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Description:
Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis. GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. Oxyntomodulin significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness. Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life.
Description:
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008].
Description:
Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p19RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p19RhoGAP, which promotes association with RASA1/p12RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways. Isoform 2 inhibits PTK6 phosphorylation and PTK6 association with other tyrosine-phosphorylated proteins.
Description:
Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, TOMM2, USP3, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognised by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by the ubiquitination of mitochondrial proteins such as TOMM2, RHOT1/MIRO1 and USP3 (PubMed:24896179). Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.
Description:
Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors. Each of a very broad range of receptors specifically detects an extracellular stimulus (i.e. a photon, pheromone, odorant, hormone or neurotransmitter), while the effectors (e.g. adenyl cyclase), which act to generate one or more intracellular messengers, are less numerous. In mammals, G protein Alpha, Beta and Gamma polypeptides are encoded by at least 16, 4 and 7 genes, respectively. Most interest in G proteins has been focused on their a subunits, since these proteins bind and hydrolyze GTP and most obviously regulate the activity of the best studied effectors. Evidence, however, has established an important regulatory role for the Beta subunits. It is becoming increasingly clear that different G protein complexes expressed in different tissues carry structurally distinct members of the Gamma as well as the Alpha and Beta subunits, and that preferential associations between members of subunit families increase G protein functional diversity.
Description:
Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors. Each of a very broad range of receptors specifically detects an extracellular stimulus (i.e. a photon, pheromone, odorant, hormone or neurotransmitter), while the effectors (e.g. adenyl cyclase), which act to generate one or more intracellular messengers, are less numerous. In mammals, G protein Alpha, Beta and Gamma polypeptides are encoded by at least 16, 4 and 7 genes, respectively. Most interest in G proteins has been focused on their a subunits, since these proteins bind and hydrolyze GTP and most obviously regulate the activity of the best studied effectors. Evidence, however, has established an important regulatory role for the Beta subunits. It is becoming increasingly clear that different G protein complexes expressed in different tissues carry structurally distinct members of the Gamma as well as the Alpha and Beta subunits, and that preferential associations between members of subunit families increase G protein functional diversity.
Description:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. G gamma4 interacts with beta-1 and beta-2, but not with beta-3. It is expressed in brain, kidney, pancreas, skeletal muscle and faintly in cardiac muscle.
Description:
Gene amplification is associated with tumor stage and progression in human gliomas. Several amplified loci are identified and comprise multiple genes. The glioma amplified sequence 41 (GAS41) is an evolutionarily conserved eukaryotic protein found in diverse species. GAS41 is related to the AF-9 and ENL proteins, which are putative transcription factors in some acute leukemias, and interacts with a component of the nuclear matrix, NuMA, in interphase cells. GAS41 has a dotted staining pattern in interphase nuclei and a uniform distribution in mitotic cells. GAS41 is ubiquitously expressed, with the highest levels of expression in human brain. In neuroblastoma, GAS41 is located in the nucleoli, but not in the nucleoplasm. GAS41 also binds to the MLL fusion partner AF10, which is involved in two distinct chromosomal translocations associated with hematologic malignancy. In addition, GAS41 interacts with INI1 (Integrase Interactor), which is a human homologue of the yeast SNF5 protein, a component of the SWI/SNF complex. The GAS41 gene maps to human chromosome 12q13-q15.
Description:
Integrins are heterodimeric cell surface receptors composed of alpha and beta subunits, which mediate cell-cell and cell-extracellular matrix attachments. Aberrant integrin expression has been found in many epithelial tumours. Changes in integrin expression have been shown to be important for the growth and early metastatic capacity of melanoma cells. Integrin alpha-v beta-6 is upregulated in cancers and during tissue remodelling but is absent from resting adult tissues. Integrin alpha-v beta-6 promotes invasion and correlates with poor survival and therefore makes a promising therapeutic target.
Description:
Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodelling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression.
Description:
TRA16 may act as a repressor of NR2C2-mediated transactivation by suppressing the binding between NR2C2/TR4 and the TR4-response element in target genes.
Description:
GALE is a 348 amino acid protein that functions as the third enzyme in the Leloir pathway of galactose metabolism. A member of the sugar epimerase family, GALE exists as a homodimer, binds FAD as a cofactor and catalyzes the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine and UDP-glucose to UDP-galactose. The gene encoding GALE maps to human chromosome 1p36.11 and mutations in this gene lead to the development of complex disorder known as epimerase-deficiency galactosemia (EDG) or galactosemia type 3, which is characterized by mental retardation, liver damage, cataracts and deafness.
Description:
The gamma-Tubulin complex is composed of gamma Tubulin and the gamma-Tubulin complex-associated proteins GCP2, GCP3, GCP4, GCP5 and GCP6, all of which are essential components of microtubule organizing centers. gamma-Tubulin complex components are localized to both the centrosome, where they are involved in microtubule nucleation, and to the cytoplasm, where they exist as soluble complexes that can be recruited to the centrosome as needed. Although the GCP proteins are related, they have distinct roles which contribute to the proper function of the gamma-Tubulin complex. GCP4 (gamma-tubulin complex component 4), also known as TUBGCP4, is a ubiquitously expressed 667 amino acid member of the gamma-Tubulin complex that localizes to the metaphase spindle during mitosis. In response to proteosome inhibition, GCP4 exhibits increased accumulation at the pericentiolar material where it participates in microtubule organization and nucleation.
Description:
This gene encodes one of several forms of glutamic acid decarboxylase, identified as a major autoantigen in insulin-dependent diabetes. The enzyme encoded is responsible for catalyzing the production of gamma aminobutyric acid from L glutamic acid. A pathogenic role for this enzyme has been identified in the human pancreas since it has been identified as an autoantibody and an autoreactive T cell target in insulin dependent diabetes. This gene may also play a role in the stiff man syndrome.
Description:
G protein-coupled receptors (GPRs), also known as seven transmembrane receptors, heptahelical receptors or 7TM receptors, comprise a superfamily of proteins that play a role in many different stimulus-response pathways. G protein coupled receptors translate extracellular signals into intracellular signals (G protein activation) and they respond to a variety of signaling molecules, such as hormones and neurotransmitters. GPR101 (G protein-coupled receptor 101), also known as GPCR6, is a 508 amino acid multi-pass membrane protein that belongs to the G-protein coupled receptor 1 family. GPR101 functions as an orphan receptor that is thought to play a role in signaling events throughout the cell. Expressed predominantly in brain, GPR101 participates in a wide range of activities in the CNS via modulation of cAMP levels.
Description:
CABLES2 is a proapoptotic factor involved in both p53-mediated and p53-independent apoptotic pathways. ik3-1/CABLES1, a closely related molecule, has been identified to be a candidate tumor suppressor for colon and head/neck cancers.The exact function of this protein is unknown, but it is probably involved in G1-S cell cycle transition. CABLES2 binds to CDK3, CDK5 and ABL1.
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