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The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC58 (coiled-coil domain containing 58) is a 144 amino acid protein that is encoded by a gene that maps to human chromosome 3q21.1. Chromosome 3 is made up of about 214 million bases encoding over 1,100 genes. Notably, there is a chemokine receptor gene cluster and a variety of human cancer related loci on chromosome 3. Particular regions of the chromosome 3 short arm are deleted in many types of cancer cells. Key tumor suppressing genes on chromosome 3 encode apoptosis mediator RASSF1, cell migration regulator HYAL1 and angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth Disease are a few of the numerous genetic diseases associated with chromosome 3.

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Tom1L-1 is a 476 amino acid Golgi apparatus protein belonging to the TOM1 family and is a member of the multivesicular body (MVB) sorting machinery. Containing a GAT domain and a VHS domain, Tom1L-1 interacts with Fyn, GRB2, PI 3-kinase p85?and various signaling proteins when phosphorylated. GAT domain of Tom1L1 binds ubiquitin, suggesting participation in the sorting of ubiquitinated proteins into MVBs. Tom1L-1 may act as an adapter protein involved in signaling pathways and may promote Fyn activation, possibly by disrupting intramolecular SH3-dependent interactions. As an interactor and a substrate of Src tyrosine kinases (SFK), Tom1L1 is considered a novel mechanism involved in negative regulation of SFK mitogenic and transforming signals. Tom1L1 modulates SFK partitioning at the plasma membrane and downregulates Src kinases in an endosomal-dependent manner. It is suggested that Tom1L-1 functions as an anti-oncogene by inhibiting the formation of squamous cell carcinomas in skin.

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Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.

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Receptor for SEMA4D. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration.

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Cytokeratins, a group comprising at least 29 different proteins, are characteristic of epithelial and trichocytic cells. Cytokeratins 1, 4, 5, 6, and 8 are members of the type II neutral to basic subfamily. Antibody to cytokeratins are specific markers of epithelial cell differentiation and have been widely used as tools in tumor identification and classification. Anti Pan Cytokeratin (mixture) is a broadly reactive reagent, which recognizes epitopes present in most human epithelial tissues. It facilitates typing of normal, metaplastic and neoplastic cells. Synergy between the various components results in staining amplification. This enables identification of cells, which would otherwise be stained only marginally. The mixture may aid in the discrimination of carcinomas and nonepithelial tumors such as sarcomas, lymphomas and neural tumors. It is also useful in detecting micrometastases in lymph nodes, bone marrow and other tissues and for determining the origin of poorly differentiated tumors. There are two types of cytokeratins the acidic type I cytokeratins and the basic or neutral type II cytokeratins. Cytokeratins are usually found in pairs comprising a type I cytokeratin and a type II cytokeratin. Usually the type II cytokeratins are 8kD larger than their type I counterparts.

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EPDR1 is a type II transmembrane protein and is similar to two families of cell adhesion molecules, the protocadherins and ependymins. It may play a role in calcium dependent cell adhesion. There are two named isoforms.

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C1orf77, also known as Friend of PRMT1 protein, is a 248 amino acid protein that plays an essential role in the ligand-dependent activation of estrogen receptor target genes. C1orf77 is tightly associated with chromatin and is modified by both asymmetric and symmetric arginine methylation. Depletion of C1orf77 results in almost complete block of estradiol-induced promter occupancy by the estrogen receptor. Also, complete knockdown of C1orf77 mRNA in adult erythroid progenitors stongly induces fetal hemoglobin, suggesting that C1orf77 is a critical modulator of _-globin gene expression. There are two isoforms of C1orf77 that are produced as a result of alternative splicing events. The gene encoding C1orf77 maps to human chromosome 1, the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1.

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The protein encoded by this gene is a serine/threonine kinase that regulates cytokinesis, smooth muscle contraction, the formation of actin stress fibres and focal adhesions, and the activation of the c-fos serum response element. This protein, which is an isozyme of ROCK1 is a target for the small GTPase Rho.

