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MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.

ME2 catalyzes the oxidative decarboxylation of malate to pyruvate, malat + NAD(P)+? pyruvate + CO2 + NAD(P)H+, and is found both in eukaryotic and prokaryotic cells. Three different isoforms of ME are known to be in mammalian tissues: a strictly cytosolic NADP+-dependent enzyme, an NADP+-dependent mitochondriail isoform, and a mitochondrial isoenzyme that is able to use both NAD+ and NADP+ but is more effective with NAD+. The mammalian isoforms size is about 62-64 kDa. A native size of 240,000 Da proposes a tetrameric structure for the active enzyme.
Mitochondrial NAD+-dependent ME 2 activity is seen in tissues that experience many cell divisions, like spleen, thymus, and the basal cells of the small intestinal mucosa. ME2 is also expressed all through the rapid cleavage stages of early Xenopus development. Activity for this isoform is low or nonexistent in brain, muscle, and normal and regenerating liver tissue from rat but was observed in rat adrenal cortex, pigeon and human skeletal muscle, and in heart muscle of some species. In addition, it is expressed in mitochondria of all tumor cells inspected to detain ascites tumors, hepatoma cells, and a variety of other tumors and transformed cell lines.

Mediator Complex Subunit 20 (MED20) is a subunit of the Mediator complex, which is a multiprotein coactivator of RNA transcription that interacts with DNA-bound transcriptional activators, RNA polymerase II, and general initiation factors. The Mediator functions as a link to transmit information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. Mediator is recruited to promoters by direct interactions with regulatory proteins and functions as a scaffold for the compilation of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

Ribosomes, the organelles which catalyze protein synthesis, contain a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and nearly 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein which is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, is a member of the L12P family of ribosomal proteins and has a vital part in the elongation step of protein synthesis. In opposed to most ribosomal proteins, which are basic, the encoded protein is acidic.The P1 C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. P1 is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene distributed all over the genome.

MX2 is a member of 2 protein families: the dynamin family and the large GTPases family. MX2 has a cytoplasmic and nuclear structure which is found in a granular pattern in the heterochromatin region under the nuclear envelope. The nuclear form has a NLS (nuclear localization signal) at the amino terminal end however it is missing in the cytoplasmic form as a result of the use of a different translation start codon. MX2 is upregulated by IFN-a, but unlike myxovirus resistance protein 1 has no antiviral activity.

Osteopontin is a glycoprotein that was primarilyfound in osteoblasts and takes part in bone remodeling, immune functions in fibroblasts, macrophages, & lymphocytes during inflammation and wound healing. SPP1 highlybinds to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury through late preconditioning. Expression of Ostepontin and CD44 in hepatocellular carcinoma is linked to advanced tumor stage &leads to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.

U-snRNPs which are a pivotal part of spliceosomes, are created between small non-coding nuclear RNAs and a protein moiety. Whereas the 7 Sm proteins are conserved, the RNP antigens are exclusive for each U-snRNP subclass.

BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

PPP1CC is vital for cell division and takes part in the regulation of protein synthesis, muscle contractility and glycogen metabolism. Additionally, PPP1CC has a role in long-term synaptic plasticity and regulation of ionic conductance, and has a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.

Macrophage Colony Stimulating Factor (M CSF) or colony stimulating factor 1, is a cytokine, that promoted differentiation in hematopoietic stem cells to macrophages. Another role of M CSF is to bind to its receptor (colony stimulating factor 1 receptor) and to take part in placenta growth and development.

MUC16, aka CA125, is a mucin protein that might be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.
The CA125 molecule is heterogeneous with regard to both size and charge, almost certainly due to continuous deglycosylation of side chains during its life-span in bodily fluids.
MUC16 is most likely a glycoprotein with a predominance of O-linkages.

Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.

FABP7 is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are are inovlved in fatty acid uptake, transport, and metabolism. FABP7 is expressed in radial glia by the activation of Notch receptors and binds DHA with the highest affinity among all of FABPs. FABP7 plays an important role in transport of hydrophobic ligand with potential morphogenic activity during cns development. FABP7 is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (by similarity).

Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.

Protein Tyrosine Phosphatase Non Receptor Type-11 or PTPN11 has 2 Src homology 2 domains and part of the tyrosine phosphatase group of proteins. PTPN11 is responsible for the catalyzation of tyrosine residues dephosphorylation in proteins and takes part in the stimulation and activation of Erk/MAP kinase transduction via signals from tyrosine kinase. Noonan syndrome and acute myeloid leukemia can be caused from mutations in PTPN11.

Ribosomes, the organelles which catalyze protein synthesis, contain a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and nearly 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein which is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, is a member of the L12P family of ribosomal proteins and has a vital part in the elongation step of protein synthesis. In opposed to most ribosomal proteins, which are basic, the encoded protein is acidic.The P1 C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. P1 is located in the cytoplasm. Two alternatively spliced transcript variants which encode varies proteins have been detected. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene distributed all over the genome.

Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.

Diphthamide Biosynthesis 3 Pseudogene 1 also known as DPH3P1 may stand for a processed pseudogene of DPH3 since it lacks the exon/intron structurefound in the functional gene. Yet, DPH3P1 does contain an intact open reading frame, though its translation has not been established.

DPPA4 takes part in the conservation of active epigenetic status of target genes and prevents differentiation of embryonic cells into a primal ectoderm extraction.

EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.

FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.

Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.