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Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8.

Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

MALD3 (a non-specific lipid transfer protein) is a major apple allergen. LTPs are found mainly in aerial plant organs such as leaves, seeds, flowers, and fruit. MALD3 is a heat-stable protein which is characterized by having resistance to pepsin hydrolysis.

Gamma-glutamylaminecyclotransferase (A2LD1) is an enzyme which converts gamma-glutamylamines to free amines and 5-oxoproline. A2LD1 demonstrates high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. A2LD1 assists in the proteolytic degradation of crosslinked fibrin by breaking down isodipeptide L-gamma-glutamyl-L-epsilon-lysine, which is a byproduct of fibrin degradation. The reaction catalyzed by the A2LD1 produces 5-oxo-L-proline and a free alkylamine.

HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures.

This gene is a member of the ADAR (adenosine deaminase acting on RNA) family. Using site-specific adenosine modification, proteins encoded by these genes participate in the pre-mRNA editing of nuclear transcripts. The protein encoded by this gene, tRNA-specific adenosine deaminase 1, is responsible for the deamination of adenosine 37 to inosine in eukaryotic tRNA.

DECR1 is a mitochondrial protein which exists as a homotetramer and is a member of a family of short-chain dehydrogenases/reductases. DECR1 acts as an auxiliary enzyme of beta-oxidation andt partakes in the metabolism of unsaturated fatty enoyl-CoA esters. in particular, DECR1 uses NADP+ to catalyze the reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA that can subsequently be used as an intermediate in the Krebs cycle. Furthermore, DECR1 is believed to work as a tumor suppressor, possibly downregulating the expression of Neu and slowing the rate of tumorigenesis.

4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.

BTLA, also known as B And T Lymphocyte Associated, is an inhibitory molecule which is part of the Ig superfamily. BTLA is a type 1 transmembrane glycoprotein in the CD28 family of T cell costimulatory molecules. BTLA is a 3rd inhibitory receptor on T lymphocytes with resemblances to CTLA-4 & PD-1. Moreover, BTLA is a ligand for TNF (receptor) superfamily, TNFRSF14, and HVEM. BTLA-HVEM complexes negatively regulate T-cell immune responses.

PDXK converts vitamin B6 to Pyridoxal-5-phosphate (PLP), which is a vital cofactor in the intermediate metabolism of amino acids and neurotransmitters. PDXK is cytoplasmic and probably acts as a homodimer. The biological validity of the alternatively spliced transcript variants has not been determined.

Pyridoxal phosphate phosphatase PHOSPHO2, orphan 2 (PHOSPHO2) is a member of the haloacid dehalogenase (HAD) superfamily. Phosphatase has an elevated activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). PHOSPHO 1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralizing cells and is believed to be implicated in the production of inorganic phosphate for bone mineralization. PHOSPHO2 is a recognized phosphatase sharing a 42% sequence identity with PHOSPHO1. PHOSPHO1 and PHOSPHO2 are especially similar, however surprisingly recombinant PHOSPHO2 hydrolyses phosphoethanolamine and phosphocholine comparatively inadequately.

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.

Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.

Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.

GMPR2 is the single known metabolic step by which guanine nucleotides can be transformed to the pivotal precursor of both adenine and guanine nucleotides. GMPR2 catalyzes the permanent NADPH-dependent reductive deamination of GMP to IMP, and is involved in re-utilization of free intracellular bases and purine nucleosides.

Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity, but not heparin.

GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.

GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

Prostaglandin-H2 D-isomerase (PTGDS) is a glutathione-independent prostaglandin D synthase which catalyzes the conversion of prostaglandin H2 (PGH2) to postaglandin D2 (PGD2). PTGDS is may have vital roles in both maturation and maintenance of the central nervous system and male reproductive system. PTGDS is the most abundant protein in the cerebral spinal fluid and recent evidence suggests that PTGDS acts as a beta-amyloid chaperone and may play a role in the deposition of Ab plaques in Alzheimer’s disease.

ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.