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Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling.

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FOXRED1 is a 486 amino acid single-pass membrane protein. Utilizing FAD as a cofactor, FOXRED1 may act as a chaperone protein essential for the function of mitochondrial complex I. Mutations to FOXRED1 may result in mitochondrial complex I deficiency (MT-C1D), which results in a wide range of clinical maladies from lethal neonatal disease to adult onset neurodegenerative disorders. Common phenotypes of MT-C1D include cardiomyopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. FOXRED1 exists as three alternatively spliced isoforms and is encoded by a gene mapping to human chromosome 11q24.2. With approximately 135 million base pairs and 1,400 genes, chromosome 11 makes up around 4% of human genomic DNA and is considered a gene and disease association dense chromosome.

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This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized. [provided by RefSeq, Jul 2008].

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Glial fibrillary acidic protein (GFAP) is a member of the class III intermediate filament protein family. It is heavily, and specifically, expressed in astrocytes and certain other astroglia in the central nervous system, in satellite cells in peripheral ganglia, and in non myelinating Schwann cells in peripheral nerves. In addition, neural stem cells frequently strongly express GFAP. to GFAP are therefore very useful as markers of astrocytic cells. In addition many types of brain tumor, presumably derived from astrocytic cells, heavily express GFAP. GFAP is also found in the lens epithelium, Kupffer cells of the liver, in some cells in salivary tumors and has been reported in erythrocytes.

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Heterotrimeric guanine nucleotide-binding proteins (G proteins) transduce extracellular signals received by transmembrane receptors to effector proteins. Transducin is a guanine nucleotide-binding protein found specifically in rod outer segments, where it mediates activation by rhodopsin of a cyclic GTP-specific (guanosine monophosphate) phosphodiesterase. Transducin is also referred to as GMPase. GNGT1 encodes the gamma subunit of transducin (Hurley et al., 1984 [PubMed 6438626]; Scherer et al., 1996 [PubMed 8661128]).[supplied by OMIM, Mar 2008].

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Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

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VAV2 is a ubiquitously expressed structural homolog of the VAV protooncogene that is expressed preferentially in hematopoetic cells. Both proteins are comprised of a Dbl homology (DH) domain with guanosine nucleotide exchange (GEF) activity exclusively directed towards Rho/Rac GTPases, a pleckstrin homology (PH) domain, a calponin-homology (CH) region, an acidic domain (AD) a zinc finger butterfly motif, two SH3 regions and one SH2 domain. GEF activity of RhoA family G proteins is induced by tyrosine phosphorylation in wild type VAV2, and is constitutively activated in N terminus deleted oncogene forms. Constitutive expression of a VAV2 oncoprotein may result in morphological alterations including highly enlarged cells in which karyokinesis and cytokinesis frequently are uncoupled.

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Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Interacts with MCC.

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The protein encoded by this gene is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This cytokine is a ligand for receptors TNFRSF13B/TACI, TNFRSF17/BCMA, and TNFRSF13C/BAFFR. This cytokine is expressed in B cell lineage cells, and acts as a potent B cell activator. It has been also shown to play an important role in the proliferation and differentiation of B cells. [provided by RefSeq].

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Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. In Saccharomyces cerevisiae, ubiquitin-like proteins include Rub1, Ula1, Uba3, Smt3, Ubc2, Ubc12 and Ubc9. Rub1 shares 53% homology with ubiquitin and requires activation via the E2 proteins, including Ula1, Uba3 and Ubc12 in order to conjugate to substrates directed to different proteolytic systems. Ubc4 catalyzes ubiquitination of IkBa in a phosphorylation and SCFB-TRCP dependent manner. In this particular reaction, E1 first transfers ubiquitin to the E2 component Ubc4, and Ubc4 then associates with E3 ligase, which conjugates the poly-ubiquitin chain on a target protein. In this fashion, the chain tags the IkBa for degradation by a proteasome thus lifting the inhibitory effect of IkBa on NFkB and allowing NFkB to enter the nucleus.

