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HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.

SecB, a significant chaperone that takes part in protein export, binds various ligands rapidly with high affinity and low specificity. SecB plays an important role during protein export through the general secretory pathway by modulating the partitioning of precursors between folding or aggregation and delivery to the membrane-bound translocation apparatus. SecB has the potential to take part in functions outside of export acting as a universal nonspecific chaperone to provide buffering capacity of the nonnative state of proteins in the cytosolic pool.

RAP2A belongs to the RAS oncogene family and a Ras-like small G protein. The RAP2A protein shares 60% identity with Rap1A and exhibits a carboxy-terminal CAAX motif and 2 upstream cysteines similar to those of the H-Ras, K-Ras and N-Ras proteins. In contrast with Rap1A and Rap1B, overexpression of RAP2A doesn’t obstruct the Ras signaling pathway.

VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.

CRAHSP1 is a serine phosphoprotein initially identified as a physiological substrate for the Ca2+-calmodulin regulated protein phosphatase calcineurin (PP2B). CRAHSP1 interacts with the STYX/dead phosphate protein in developing spermatids and is a paralog of the brain-specific mRNA-binding protein PIPPIN. It is believed to have a common role in calcium-mediated signal transduction resulting from phosphorylation on serine residues.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

Docking Protein 4(DOK4) is a member of the DOK family. DOK proteins are enzymatically inert adaptor or scaffolding proteins. The DOK proteins present a docking platform for the compilation of multimolecular signaling complexes. DOK4 serves in RET-mediated neurite outgrowth and has a positive role in activation of the MAP kinase pathway. DOK4 is a putative link with downstream effectors of RET in neuronal differentiation. DOK4 is involved in the regulation of the immune response induced by T-cells.

tRNA wybutosine-synthesizing protein 5 (TYW5) functions as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position closest to the anticodon of eukaryotic phenylalanine tRNA. TYW5 catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW). OHyW is a derivative of wybutosine observed in higher eukaryotes.

RANBP1 is a member of a family of proteins which bind Ran GTPase. Ran GTPase is vital for cell cycle control, mRNA processing, nuclear transport, mitotic spindle assembly, and postmitotic nuclear re-assembly and nuclear architecture maintenance. RANBP1 does not stimulate GTPase activity of RAN however RANBP1 does distinctly raise GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). Additionally, RANBP1 operates as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.

Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.

SURF1 plays a role in the biogenesis of the COX complex. SURF1 is found in the inner mitochondrial membrane and takes part in the biogenesis of the cytochrome c oxidase complex. SURF1 is shares a bidirectional promoter with SURF2 on the opposite strand. Defects in this SURF1 cause Leigh syndrome, a rigorous neurological disorder that is generally associated with systemic cytochrome c oxidase deficiency.

Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.

Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.

Cullin1, is an essential component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, that facilitate the ubiquitination of proteins which take part in cell cycle progression, signal transduction and transcription. In the SCF complex. Cullin1 assists in a rigid scaffold which organizes the SKP1-F-box protein and RBX1 subunits. Cullin1 contributes to catalysis by positioning of the substrate and the ubiquitin-conjugating enzyme.

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.

Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.

Non-Metastatic Cells 2 or NME2, is a protein, that acts as a nucleoside diphosphate kinase. This protein is of a heterodimeric structure and has 152 aa A & B polypeptide chains that builds the whole protein. Erythrocyte NDP kinase beta subunit has an identical structure to NME2. NDP kinases linked to nucleoside triphosphates synthesis and it appears as though NME2 takes part in regulating signal transduction.

Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).

Cofilin is a family of actin-binding proteins which disassembles actin filaments. It is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.

Kelch Domain Containing 8B, also known as KLHDC8B shapes a distinct beta-propeller protein structure of kelch domains which allow for protein-protein interactions. In addition,mutations in KLHDC8B have been connected with Hodgkin lymphoma.

RAN is a GTP-binding protein that participates in nucleocytoplasmic transport. RAN is necessary for the import of protein into the nucleus and also for RNA export. RAN takes part in chromatin condensation and control of cell cycle. The RAN complex with BIRC5 participates in mitotic spindle formation by being as a physical scaffold to assist the delivery of the RAN effector molecule TPX2 to microtubules. RUN increases AR-mediated transactivation.

RAB11A is part of the small GTPase superfamily, Rab family. RAB11A is related with both constitutive and regulated secretory pathways, and takes part in protein transport. RAB11A is a well-known marker for protein trafficking, sorting, and recycling in the endosomal pathway. RAB11A is a main regulator of membrane delivery during cytokinesis.

Dynein Axonemal Light Intermediate Chain1 also known as DNALI1 belongs to the inner dynein arm light chain family. DNALI1 take a dynamic role in flagellar motility. DNALI1 is the human homolog of the Chlamydomonas inner dynein arm gene, p28. The exactfunction of DNALI1 is not known yet, on the other hand, it is a potential candidate for immotile cilia syndrome. In addition it has been found that the following diseases: primary ciliary dyskinesia, and huntington's disease have been associated with DNALI1. Ultrastructural defects of the inner dynein arms are seen in patients with ICS. Immotile mutant strains ofChlamydomonas, biflagellated algae, show similar defects.