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GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

MMADHC is a mitochondrial protein which takes part in an early step of vitamin B1 2 metabolism. Vitamin B12 (cobalamin) is vital for regular development and existence in humans. Mutations in MMADHC can result in methylmalonic aciduria and homocystinuria type cblD, a cobalamin metabolism syndrome which is characterized by decreased levels of the coenzymes methylcobalamin and adenosylcobalamin.

Annexin A13 (ANXA13) belongs to the annexin protein family, whose members play a role in cytoskeletal interactions, phospholipase inhibition, regulation of cellular growth, and intracellular signal transduction pathways. ANXA13 is believed to be the original originator of the 12 members of vertebrate annexins. ANXA13 expression is decidedly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is linked with a highly differentiated intracellular transport function.

ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.

L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.

PRDX5 belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides with reducing equivalents supplied through the thioredoxin system. PRDX5 has an antioxidant protective function in different tissues under normal conditions and during inflammatory processes. Peroxiredoxin-5 interacts with peroxisome receptor 1 and is involved in intracellular redox signaling. PRDX5 is involved in intracellular redox signaling. Peroxiredoxin-5 is a significant antioxidant protein of lung epithelial cells for its expression in the human lung increases during inflammation. PRDX5 expression is upregulated in osteoarthritis. PRDX5 may be significant in mitochondrial genome stability. Peroxiredoxin-5 has a protective role in human tendon cells against oxidative stress by reducing apoptosis and upholding collagen synthesis.

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.

GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.

Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Amelogenin, X-Linked (AMELX) belongs to the amelogenin family of extracellular matrix proteins. Amelogenins have a role biomineralization during tooth enamel development. AMELX gene mutations cause X-linked amelogenesis imperfecta. AMELX regulates the formation of crystallites during the secretory stage of tooth enamel development. AMELX is transiently but amply expressed by ameloblasts during tooth development. Amelogenin is the principal protein in developing dental enamel.

SNX1 belongs to the large family of hydrophilic proteins that interact with a range of receptor types that participate in intracellular trafficking. SNX1 and the associated splice variant, SNX1A, bind the EGFR, enable its transport to the lysosome, and thus contribute to the degradation of the receptor. SNX1 is related with cellular membranes, and they, also, associate with EGF, PDGF and the receptor tyrosine kinases.

GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 participates in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.

Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.

Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.

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GLIPR2 is linked to plant pathogenesis-related (PR-1) proteins, which are upregulated in reaction to pathogen attack. GLIPR2 is localized within lipid-enriched microdomains on the cytosolic side of the endomembrane system. GLIPR2 is closely attached to membranes and lacks the cytosol, though it lacks a membrane-spanning domain.

Alanine transaminase or ALT is a transaminaseenzyme.
ALT is found in serumand in various bodily tissues, but is most commonly associated with the liver; It catalyzes the transfer of an aminogroup from alanineto a-ketoglutarate, the products of this reversible transaminationreaction being pyruvateand glutamatealanine+ a-ketoglutarate= pyruvate+ glutamate
It is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. It is also called serum glutamate pyruvate transaminase (SGPT) or alanine aminotransferase (ALAT). Diagnostically, it is almost always measured in units/litre (U/L).

Alpha-galactosidase A (GLA) is a homodimeric glycoprotein which hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. GLA catalyzes the hydrolysis of melibiose into galactose and glucose. Various mutations in the GLA gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease (a rare lysosomal storage disorder which results from a failure to catabolize alpha-D-galactosyl glycolipid moieties).

GPD2 (Mitochondrial glycerol-3-phosphate dehydrogenase) is a Ca2+-sensitive, FAD-binding protein, which is located on the outer surface of the inner mitochondrial membrane. Two isoforms have been identified for mGPD: Isoform 1 is comprised of 727 a.a. residues, while isoform 2 lacks 126 a.a. residues of the N-terminus. GPD2 catalyses the oxidation of glycerol-3-phosphate to DHAP (dihydroxyacetone phosphate) with associated reduction of the enzyme-bound FAD. GPD2 is a testis-specific promoter of mitochondrial GPDH. GPD2 along with a cytosolic NAD-linked GPD forms the glycerol phosphate shuttle that uses the interconversion of G-3-P and DHAP to transfer reducing equivalents into mitochondria, which results in the reoxidation of NADH produced during glycolysis.
GPD2 deficiency contributes to the impairment of glucose-stimulated INS discharge in a number of animal models of non-INS dependent diabetes mellitus. GPD2 up-regulation as a result of a highly glycolytic environment contributes to the general increase in ROS generation and may lead to the progression of prostate cancer.

GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.