) is a mitochondrial protein. PTRH2 is released during apoptosis from the mitochondria to the cytoplasm. When in the cytoplasm, PTRH2 regulates the function of 2 transcriptional regulators, TLE5 and TLE1, thus promoting caspase-independent cell death. Natural substrates for PTRH2 may be petidyl-tRNAs which drop off the ribosome during protein synthesis.

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.

Nicotinamide Nucleotide Adenylyltransferase 2, also known as NMNAT2 is a member of the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze a vital step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; NMNAT2 is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for NMNAT2. Among the diseases associated with NMNAT2 are tauopathy, and systemic lupus erythematosus.

SUMO-activating enzyme subunit 2 (UBA2) belongs to a family of small and related proteins which can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. UBA2 is conjugated to various molecules in the presence of the SAE1/UBA2 SUMO-activating(E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating(E2) enzyme. UBA2 represents a vital mechanism to protect neurons during episodes of cerebral ischemia.

Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

UCK2 is a member of the uridinekinase family. UCK2 catalyzes the phosphorylation of uridine monophosphate to uridine diphosphate and cytidine monophosphate. UCK2 has a part in the production of pyrimidine nucleoside triphosphates essential for RNA and DNA synthesis. Furthermore, an allele of this gene is an important player in mediating nonhumoral immunity to Hemophilus influenzae type B.

Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.

Rnase P protein, AKA rnpA, is an important enzyme consisting of the C5 protein (which encoded by rnpA) and the catalytic M1 RNA (encoded by rnpB) subunits. rnpA is ribonucleoprotein that catalyzes the removal of the 50- leader elements of precursor tRNAs and generates the mature 50-end of tRNAs. This step is critical for theformation of functional tRNA molecules in bacteria, archaea and eukarya. More importantly, it has lately been established that RNase P is essential for the endonucleolytic separation of certain polycistronic tRNA transcripts such as valV valW, leuQ leuP leuV and secG leuU. Therefore, it was hypothesized that the essential function of RNase P might be related to the complete absence of a particular tRNAthat was dependent on the enzyme for initial separation from polycistronic transcripts.

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.

Ectonucleoside Triphosphate Diphosphohydrolase 6 or ENTPD6 is an enzyme, akin to E-type nucleotidases. E-type nucleotidases, for instance CD39, are responsible for extracellular nucleotides catabolism. ENTPD6 has four apyrase-conserved areas like all to E-type nucleotidases. Rather spliced transcript agents that codes various isoforms were discovered for the DNA segment.

NT5C2 (NT5B/PNT5) has a vital role in the maintenance of purine/pyrimidine nucleotides. NT5C2 contains a phosphotransferase active site which catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. Furthermore, NT5C2 regulates the level of inosine monophosphate (IMP) and guanosine monophosphate (GMP) pools inside cells by way of hydrolysis.

IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.