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SUMO1 is a protein that belongs to the SUMO (small ubiquitin-like modifier) protein family. SUMO1 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. Still, unlike ubiquitin which targets proteins for degradation, SUMO1 is involved in a variety of cellular processes, for example nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO1 is not active until the last four amino acids of the carboxy-terminus are cleaved off.

MMP-1 (interstitial collagenase) 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, IGFBP-3, IGFBP-5, casein, gelatin, 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.

SNURF is an extremely basic protein restricted to the nucleus. The evolutionarily reserved open reading frame is located on a bicistronic transcript which has a downstream ORF encoding the small nuclear ribonucleoprotein polypeptide N. The first three exons of the transcript are exploited by the upstream coding region which is known as an imprinting center. The full-length nature of these transcripts is yet to be determined but multiple transcription initiation sites have been identified and large scale alternative splicing takes place in the 5' untranslated region. An alternate exon which substitutes for exon 4 and leads to a truncated, monocistronic transcript was identified. Deletion or alternative splicing produced by a translocation event in the 5' UTR or coding region of this gene results in Prader-Willi syndrome or Angelman syndrome because of parental imprint switch failure.

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.

IMPDH2 is a member of the IMPDH/GMPR family. IMPDH2 catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is afterward converted into guanosine-5'-monophosphate. IMPDH2 is the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. IMPDH2 is consequently involved in maintaining cellular guanine deoxy- and ribonucleotide pools required for DNA and RNA synthesis. In addition, IMPDH1 and IMPDH2 are targets for the important immunosuppressive drug, MPA. Furthermore, the IMPDH2 gene is up-regulated in some neoplasms, suggesting it may have a role in malignant transformation.

PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

UNG is a member of the Uracil-DNA glycosylase family. One of his functions is to prevent mutagenesis by eliminating uracil from DNAmolecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil basesare formed as a result of cytosine deamination or misincorporation of dUMP residues. After a mutation is formed, the mutagenicthreat of uracil propagates through any subsequent DNA replication steps. Among the diseases associated with UNG are: congenital rubella, and immunodeficiency with hyper igm type 4.

ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

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.

The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.

General control of amino acid synthesis protein 5 like 2 (KAT2A) is a member of the GCN5 family. KAT2A functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. KAT2A interacts with Ku70, TAF9, transcription initiation protein SPT3 homolog, TADA2L, Ku80 and DDB1.

Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.

Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.

UBE2D1 is a member of the ubiquitin-conjugating enzyme family. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2D1 is strongly related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. In addition, UBE2D1 functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.

Phosphoribosyltransferase domain-containing protein 1 (PRTFDC1) is a member of the purine/pyrimidine phosphoribosyltransferase family. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro). PRTFDC1 can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). PRTFDC1 is not expected to impact purine metabolism or GMP salvage.

Phosphoserine aminotransferase (PSAT1) catalyzes the conversion of 3-phosphohydroxypyruvate into 3-phosphoserine which is dephosphorylated consequently by phosphoserine phosphatase to form L-serine. PSAT1 is probably a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila. PSAT1 is expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon. Defects in the PSAT1 gene are the cause of phosphoserine aminotransferase deficiency (PSATD). PSATD is distinguished biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.

PTGES3 takes part as a cochaperone and is involved in signal transduction.
PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.

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.

REV1 Polymerase (REV1) contains a BRCT domain, which is imperative in protein-protein interactions. REV1 is a deoxycytidyl transferase involved in DNA repair. REV1 assists in the 1st step in the bypass of abasic lesions by the incorporation of a nucleotide opposite the lesion. REV1 is essential for normal generation of mutations by physical and chemical agents. REV1 transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. A role for the human Rev1-like protein has been suggested as a scaffold which recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA.

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described.
Protein phosphatase 2C(PP2C?) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.

D-amino-acid oxidase or DAAO is an enzyme that oxidizes D-amino acids to their imino acids form while using FAD (flavin adenine dinucleotide) as a co-factor, resulting in the formation of ammonia & hydrogen peroxide. the enzyme may take part in keeping the balance of acid base in the kidney tissue. Another role is to detoxifying molecules that abolish D-amino acids aggregated while the cell ages.