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PBX/Knotted 1 Homeobox 1 (PKNOX1) is a DNA-binding factor which takes part in the regulation of the transcriptional activity of AP-1 containing promoters. PKNOX1, which is also known as UEF3, PRP-1 and p64, is a Hmeobox protein. PKNOX1 forms stable complexes containing PBX proteins which synergize with AP-1 binding factors.

Human immunodeficiency virus (HIV) is a retrovirusthat can lead to a condition in which the immune systembegins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the humanimmune systemsuch as helper T cells(specifically CD4+ T cells), macrophagesand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosisin infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytesthat recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunityis lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genomeis converted to double-stranded DNAby a virally encoded reverse transcriptasethat is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integraseso that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latentand the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.

RCN1 is a calcium-binding protein which binds calcium and controls calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. RCN1 withholds six conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.
High conservation of amino acid residues outside of these motifs, in relation to mouse reticulocalbin, is consistent with a biochemical function further to that of calcium binding. In human endothelial and prostate cancer cell lines RCN1 protein is localized to the plasma membrane.

Human HSP40 (heat shock protein with molecular size of 40kDa) is one of the mammalian homologues of bacterial DnaJ heat shock protein and regulates cellular processes by aiding in the folding, transport and assembly. HSP40 protein contains the J-domain which controls interaction with the ATPase domain of DnaK.

SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.

CDKN1A holds a key part in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. When collaborating with CDK2 complexes, CDKN1A aids to prevent kinase activity and inhibits progression through G1/S. Nevertheless, CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D. CDKN1A is a vital intermediary by which p53/TP53 facilitates its part as an inhibitor of cellular proliferation as a reaction to DNA impairment.

Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

N-acetylneuraminate lyase (NanA) is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.

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.

Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

Protein Interacting with PRKCA 1, also known as PICK1 includes a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). PICK1 performs as an adaptor which binds to and arranges the subcellular localization of various membrane proteins. PICK1 interacts with multiple glutamate receptor subtypes, monoamine plasma membrane transporters, in addition to non-voltage gated sodium channels, and might target PRKCA to these membrane proteins and therefore regulates their distribution as well as function. PICK1 has also been found to perform as an anchoring protein which particularly targets PRKCA to mitochondria in a ligand-specific manner.

Cyclin-dependent kinase 1 (CDK1) plays a significant part in the control of the eukaryotic cell cycle through modulating the centrosome cycle in addition to mitotic onset; CDK1 promotes G2-M transition and regulates G1 progress and G1-S transition using association with multiple interphase cyclins. CDK1 is essential in higher cells for the entry into S-phase and mitosis.

Protein Kinase IFN Double Stranded RNA Activator, also known as PRKRA, mediates the effects of interferon when a viral infection takes place. PRKRA activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA) and leads to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Mutations in PRKRA are associated with dystonia.

DNAL4 is a member of the dynein light chain family. DNAL4 is a component of the dynein motor complex in cells that converts the chemical energy contained in ATP into the mechanical energy of movement. Dynein transports various cellular cargos by moving the length of cytoskeletal microtubules towards the minus-end of the microtubule, which is typically oriented towards the cell center.

PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

PDIA6 belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDIA6 functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6, also has a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

PPA2 shares great imagination with members of the inorganic pyrophosphatase (PPase) family. PPA2 is localized to the mitochondrion and owns the signature sequence necessary for the catalytic activity of PPase. PPases catalyze the hydrolysis of pyrophosphate to inorganic phosphate, which is vital for the phosphate metabolism of cells.

Protein Kinase, AMP-Activated, Alpha 1 (PRKAA1) is a protein coding gene which is the catalytic subunit of AMPK. AMPK is an energy sensor protein kinase which regulates cellular energy metabolism. AMPK adjusts the activity of various important metabolic enzymes by direct phosphorylation. Among its other features, AMPK protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.

Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.

Calponin 2 also known as CNN2 protein is capable of binding actin, calmodulin, troponin C, and tropomyosin, and also function in the structural organization of actin filaments. Furthermore, the interaction of CNN2 with actin inhibits the actomyosin Mg-ATPase activity. CNN2 takes part in smooth muscle contraction and cell adhesion. Two transcript variants encoding different isoforms have been found for this gene.