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GMEB-2 is a DNA-binding protein that plays a crucial role modulating transcription upon activation by steroid hormones. GMEB-2 is ubiquitously expressed with preferential expression in developmentally important tissues, such as testis, bone marrow, placenta and fetal tissues. It localizes to the nucleus and cytoplasm and contains a SAND domain near its N-terminus and a C-terminal coiled coil structure. GMEB-2 functions as a homodimer or as a heterodimer with GMEB-1. The formed complex specifically binds to glucocorticoid modulatory elements (GME) in the promoter region of target genes and recruits the histone acetylase CREB binding protein (CBP) during glucocorticoid signaling. This acts to increase sensitivity to low concentrations of glucocorticoids. In addition, GMEB-2 functions as an auxiliary factor required for parvovirus replication.

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Smad3 is a 50 kDa member of a family of proteins that act as key mediators of TGF beta superfamily signaling in cell proliferation, differentiation and development. The Smad family is divided into three subclasses: receptor regulated Smads, activin/TGF beta receptor regulated (Smad2 and 3) or BMP receptor regulated (Smad 1, 5, and 8); the common partner, (Smad4) that functions via its interaction to the various Smads; and the inhibitory Smads, (Smad6 and 7). Activated Smad3 oligomerizes with Smad4 upon TGF beta stimulation and translocates as a complex into the nucleus, allowing its binding to DNA and transcription factors. Phosphorylation of the two TGF beta dependent serines 423 and 425 in the C terminus of Smad3 is critical for Smad3 transcriptional activity and TGF beta signaling.

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GMEB-1 is a 573 amino acid protein that contains one SAND domain and is a member of the KDWK family of combinatorial transcription modulators. Localized to both the cytoplasm and the nucleus, GMEB-1 forms a heterodimer with GMEB-2 (Glucocorticoid modulatory element-binding protein 2) and, once associated with GMEB-2, plays a key role in parvovirus DNA replication. In addition, GMEB-1 functions alone as a trans-acting factor that, by binding to glucocorticoid modulatory elements (GMEs) in TAT (tyrosine aminotransferase) promoters, increases intracellular sensitivity to glucocorticoid concentrations. GMEB-1 also interacts with initiator procaspases and, via this interaction, can inhibit caspase-induced apoptosis. Due to alternative splicing events, GMEB-1 is expressed as two isoforms.

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Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments (PubMed:18039658). Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation (PubMed:18799458, PubMed:17461796, PubMed:18197702, PubMed:22074827). Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway (PubMed:18660751). Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways.

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Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.

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Smad3 is a 50 kDa member of a family of proteins that act as key mediators of TGF beta superfamily signaling in cell proliferation, differentiation and development. The Smad family is divided into three subclasses: receptor regulated Smads, activin/TGF beta receptor regulated (Smad2 and 3) or BMP receptor regulated (Smad 1, 5, and 8); the common partner, (Smad4) that functions via its interaction to the various Smads; and the inhibitory Smads, (Smad6 and 7). Activated Smad3 oligomerizes with Smad4 upon TGF beta stimulation and translocates as a complex into the nucleus, allowing its binding to DNA and transcription factors. Phosphorylation of the two TGF beta dependent serines 423 and 425 in the C terminus of Smad3 is critical for Smad3 transcriptional activity and TGF beta signaling.

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Neurofibromin is a product of the tumor suppressor gene, Neurofibromatosis type I. Neurofibromin is known to have GTPase activity that modulates the ras pathway. The absence of or alteration of the neurofibromin protein may lead to Neurofibromatosis disease. This protein has not been purified, therefore, most of the information regarding this protein has been deduced from homology analysis of its gene sequence.

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S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene.

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S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene.

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Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin (By similarity).

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TUSC3 belongs to the OST3/OST6 family of proteins and may be involved in N-glycosylation through its association with N-oligosaccharyl transferase. The TUSC3 gene is a candidate tumour supressor.

