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FGD1
FYVE, RhoGEF and PH domain-containing protein 1 (FGD1) also known as faciogenital dysplasia 1 protein (FGDY), zinc finger FYVE domain-containing protein 3 (ZFYVE3), or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF) is a protein that in humans is encoded by the ''FGD1'' gene that lies on the X chromosome. Orthologs of the ''FGD1'' gene are found in dog, cow, mouse, rat, and zebrafish, and also budding yeast and ''C. elegans ''Caenorhabditis elegans'' () is a free-living transparent nematode about 1 mm in length that lives in temperate soil environments. It is the type species of its genus. The name is a blend of the Greek ''caeno-'' (recent), ''rhabditis'' ( ...''. It is a member of the FYVE, RhoGEF and PH domain containing family. FGD1 is a guanine-nucleotide exchange factor (GEF) that can activate the Rho GTPase Cdc42. It localizes preferentially to the trans-Golgi network (TGN) of mammalian cells and regulates, for example, the secretory transpo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FYVE, RhoGEF And PH Domain Containing
FYVE, RhoGEF and PH domain containing (FGD) is a gene family consisting of: * FGD1 FYVE, RhoGEF and PH domain-containing protein 1 (FGD1) also known as faciogenital dysplasia 1 protein (FGDY), zinc finger FYVE domain-containing protein 3 (ZFYVE3), or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF) is a protein th ... * FGD2 * FGD3 * FGD4 Type 1 is associated with Aarskog-Scott syndrome. See also * Guanine nucleotide exchange factor References External links * * Gene families {{GTP-binding protein regulators ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RhoGEF Domain
RhoGEF domain describes two distinct structural domains with guanine nucleotide exchange factor (GEF) activity to regulate small GTPases in the Rho family. Rho small GTPases are inactive when bound to GDP but active when bound to GTP; RhoGEF domains in proteins are able to promote GDP release and GTP binding to activate specific Rho family members, including RhoA, Rac1 and Cdc42. The largest class of RhoGEFs is composed of proteins containing the " Dbl-homology" (DH) domain, which almost always is found together with a pleckstrin-homology (PH) domain to form a combined DH/PH domain structure. A distinct class of RhoGEFs is those proteins containing the DOCK/CZH/DHR-2 domain. This structure has no sequence similarity with DBL-homology domains. Human proteins containing DH/PH RhoGEF domain ABR; AKAP13/ARHGEF13/Lbc; ALS2; ALS2CL; ARHGEF1/p115-RhoGEF; ARHGEF10; ARHGEF10L; ARHGEF11/PDZ-RhoGEF.; ARHGEF12/LARG; ARHGEF15; ARHGEF16; ARHGEF17; ARHGEF18; ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FYVE Domain
In molecular biology the FYVE zinc finger domain is named after the four cysteine-rich proteins: Fab 1 (yeast orthologue of PIKfyve), YOTB, Vac 1 (vesicle transport protein), and EEA1, in which it has been found. FYVE domains bind phosphatidylinositol 3-phosphate, in a way dependent on its metal ion coordination and basic amino acids. The FYVE domain inserts into cell membranes in a pH-dependent manner. The FYVE domain has been connected to vacuolar protein sorting and endosome function. Structure The FYVE domain is composed of two small beta hairpins (or zinc knuckles) followed by an alpha helix. The FYVE finger binds two zinc ions. The FYVE finger has eight potential zinc coordinating cysteine positions and is characterized by having basic amino acids around the cysteines. Many members of this family also include two histidines in a sequence motif: The FYVE finger is structurally similar to the RING domain and the PHD finger. Examples The following is a list of human prote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cortactin
Cortactin (from "''cortical actin'' binding protein") is a monomeric protein located in the cytoplasm of cells that can be activated by external stimuli to promote polymerization and rearrangement of the actin cytoskeleton, especially the actin cortex around the cellular periphery. It is present in all cell types. When activated, it will recruit Arp2/3 complex proteins to existing actin microfilaments, facilitating and stabilizing nucleation sites for actin branching. Cortactin is important in promoting lamellipodia formation, invadopodia formation, cell migration, and endocytosis. Gene In humans, cortactin is encoded by the ''CTTN'' gene on chromosome 11. Structure Cortactin is a thin, elongated monomer that consists of an amino-terminal acidic (NTA) region; 37-residue-long segments that are highly conserved among cortactin proteins of all species and repeated up to 6.5 times in tandem (“cortactin repeats”); a proline-rich region; and an SH3 domain. This basic structure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphatidylinositol 3-phosphate
Phosphatidylinositol 3-phosphate (PtdIns3''P'') is a phospholipid found in cell membranes that helps to recruit a range of proteins, many of which are involved in protein trafficking, to the membranes. It is the product of both the class II and III phosphoinositide 3-kinases (PI 3-kinases) activity on phosphatidylinositol. PtdIns3''P'' is dephosphorylated by the myotubularin family of phosphatases, on the D3 position of the inositol ring, and can be converted to PtdIns(3,5)''P''2 by the lipid kinase PIKfyve. Both FYVE domains and PX domains – found in proteins such as SNX1, HGS, and EEA1 – bind to PtdIns3''P''. The majority of PtdIns3''P'' appears to be constitutively synthesised by the class III PI 3-kinase, PIK3C3 (Vps34), at endocytic membranes. Class II PI 3-kinases also appear to synthesise PtdIns3''P'', their activity however appears to be regulated by a range of stimuli, including growth factors. This suggests that specific pools of PtdIns3''P'' may be s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PH Domain
In chemistry, pH (), historically denoting "potential of hydrogen" (or "power of hydrogen"), is a scale used to specify the acidity or basicity of an aqueous solution. Acidic solutions (solutions with higher concentrations of ions) are measured to have lower pH values than basic or alkaline solutions. The pH scale is logarithmic and inversely indicates the concentration of hydrogen ions in the solution.Bates, Roger G. ''Determination of pH: theory and practice''. Wiley, 1973. :\ce = - \log(a_\ce) = -\log( ce\ce M) where M = mol dm−3. At 25 °C (77 °F), solutions with a pH less than 7 are acidic, and solutions with a pH greater than 7 are basic. Solutions with a pH of 7 at this temperature are neutral (i.e. have the same concentration of H+ ions as OH− ions, i.e. pure water). The neutral value of the pH depends on the temperaturebeing lower than 7 if the temperature increases above 25 °C. The pH value can be less than 0 for very concentrated strong acids, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
