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Interleukin-13 receptor subunit alpha-1 (IL13RA1) is a subunit of the interleukin 13 receptor. The IL13RA1 subunit forms a receptor complex with IL4 receptor alpha, which is a subunit shared by IL13 and IL4 receptors. IL13RA1 binds tyrosine kinase TYK2, and thus may mediate the signaling processes which leads to the activation of JAK1, STAT3 and STAT6 induced by IL13 and IL4. IL13RA1 is vital for allergen-induced airway hyperactivity and mucus hypersecretion.

IMP2 Inner Mitochondrial Membrane Peptidase-Like (IMMP2L) is implicated in processing the signal peptide sequences, IMMP2L is used to direct mitochondrial proteins to the mitochondria. IMMP2L resides in the mitochondria and is one of the essential proteins for the catalytic activity of the mitochondrial inner membrane peptidase (IMP) complex. Two variants which encode the same protein have been found for IMMP2L.

Impact RWD Domain Protein (IMPACT) is a member of the IMPACT family which is comprised of 1 RWD domain. IMPACT is a translational regulator which certifies constant high levels of translation under amino acid starvation. IMPACT interacts with GCN1/GCN1L1, thus preventing activation of GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation of protein synthesis. IMPACT is highly expressed especially in brain.

Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.

LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.

Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.

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.

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.

Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.

IRF5 belongs to the interferon regulatory factor (IRF) family, which is a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats.

CIB1 (Calcium and integrin binding 1) is regulatory protein with 50% homology to calmodulin and calcineurin B, that encodes a member of the calcium-binding protein family. CIB1 interacts with DNA-dependent protein kinase and may play a role in kinase-phosphatase regulation of DNA end joining. Also CIB1 is widely expressed and binds to a number of effectors, such as integrin αIIb, PAK1, and polo-like kinases, in different tissues.

Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.

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.

H1N1 is a subtype specie of Influenza A virus. H1N1 Influenza Virus has mutated into various strains such as the Spanish Flustrain, mild humanflu strains, endemic pigstrains, and various strains found in birds. The Influenza A Virus is a globular particle about 100nm in diameter, sheathed in a lipid bilayer derived from the plasma membrane of its host. Studded in the lipid bilayer are two integral membrane proteins some 500 molecules of hemagglutinin ("H") and some 100 molecules of neuraminidase ("N"). Within the lipid bilayer are 3000 molecules of matrix protein and 8 pieces of RNA. Each of the 8 RNA molecules is associated with many copies of a nucleoprotein, several molecules of the three subunits of its RNA polymerase some "non-structural" protein molecules of uncertain function.

TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.

ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.

IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

RTN4IP1 is a unique mitochondrial protein that interacts with reticulon 4, which is an effective inhibitor of regeneration ensuing spinal cord injury. The reticulon 4 interaction with mitochondrial proteins may offer insight into the mechanisms for reticulon-induced inhibition of neurite growth.

ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus.

S100A10 is a member of the S100 family of proteins contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A10 may function in exocytosis and endocytosis.