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Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

B2 microglobulin is an 11 kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. ?2 microglobulin associates with class I-like molecules such as CD1 and Qa as well as with the alpha chain of MHC class I molecules. Very limited amounts of MHC class I molecules can be found on the surface in the absence of ?2 microglobulin. CD8 T cells cannot develop in the absence of MHC class I.
Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinaemia, renal failure, or kidney transplants. Human Beta 2 microglobulin levels can rise either because its rate of synthesis has increased (e.g. in AIDS, malignant monoclonal plasma cell dyscrasia, solid tumors and autoimmune disease) or because of impaired renal filtration (e.g. due to renal insufficiency, graft rejection or nephrotoxicity induced by post-transplantation immunosuppressive therapy). Beta-2 microglobulin levels might also be elevated in multiple myeloma and lymphoma cases. Dialysis-related amyloidosis develops after a long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces.

BIN2, also known as Bridging Integrator 2, is a cytoplasmic protein. BIN2 comprises one BAR domain and Interacts with BIN1. BIN2 is highly expressed in some hematopoietic tissues, including peripheral blood, colon, thymus and placenta. BIN2 stimulates cell motility and migration, most likely through its interaction with the cell membrane and with podosome proteins which mediate interaction with the cytoskeleton and likewise modulates membrane curvature & mediates membrane tubulation.

BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.

Bone Morphogenetic protein Receptor-1B, also known as BMPR1B belongs to the TKL Ser/Thr protein kinase family. BMPR1Bis on ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate as well as activate type I receptors which autophosphorylate, afterward bind and activate SMAD transcriptional regulators. BMPR1B is receptor for BMP7/OP-1 as well as GDF5.

RGS2 belongs to the RGS family which are regulatory molecules that act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. RGS2 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits and as a result driving them into their inactive GDP-bound form.

PSMB10 is a member of the proteasome B-type family (T1B family) which is a 20S core beta subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. This core structure is comprised of four rings of 28 non-identical subunits; two rings are composed of seven alpha subunits and two rings are composed of seven beta subunits. Proteasomes are circulated in eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. A crucial function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB10 gene expression is induced by INFg, and it replaces catalytic subunit 2 (proteasome beta 7 subunit) in the immunoproteasome.

Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinasessuch as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.
The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that RasGTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK).
Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation.
Transgenic gene knockoutmice lacking MAPK1 have major defects in early development.

The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

Type 1 cystatins are also called stefins which function as intracellular thiol protease inhibitors. Cystatin-B protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. CSTB protein protects proteases leakage from lysosomes. Mutations in Stefin-B gene cause primary defects in patients with progressive myoclonic epilepsy (EPM1), a degenerative disease of the central nervous system. CSTB is overexpressed & elevated in the serum of HCC patients. Cystatin-B in vivo has a polymeric structure which is sensitive to the redox environment. Cystatin-B inhibits bone resorption by down-regulating intracellular cathepsin K activity despite increased osteoclast survival. Protein and mRNA levels of stefin B are significantly lower in atypical benign meningiomas. Stefins-A & Stefin-B which belong to the type-1 Cystatins, are up-regulated in lung tumours and thus able to counteract harmful tumour-associated proteolytic activity. Human stefin-A & Stefin-B form amyloid fibrils. Copper binding by stefin-B reduces amyloid fibril formation. A number of alternatively spliced CSTB isoforms were recognized in patients with progressive myoclonus epilepsy. Decreased CSTB activity in EPM1 pathogenesis is controled by cathepsins through increased activity of cathepsin-S & cathepsin-L.

S100B faintly binds calcium but binds zinc extremely strongly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. S100B binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction participates in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.

Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.

NCBP2 is a part of the nuclear cap-binding protein complex (CBC) that binds to the monomethylated 5'' cap of nascent pre-mRNA in the nucleoplasm. NCBP2 protein has an RNP domain usually located in RNA binding proteins, and contains the cap-binding activity. CBC promotes pre-mRNA splicing, 3''-end processing, RNA nuclear export, and nonsense-mediated mRNA decay.

Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

ARL4D is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). ARL4D takes part in membrane-associated intracellular trafficking. Mutations in this gene is linked to Bardet-Biedl syndrome (BBS).

EBAG9 is a type III transmembrane protein that is primarily located in the Golgi. EBAG9 is a tumor-associated antigen that is expressed at high frequency in a variety of cancers, such as advanced breast and prostate cancers. while the EBAG9 acts to inhibit the growth of receptor-binding cells and induced apoptosis of immune cells, cancer cells may evade immune surveillance. Thus immunodetection of EBAG9 expression can be a negative prognostic indicator. EBAG9 promotes progression of bladder cancer. In rheumatoid arthritis, the deficiency of EBAG9 induces CTL infiltration through failure to evade immune attack, therefore leading to apoptosis of the synovial lining cells. EBAG9 is involved in controlling exocytosis processes. EBAG9 expression plays a role in the progression of oral squamous cell carcinoma. EBAG9 plays a specific role in premature stages of breast carcinogenesis.

NDK (Nucleoside diphosphate kinase) exists as a hexamer composed of 'A' (encoded by NME1) and 'B' (encoded by NME2) isoforms. NME1 is involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. It also has tumor metastasis-suppressive capacity. NME1 has a key role in the synthesis of nucleoside triphosphates other than ATP. NME1 is essential for neural development including neural patterning and cell future determination.
The NME1 gene is expressed in various tumor types where its levels have been alternatively linked to reduced or increased metastatic potential.
Decrease in NME1 expression is notably connected to aggressive behavior in melanoma, breast, colon, and gastric carcinomas. In contrast, elevated levels of NME1 gene expression are noted in the advanced stage of thyroid carcinomas.
Somatic mutations of the NME1 gene are found in neuroblastoma. Increased NME1 in neuroblastoma is linked to features of the disease that are associated with aggressive tumors.

NME2 takes an important part in the synthesis of nucleoside triphosphates other than ATP. NME2 negatively controls Rho activity by interacting with AKAP13/LBC. NME2 acts as a transcriptional activator of the MYC gene. NME2 binds DNA non-specifically. NME2 is a heterodimeric enzyme functioning as a nucleoside diphosphate kinase. NME1 and NME2 contain 152 amino acids, A and B polypeptide chains of the NM23 enzyme, respectively. NME2 is identical to the beta subunit of human erythrocyte NDP kinase. NDP kinases participate in the synthesis of nucleoside triphosphates, and NM23 is involved in the regulation of signal transduction by complexing with G proteins, causing activation/inactivation of developmental pathways.

Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.

OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.

Bromodomain Containing 1 also known as BRD1 contains a bromodomain, which is a sequence motif frequently found in transcriptional coactivators, and localizes to the nucleus in testis and several other cell types. Variations in BRD1 are connected with schozophrenia & bipolar disorder.

Bromodomain Containing 3 (BRD3) was classified based on its homology to the gene encoding the RING3 protein, which is a serine/threonine kinase. The BRD3 protein localizes to 9q34, a region which contains a number of major histocompatibility complex (MHC) genes. The function of the BRD3 protein is unknown.