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PSMD9 is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. PSMD9 acts as a chaperone through the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex compilation, PSMD9 is part of an intermediate PSMD9:PSMC6:PSMC3 module, also called modulator trimer complex. PSMD9 is released during the further base assembly process.

Protein tyrosine phosphatase type IVA 1 (PTP4A1) is a cell signaling molecule that has regulatory roles in a variety of cellular processes. PTP4A1 is a unique nuclear PTP which is induced in regenerating liver and mitogen stimulated cells. PTP4A1 is primarily expressed in the spleen, bone marrow, thymus, lymph nodes, T lymphocytes and tonsil and is overexpressed in tumor cell lines.

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 kinases such 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 Ras GTP-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 knockout mice lacking MAPK1 have major defe

Mediator complex subunit 4 (MED4) is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. MED4 is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is able to activate nuclear receptors in a ligand-dependent manner. MED4 functions as a link to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. MED4 is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.

Zinc Finger HIT-Type Containing 3 (ZNHIT3) which contains one HIT-type zinc finger, requires the presence of thyroid hormone for its interaction. Thyroid receptor interacting proteins particularly interact with the ligand binding domain of the thyroid receptor (TR).

Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.

BCDIN3D is a member of the methyltransferase superfamily and contains 1 Bin3-type SAM domain. BCDIN3D acts in the catalysis of the transfer of a methyl group to an acceptor molecule. BCDIN3D is an O-methyltransferase which specifically dimethylates the 5' monophosphate of pre-miRNAs, serving as a negative regulator of miRNA processing. BCDIN3D mediates the methylation of pre-miR-145, as well as other pre-miRNAs.

STMN3 is a neuronal specific protein which belongs to the stathmin/oncoprotein 18 family of microtubule-destabilizing phosphoproteins. It is similar to the SCG10 protein and is involved in signal transduction and regulation of microtubule dynamics.

Family With Sequence Similarity 19 Member-A5 (FAM19A5) belongs to the TAFA family which is comprised of 5 highly homologous genes encoding small secreted proteins. These proteins have conserved cysteine residues at fixed positions, and are remotely related to MIP-1alpha, which is a member of the CC-chemokine family. The TAFA proteins are primarily expressed in specific regions of the brain, and are assumed to serve as brain-specific chemokines or neurokines which act as regulators of immune and nervous cells.

Transcription elongation factor A protein-like 8 (TCEAL8) is a member of the TFS-II family and TFA subfamily. TCEAL8 is involved in transcriptional regulation and localized in nucleus. TFS-II family members contain TFA domains and act as nuclear phosphoproteins which control transcription in a promoter context-dependent mode. Numerous family members are found on the X chromosome.

TEN1 is part of a complex that binds to single-stranded DNA and is necessary in order to protect telomeres from DNA degradation (CST complex). The CST complex binds single-stranded DNA with high affinity in a sequence-independent mode, while isolated subunits bind DNA with low affinity by themselves. Further to telomere protection, the CST complex has most likely a more general part in DNA metabolism at non-telomeric sites.

HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.

Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.

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.

TCEA1 is a member of the TFS-II family. TCEA1 binds to Pol II and operates to cleave the emerging transcript, thus unlocking the complex and permitting transcription to continue. TCEA1 is localized to the nucleus and holds three independently-folding domains that are essential for accurate binding to Pol II. The arresting sites in are able to trap a certain segment of elongating RNA polymerases that goes through, causing in a locked ternary complex. Cleavage of the emerging transcript by S-II enables the renewal of elongation from the new 3'-terminus.

TCEB1 (elongin C) is a subunit of elongin, which is a common transcription elongation factor that increases the RNA polymerase II transcription elongation past template encoded arresting sites. The SIII complex is comprised of elongins A/A2, B and C. The SIII complex activates elongation by RNA polymerase II by curbing transient pausing of the polymerase at numerous sites within transcription units. Elongin A acts as the transcriptionally active component of the SIII complex, while elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and able to forming a stable complex with elongins B and C. The VHL (von Hippel-Lindau) tumor suppressor protein binds to elongins B and C, and thus inhibits transcription elongation.

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.

Lysyl-tRNA synthetase (KARS) is a member of the class-II aminoacyl-tRNA synthetase family. KARS exists as both mitochondrial and cytoplasmic isoforms produced by alternative splicing, and believed to have a role in autoimmune diseases, such as polymyositis or dermatomyositis. The KARS protein functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids, so linking amino acids with tRNA-contained nucleotide triplets.

PMP2 is a small protein found in peripheral nerve myelin and spinal cord myelin, belongs to a family of fatty acid binding proteins. PMP2 partly decreases the inhibitory effect of T suppressors in the culture of immune lymph node cells. PMP2 protein is a lipid transport protein in schwann cells.

TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.