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PNMT is an enzyme located in the adrenal medulla and it catalyzes the final step of the catecholamine biosynthesis pathway, which methylates norepinephrine to form epinephrine (adrenaline). PNMT has beta-carboline 2N-methyltransferase activity. PNMT takes part in regulating epinephrine production. Glucocorticoid receptors form multimers of PNMT independent of the DNA binding domain. PNMT expression is regulated late in mouse gestation by AP2-alpha and glucocorticoids.

PNMT is an enzyme located in the adrenal medulla and it catalyzes the final step of the catecholamine biosynthesis pathway. PNMT has beta-carboline 2N-methyltransferase activity. PNMT takes part in regulating epinephrine production. Glucocorticoid receptors form multimers of PNMT independent of the DNA binding domain. PNMT expression is regulated late in mouse gestation by AP2-alpha and glucocorticoids.

Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.

PNP is a member of the PNP/MTAP phosphorylase family of proteins. PNP catalyzes the reversible phosphorolysis of ribonucleosides and 2’-deoxyribonucleosides with specificity for guanine, hypoxanthine and their analogs. PNP deficiency is a rare autosomal recessive genetic disease linked to a severe defect in T-lymphocyte function and neurologic disorder in children, comprising four percent of combined immunodeficiency cases.

PNPLA2 is an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue. Mutations in the PNPLA2 gene are linked to neutral lipid storage disease with myopathy.

Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.

Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.

Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

Proline-Rich Nuclear Receptor Coactivator 2 (PNRC2) takes part in controlling the energy balance between energy storage and energy expenditure. PNRC2 is involved in nonsense-mediated mRNA decay (NMD) by operating as a bridge between the mRNA decapping complex and the NMD machinery. PNRC2 is needed for UPF1/RENT1 localization to the P-body and also plays a role as a nuclear receptor coactivator.

Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.

Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.

GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.

POGLUT1 is a homologue of Rumi from Drosophila, an endoplasmic reticulum (ER)-retaining glucosyltransferase which catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats on the consensus sequence C-X-S-X-P-C. POGLUT1 positively regulates Notch signaling without affecting Notch ligand binding.

DNA polymerase beta (POLB) is a member of the DNA polymerase type-X family. In eukaryotic cells, POLB performs base excision repair necessary for DNA maintenance, replication, recombination, and drug resistance. POLB has 2 separate domains; the larger is the polymerase domain itself, whereas a small basic N-terminal domain contains an AP lyase activity which excises the abasic sugar-phosphate residue at the strand break. POLB fills single nucleotide gaps in DNA produced by the base excision repair pathway of mammalian cells. POLB overexpression, as seen in some human tumors, could convene an increase in spontaneous mutagenesis.

Phl p 7.0101 is a secondary allergen of timothy grass pollen, which is non-glycosylated protein. Grass pollen-sensitized individuals show IgE antibodies in their blood system. Phl p 7.0101 is a calcium binding protein with similar sequence to pollen antigens that exist in different plants, hence, cross-reactions are possible.

Polymerase Delta 4 also known as POLD4 is the smallest subunit of DNA polymerase delta. DNA polymerase delta which takes a vital part in DNA replication and repair possesses both polymerase and 3' to 5' exonuclease activity. POLD4 increases the activity of DNA polymerase delta and takes a part in fork repair and stabilization during interactions with the DNA helicase Bloom syndrome protein. POLD4 contributes to PCNA-dependent activity of DNA polymerase delta.

Polymerase (DNA Directed), Epsilon 3, also know as POLE3, is a histone-fold protein which interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers merge into larger enzymatic complexes for DNA transcription, replication, and packaging.

DNA polymerase POLL is involved in base excision repair (BER). POLL is a low-fidelity polymerase that takes part in both spontaneous and DNA damage-induced mutagenesis. Furthermore, POLL takes part in the mutagenic bypass of T-T dimers. Pol lambda possesses terminal transferase and 5’-deoxyribose-5-phosphate lyase activity which is synchronized by PCNA and replication protein A.