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SMYD3 is a gene that is over-expressed in the majority of colorectal carcinomas and hepatocellular carcinomas. SMYD3 forms a complex with RNA polymerase II through an interaction with the RNA helicase HELZ and transactivates a set of genes that included oncogenes, homeobox genes and genes associated with cell-cycle regulation. SMYD3 binds to a motif, 5'-CCCTCC-3', present in the promoter region of downstream genes such as Nkx2.8. The SET domain of SMYD3 shows histone H3-lysine 4 (H3-K4)-specific methyltransferase activity, which is enhanced in the presence of the heat-shock protein HSP90A.

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RORET, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is a 465 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Found in all eukaryotes, members of the RBCC family typically function within a larger protein complex and possess ubiquitin-protein isopeptide ligase activity.The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The function of this protein has not been identified.

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Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription.

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This gene encodes a member of the p53 family of transcription factors involved in cellular responses to stress and development. It maps to a region on chromosome 1p36 that is frequently deleted in neuroblastoma and other tumors, and thought to contain multiple tumor suppressor genes. The demonstration that this gene is monoallelically expressed (likely from the maternal allele), supports the notion that it is a candidate gene for neuroblastoma. Many transcript variants resulting from alternative splicing and/or use of alternate promoters have been found for this gene, but the biological validity and the full-length nature of some variants have not been determined. [provided by RefSeq, Feb 2011].

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Receptor for thyrothropin. Plays a central role in controlling thyroid cell metabolism. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Also acts as a receptor for thyrostimulin (GPA2+GPB5).

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This gene encodes a member of the dishevelled (dsh) protein family. The vertebrate dsh proteins have approximately 40% amino acid sequence similarity with Drosophila dsh. This gene encodes a 90-kD protein that undergoes posttranslational phosphorylation to form a 95-kD cytoplasmic protein, which may play a role in the signal transduction pathway mediated by multiple Wnt proteins. The mechanisms of dishevelled function in Wnt signaling are likely to be conserved among metazoans. [provided by RefSeq, Jul 2008].

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Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.

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The catenins are ubiquitously expressed, cytoplasmic proteins that associate with E-cadherin at cellular junctions. Catenin/cadherin complexes play an important role in mediating cellular adhesion. alpha T-catenin, also referred to as VR22, is a 895-amino acid protein that is most abundantally expressed in cardiomyocytes and in the peritubular myoid cells of the testis. alpha T-catenin binds to alpha E-catenin as well as to beta-catenin, and it functions to inhibit Wnt signaling. CTNNA3, the gene that encodes for alpha-T-catenin, is located on chromosome 10, and mutations in this gene show a strong correlation to late-onset Alzheimer's disease (LOAD) as well as to dilated cardiomyopathy.

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In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Sequence similarities Belongs to the heat shock protein 70 family.

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PDK1 (3 Phosphoinositide Dependent Protein Kinase 1) phosphorylates AGC kinases. PDK1 activates conventional PKC and PKC zeta through phosphorylation of critical threonine residues in the activation loop. PDK1 also phosphorylates Protein Kinase B (PKB) at threonine 308 in the presence of phosphatidylinositol-3,4,5-trisphosphate. Active Akt inactivates Glycogen Synthase Kinase 3 (GSK3), eventually leading to the dephosphorylation and activation of glycogen synthase and the stimulation of glycogen synthesis. Because of the role that PDK plays in insulin-induced glycogen synthesis and PKC activation it is a potentially important target for metabolic drug research. There are three named isoforms.

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CaMKI gamma is a Calcium/calmodulin-dependent protein kinase which belongs to a proposed calcium-triggered signaling cascade. In vitro it phosphorylates transcription factor CREB1. It has been proposed that CaMKI gamma is involved in dendritic outgrowth mediated by CaM-dependant protein kinase kinase.