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This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and hydroxylates steroids at the 21 position. Its activity is required for the synthesis of steroid hormones including cortisol and aldosterone. Mutations in this gene cause congenital adrenal hyperplasia. A related pseudogene is located near this gene; gene conversion events involving the functional gene and the pseudogene are thought to account for many cases of steroid 21-hydroxylase deficiency. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].

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MAVS (Mitochondrial Antiviral Signaling) mediates the activation of NF-kappaB and IRF3 in response to antiviral infection. Silencing of MAVS expression permits derepression of viral replication, while over expression of MAVS boosts antiviral immunity.

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The gene encoding DYX1C1 maps in the 15q21 region, which is disrupted by a translocation t(2;15)(q11;q21) and segregates with dyslexia. Two sequence changes in DYX1C1, including one involving the translation initiation sequence and an Elk-1 transcription factor binding site (-3G -->A) and a codon (1249G -->T), introduce a premature stop codon and truncate the protein by 4 amino acids. DYX1C1 encodes a nuclear tetratricopeptide repeat domain protein that is dynamically regulated in brain. In human brain, DYX1C1 protein localizes to a fraction of cortical neurons and white matter glial cells. It is also expressed in lung, kidney and testis.

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DNA PK is the key component of the non-homologous end-joining (NHEJ) pathway of DSB repair in mammalian cells. DNA PK consists of a heterodimeric DNA-binding subunit (Ku70/80) and an approximately 465 kDa catalytic subunit (DNA PKcs). DNA PKcs is a serine/threonine protein kinase whose activity is greatly stimulated by its recruitment to DNA breaks by the Ku heterodimer.

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Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.

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This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008].

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SH2D3A

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Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.

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C1orf201

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Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes.

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Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling.

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Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

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The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein kinase is highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2. It is a catalytic subunit of the cyclin-dependent protein kinase complex, whose activity is restricted to the G1-S phase, and essential for cell cycle G1/S phase transition. This protein associates with and regulated by the regulatory subunits of the complex including cyclin A or E, CDK inhibitor p21Cip1 (CDKN1A) and p27Kip1 (CDKN1B). Its activity is also regulated by its protein phosphorylation. Two alternatively spliced variants and multiple transcription initiation sites of this gene have been reported. [provided by RefSeq, Jul 2008].

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Myosin is a protein which is known to interact with actin in muscle and non-muscle cells. It contains two identical heavy chains and four light chains. Myosin molecules consist of two major regions: tails (rods) and heads. They aggregate into filaments through the tail region and interact with actin and with ATP through the head region. Multiple forms of myosin heavy chains exist for each muscle type-skeletal, cardiac, smooth and non-muscle isomyosin forms exist in different types of skeletal muscle, depending on the physiological function of the muscle. They are designated at type I (slow twitch) and type II (fast twitch).

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C1orf191

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Gem belongs to the Rad/Gem/Kir (RGK) subfamily of Ras-related GTPases, which lack typical C-terminal amino acid motifs for isoprenylation. Rad and Gem bind calmodulin in a Ca2+-dependent manner via this C-terminal extension, involving residues 278–297 in human Rad. High intracellular Gem levels, which interact with intact microtubules and microfilaments, promote profound changes in cell morphology. Ectopic Gem expression is sufficient to stimulate cell flattening and neurite extension in N1E-115 and SH-SY5Y neuroblastoma cells, suggesting a role for Gem in cytoskeletal rearrangement and/or morphological differentiation of neurons. Gem was also observed in developing trigeminal nerve ganglia in 12.5 day mouse embryos, demonstrating that Gem expression is a property of normal ganglionic development. The interaction of Gem with beta-subunits regulates Ca2+ channel expression at the cell surface. The human Gem gene maps to chromosome 8q22.1.

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Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

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The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

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p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

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Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.