Polymerase (RNA) I (DNA directed) Polypeptide C (POLR1C) is a subunit of both RNA polymerase I and RNA polymerase III complexes whose defects are related with Collins syndrome. POLR1C is a protein-coding gene and is part of the Pol core element

Polymerase (RNA) II (DNA directed) Polypeptide C (POLR2C) is the 3rd largest subunit of RNA polymerase II. The product of POLR2C consists of a cysteine rich area and exists as a heterodimer with an additional polymerase subunit, POLR2J. Those 2 subunits shape a core subassembly unit of the polymerase.

Polymerase II Polypeptide D (POLR2D) is a member of the eukaryotic RPB4 RNA polymerase subunit family. POLR2D is the fourth largest subunit of RNA polymerase II. Pol II is the main element of the basal RNA polymerase II transcription machinery. polymerase is responsible forsynthesizing messenger RNA in eukaryotes. In yeast, POLR2D subunit is connected with the polymeraseunder suboptimal growth conditions and might have a stress protective role. POLR2D catalyzes the transcription of DNA into RNA by the 4 ribonucleoside triphosphates as substrates.

DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E) is a member of the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family. POLR2E being a DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. POLR2E is the 5th largest subunit of RNA polymerase II (the polymerase which is responsible for synthesizing messenger RNA in eukaryotes). The POLR2E subunit is shared by the other 2 DNA-directed RNA polymerases and is present in two-fold molar excess over the other polymerase subunits. An interaction between the POLR2E subunit and a hepatitis virus transactivating protein has been established, suggesting that an interaction between transcriptional activators and the polymerase can occur through the POLR2E subunit.

Polymerase II Polypeptide F (POLR2F) is the 6th largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes, which is also shared by the other two DNA-directed RNA polymerases. In yeast, POLR2F, in combination with at least 2 other subunits, forms a structure which stabilizes the transcribing polymerase on the DNA template. DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA via the 4 ribonucleoside triphosphates as substrates. Pol II is the principal element of the basal RNA polymerase II transcription apparatus. Pols are comprised of mobile elements which move close to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and along with parts of RPB1 and RPB2 constructs a compartment to which the RPB4-RPB7 subcomplex attaches.

POLR2H is an essential and highly conserved subunit of RNA polymerase II which is shared by the other 2 eukaryotic DNA-directed RNA polymerases, I and III. The three eukaryotic RNA polymerases are complex multisubunit enzymes which play a vital role in the transcription of nuclear genes. POLR2H encodes an essential and highly conserved subunit of RNA polymerase II which is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III.

Polymerase II Polypeptide I (POLR2I) is a member of the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family. POLR2I is a subunit of RNA polymerase II, which is a polymerase responsible for synthesizing messenger RNA in eukaryotes. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. In addition POLR2I synthesizes mRNA precursors and numerous functional non-coding RNAs.

Polymerase (RNA) II (DNA directed) Polypeptide J (POLR2J) is a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The POLR2J protein occurs as a heterodimer with another polymerase subunit; together they develop a core subassembly unit of the polymerase. POLR2J is ubiquitously expressed, having a high expression in the heart and skeletal muscle.

POLR2J2 belongs to the RNA polymerase II subunit 11 gene family, that includes 3 genes in a cluster on chromosome 7q22.1 and a pseudogene on chromosome 7p13. DNA directed RNA polymerase II polypeptide J family encodes a subunit of RNA polymerase II, the polymerase which is responsible for synthesizing messenger RNA in eukaryotes. This locus produces multiple, otherwise spliced transcripts which express isoforms with distinct C-termini compared to DNA directed RNA polymerase II polypeptide J. Most or all variants are spliced to include additional non-coding exons at the 3' end that makes them candidates for nonsense-mediated decay (NMD). Therefore, it is unknown if this locus expresses a protein or proteins in vivo.

DNA-directed RNA polymerase II subunit RPB11-b2 (POLR2J3) is a member of the eukaryotic RPB11 RNA polymerase subunit family. POLR2J (DNA-directed RNA polymerase II subunit J) exists in 3 variants POLR2J1 (RPB11-a), POLR2J2 (RPB11-b1), and POLR2J3 (RPB11-b2). POLR2J3 is a DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Polymerase (RNA) II (DNA directed) Polypeptide K, also knownas POLR2K is am ember of the archaeal RpoP/eukaryotic RPC10 RNA polymerase subunit family. POLR2K is one of the smallest subunits of RNA polymerase II, the polymerase is responsible for synthesizing messenger RNA in eukaryotes. In addition, the other two DNA-directed RNA polymerases share this subunit.

Polymerase III Polypeptide F (POLR3F) is a member of the eukaryotic RPC34/RPC39 RNA polymerase subunit family. POLR3F is DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. POLR3F is one of many subunits forming eukaryotic RNA polymerase III (RNA Pol III), which transcribes 5S ribosomal RNA and tRNA genes. POLR3F binds both TFIIIB90 and TBP, 2 subunits of RNA polymerase III transcription initiation factor IIIB (TFIIIB).

Polymerase (RNA) III (DNA directed) Polypeptide H(POLR3H) is a member of the eukaryotic RPB7/RPC8 RNA polymerase subunit family. POLR3H is DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA utilizing the 4 ribonucleoside triphosphates as substrates. POLR3H has a central role in sensing and curbing infection by intracellular bacteria and DNA viruses. POLR3H functions as nuclear and cytosolic DNA sensor which is involved in innate immune response.

Polymerase III Polypeptide K, known as PORL3K, is a small vital subunit of RNA polymerase III. The carboxy-terminal domain of PORL3K owns a sequence which is very similar to the carboxy-terminal domain of an RNA polymerase II elongation factor. PORL3K takes part in sensing and limiting infection by intracellular bacteria and DNA viruses. PORL3K is also plays a role as nuclear and cytosolic DNA sensor which takes part in the innate immune response.

Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.

POM121 And ZP3 Fusion (POMZP3) is a DNA sequences derived from two distinct loci, particularly through the duplication of 2 internal exons from the POMZP3 gene and 4 3' exons from the ZP3 gene. POMZP3 is a protein-coding gene which lacks the nuclear pore localization motif.

Paraoxonase 1 also called Esterase-A is involved in the detoxification of organophosphate insecticides such as parathion. Paraoxonase 1 may also confer protection against coronary artery disease by destroying proinflammatory oxidized lipids present in oxidized low-density lipoproteins (LDLs).

Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.

Paraoxonase 2 (PON2) is a member of a multigene family whose genes share 65% identity at the amino acid level, and is expressed in a variety of tissues, including the pancreas. PON2 overexpression has been shown to lower the intracellular oxidative state and reduce the cells ability to oxidize LDL. PON2 is therefore implicated in the modulation of oxidative stress.

Processing of Precursor 4 (POP4) is a member of the eukaryotic/archaeal RNase P protein component 1 family. POP4 is one of the protein subunits of the small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. POP4 is confined to the nucleus and associates promptly with the RNA component of this complexes.POP4 is participating in processing of precursor RNAs.

Processing Of Precursor 7, also known as POP7, is a part of the histone-like Alba family. POP7 is a part of ribonuclease P which is a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. POP7 is also a part of RNase MRP complex, which cleaves pre-rRNA sequences.

P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.

P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.

POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.

POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.

POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.

POU6F1 is a member of the POU transcription factor family. POU6F1 is transcription factor that binds favorably to a variant of the octamer motif (5'-ATGATAAT-3'). POU6F1 is exclusively expressed in the embryo in the developing brain, however in the adult its expression is confined to the brain, heart, skeletal muscle and lung. In the brain, the highest expression levels are found in specific cell layers of the cortex, the olfactory bulb, the hippocampus and the cerebellum.